UniProt functional annotation for P35555



	UniProt functional annotation for P35555

UniProt code: P35555.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). {ECO:0000250|UniProtKB:Q61554, ECO:0000269|PubMed:11461921, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15062093, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:1860873, ECO:0000269|PubMed:24039232, ECO:0000303|PubMed:27026396}.

Function: [Asprosin]: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. {ECO:0000269|PubMed:27087445}.

Subunit: [Fibrillin-1]: Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C- terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Interacts (via N-terminal domain) with EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (PubMed:17255108, PubMed:19349279, PubMed:19570982). {ECO:0000250|UniProtKB:Q61554, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15062093, ECO:0000269|PubMed:15131124, ECO:0000269|PubMed:15165854, ECO:0000269|PubMed:15790312, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17255108, ECO:0000269|PubMed:17293099, ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:19349279, ECO:0000269|PubMed:19570982, ECO:0000269|PubMed:21402694, ECO:0000269|PubMed:23010571, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26601954}.

Subcellular location: Secreted {ECO:0000269|PubMed:24982166}. Note=Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). {ECO:0000269|PubMed:24982166}.

Subcellular location: [Asprosin]: Secreted {ECO:0000269|PubMed:27087445}. Note=Secreted into the plasma. {ECO:0000269|PubMed:27087445}.

Subcellular location: [Fibrillin-1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11461921, ECO:0000269|PubMed:24982166}.

Ptm: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). {ECO:0000269|PubMed:10636927, ECO:0000269|PubMed:24982166, ECO:0000303|PubMed:27026396}.

Ptm: [Fibrillin-1]: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. {ECO:0000269|PubMed:9362480}.

Disease: Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life. {ECO:0000269|PubMed:10425041, ECO:0000269|PubMed:10441597, ECO:0000269|PubMed:10694921, ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12161601, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:12402346, ECO:0000269|PubMed:1301946, ECO:0000269|PubMed:14695540, ECO:0000269|PubMed:15161917, ECO:0000269|PubMed:15221638, ECO:0000269|PubMed:1569206, ECO:0000269|PubMed:16220557, ECO:0000269|PubMed:16222657, ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:18435798, ECO:0000269|PubMed:1852208, ECO:0000269|PubMed:19533785, ECO:0000269|PubMed:19941982, ECO:0000269|PubMed:20803651, ECO:0000269|PubMed:21542060, ECO:0000269|PubMed:22772377, ECO:0000269|PubMed:7611299, ECO:0000269|PubMed:7738200, ECO:0000269|PubMed:7762551, ECO:0000269|PubMed:7870075, ECO:0000269|PubMed:7951214, ECO:0000269|PubMed:7977366, ECO:0000269|PubMed:8004112, ECO:0000269|PubMed:8040326, ECO:0000269|PubMed:8071963, ECO:0000269|PubMed:8136837, ECO:0000269|PubMed:8281141, ECO:0000269|PubMed:8406497, ECO:0000269|PubMed:8504310, ECO:0000269|PubMed:8863159, ECO:0000269|PubMed:8882780, ECO:0000269|PubMed:9016526, ECO:0000269|PubMed:9254848, ECO:0000269|PubMed:9338581, ECO:0000269|PubMed:9401003, ECO:0000269|PubMed:9452085, ECO:0000269|PubMed:9837823, ECO:0000269|Ref.70}. Note=The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini.

Disease: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1) [MIM:129600]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. {ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:8188302}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:12525539}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Overlap connective tissue disease (OCTD) [MIM:604308]: Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable. {ECO:0000269|PubMed:2739055}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness. {ECO:0000269|PubMed:20375004}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: [Asprosin]: Marfanoid-progeroid-lipodystrophy syndrome (MFLS) [MIM:616914]: An autosomal dominant syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome. Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly. Mental and motor development are within normal limits. {ECO:0000269|PubMed:20979188, ECO:0000269|PubMed:21594992, ECO:0000269|PubMed:21594993, ECO:0000269|PubMed:24039054, ECO:0000269|PubMed:24613577, ECO:0000269|PubMed:24665001, ECO:0000269|PubMed:26860060, ECO:0000269|PubMed:27087445}. Note=The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous: [Asprosin]: Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. {ECO:0000303|PubMed:27087445}.

Similarity: Belongs to the fibrillin family. {ECO:0000305}.

Sequence caution: Sequence=CAA45118.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		[Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). {ECO:0000250\|UniProtKB:Q61554, ECO:0000269\|PubMed:11461921, ECO:0000269\|PubMed:12807887, ECO:0000269\|PubMed:15062093, ECO:0000269\|PubMed:17158881, ECO:0000269\|PubMed:1860873, ECO:0000269\|PubMed:24039232, ECO:0000303\|PubMed:27026396}.



Function:		[Asprosin]: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. {ECO:0000269\|PubMed:27087445}.


Subunit:		[Fibrillin-1]: Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C- terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Interacts (via N-terminal domain) with EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (PubMed:17255108, PubMed:19349279, PubMed:19570982). {ECO:0000250\|UniProtKB:Q61554, ECO:0000269\|PubMed:12807887, ECO:0000269\|PubMed:15062093, ECO:0000269\|PubMed:15131124, ECO:0000269\|PubMed:15165854, ECO:0000269\|PubMed:15790312, ECO:0000269\|PubMed:17158881, ECO:0000269\|PubMed:17255108, ECO:0000269\|PubMed:17293099, ECO:0000269\|PubMed:18339631, ECO:0000269\|PubMed:19349279, ECO:0000269\|PubMed:19570982, ECO:0000269\|PubMed:21402694, ECO:0000269\|PubMed:23010571, ECO:0000269\|PubMed:24039232, ECO:0000269\|PubMed:26601954}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:24982166}. Note=Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). {ECO:0000269\|PubMed:24982166}.
Subcellular location:		[Asprosin]: Secreted {ECO:0000269\|PubMed:27087445}. Note=Secreted into the plasma. {ECO:0000269\|PubMed:27087445}.
Subcellular location:		[Fibrillin-1]: Secreted, extracellular space, extracellular matrix {ECO:0000269\|PubMed:11461921, ECO:0000269\|PubMed:24982166}.
Ptm:		Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). {ECO:0000269\|PubMed:10636927, ECO:0000269\|PubMed:24982166, ECO:0000303\|PubMed:27026396}.
Ptm:		[Fibrillin-1]: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. {ECO:0000269\|PubMed:9362480}.
Disease:		Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life. {ECO:0000269\|PubMed:10425041, ECO:0000269\|PubMed:10441597, ECO:0000269\|PubMed:10694921, ECO:0000269\|PubMed:11700157, ECO:0000269\|PubMed:11826022, ECO:0000269\|PubMed:12161601, ECO:0000269\|PubMed:12203992, ECO:0000269\|PubMed:12402346, ECO:0000269\|PubMed:1301946, ECO:0000269\|PubMed:14695540, ECO:0000269\|PubMed:15161917, ECO:0000269\|PubMed:15221638, ECO:0000269\|PubMed:1569206, ECO:0000269\|PubMed:16220557, ECO:0000269\|PubMed:16222657, ECO:0000269\|PubMed:17657824, ECO:0000269\|PubMed:18435798, ECO:0000269\|PubMed:1852208, ECO:0000269\|PubMed:19533785, ECO:0000269\|PubMed:19941982, ECO:0000269\|PubMed:20803651, ECO:0000269\|PubMed:21542060, ECO:0000269\|PubMed:22772377, ECO:0000269\|PubMed:7611299, ECO:0000269\|PubMed:7738200, ECO:0000269\|PubMed:7762551, ECO:0000269\|PubMed:7870075, ECO:0000269\|PubMed:7951214, ECO:0000269\|PubMed:7977366, ECO:0000269\|PubMed:8004112, ECO:0000269\|PubMed:8040326, ECO:0000269\|PubMed:8071963, ECO:0000269\|PubMed:8136837, ECO:0000269\|PubMed:8281141, ECO:0000269\|PubMed:8406497, ECO:0000269\|PubMed:8504310, ECO:0000269\|PubMed:8863159, ECO:0000269\|PubMed:8882780, ECO:0000269\|PubMed:9016526, ECO:0000269\|PubMed:9254848, ECO:0000269\|PubMed:9338581, ECO:0000269\|PubMed:9401003, ECO:0000269\|PubMed:9452085, ECO:0000269\|PubMed:9837823, ECO:0000269\|Ref.70}. Note=The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini.
Disease:		Ectopia lentis 1, isolated, autosomal dominant (ECTOL1) [MIM:129600]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. {ECO:0000269\|PubMed:11700157, ECO:0000269\|PubMed:11826022, ECO:0000269\|PubMed:12203992, ECO:0000269\|PubMed:17657824, ECO:0000269\|PubMed:8188302}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269\|PubMed:12525539}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Overlap connective tissue disease (OCTD) [MIM:604308]: Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable. {ECO:0000269\|PubMed:2739055}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness. {ECO:0000269\|PubMed:20375004}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. {ECO:0000269\|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal. {ECO:0000269\|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		[Asprosin]: Marfanoid-progeroid-lipodystrophy syndrome (MFLS) [MIM:616914]: An autosomal dominant syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome. Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly. Mental and motor development are within normal limits. {ECO:0000269\|PubMed:20979188, ECO:0000269\|PubMed:21594992, ECO:0000269\|PubMed:21594993, ECO:0000269\|PubMed:24039054, ECO:0000269\|PubMed:24613577, ECO:0000269\|PubMed:24665001, ECO:0000269\|PubMed:26860060, ECO:0000269\|PubMed:27087445}. Note=The disease is caused by variants affecting the gene represented in this entry.
Miscellaneous:		[Asprosin]: Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. {ECO:0000303\|PubMed:27087445}.
Similarity:		Belongs to the fibrillin family. {ECO:0000305}.
Sequence caution:		Sequence=CAA45118.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};