UniProt functional annotation for Q86XP0



	UniProt functional annotation for Q86XP0

UniProt code: Q86XP0.

Organism: Homo sapiens (Human).

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

Function: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position (PubMed:14709560). Has a preference for linoleic acid at the sn-2 position (PubMed:14709560). {ECO:0000269|PubMed:14709560}.

Catalytic activity: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:14709560};

Catalytic activity: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000269|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000305|PubMed:14709560};

Catalytic activity: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000305|PubMed:14709560};

Catalytic activity: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:14709560};

Catalytic activity: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:Q50L43}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:Q50L43};

Catalytic activity: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:Q50L43}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:Q50L43};

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};

Activity regulation: Stimulated by cytosolic Ca(2+). {ECO:0000269|PubMed:14709560}.

Biophysicochemical properties: Kinetic parameters: Vmax=9.23 pmol/min/mg enzyme with 1-palmitoyl-2-arachidonyl- phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560}; Vmax=58.56 pmol/min/mg enzyme with 1-palmitoyl-2-linoleoyl- phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560}; Vmax=11 pmol/min/mg enzyme with 1-palmitoyl-2-oleoyl- phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560};

Pathway: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:14709560}.

Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q50L43}. Membrane {ECO:0000250|UniProtKB:Q50L43}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q50L43}; Cytoplasmic side {ECO:0000250|UniProtKB:Q50L43}. Note=Translocates to perinuclear membranes that may correspond to endoplasmic reticulum or Golgi in a calcium-dependent fashion. {ECO:0000250|UniProtKB:Q50L43}.

Tissue specificity: Expressed in stratified squamous epithelia, such as those in skin and cervix, but not in other tissues (PubMed:14709560). Strongly expressed in the upper spinous layer of the psoriatic epidermis, expressed weakly and discontinuously in atopic dermatitis and mycosis fungoides, and not detected in the epidermis of normal skin (PubMed:14709560). {ECO:0000269|PubMed:14709560}.

Domain: The N-terminal C2 domain mediates the association with lipid membranes upon calcium binding (Probable). An additional second C2 domain may stand in between the C2 domain and the PLA2c domain (Probable). {ECO:0000305|PubMed:14709560}.

Miscellaneous: [Isoform 2]: May be due to an intron retention. {ECO:0000305}.

Sequence caution: Sequence=AAH34571.1; Type=Erroneous initiation; Note=Truncated 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:		Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position (PubMed:14709560). Has a preference for linoleic acid at the sn-2 position (PubMed:14709560). {ECO:0000269\|PubMed:14709560}.


Catalytic activity:		Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269\|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305\|PubMed:14709560};
Catalytic activity:		Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000269\|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000305\|PubMed:14709560};
Catalytic activity:		Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000269\|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000305\|PubMed:14709560};
Catalytic activity:		Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269\|PubMed:14709560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305\|PubMed:14709560};
Catalytic activity:		Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250\|UniProtKB:Q50L43}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250\|UniProtKB:Q50L43};
Catalytic activity:		Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1- hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250\|UniProtKB:Q50L43}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250\|UniProtKB:Q50L43};
Cofactor:		Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00041};
Activity regulation:		Stimulated by cytosolic Ca(2+). {ECO:0000269\|PubMed:14709560}.
Biophysicochemical properties:		Kinetic parameters: Vmax=9.23 pmol/min/mg enzyme with 1-palmitoyl-2-arachidonyl- phosphatidylcholine as substrate {ECO:0000269\|PubMed:14709560}; Vmax=58.56 pmol/min/mg enzyme with 1-palmitoyl-2-linoleoyl- phosphatidylcholine as substrate {ECO:0000269\|PubMed:14709560}; Vmax=11 pmol/min/mg enzyme with 1-palmitoyl-2-oleoyl- phosphatidylcholine as substrate {ECO:0000269\|PubMed:14709560};
Pathway:		Lipid metabolism; fatty acid metabolism. {ECO:0000269\|PubMed:14709560}.
Subcellular location:		Cytoplasm, cytosol {ECO:0000250\|UniProtKB:Q50L43}. Membrane {ECO:0000250\|UniProtKB:Q50L43}; Peripheral membrane protein {ECO:0000250\|UniProtKB:Q50L43}; Cytoplasmic side {ECO:0000250\|UniProtKB:Q50L43}. Note=Translocates to perinuclear membranes that may correspond to endoplasmic reticulum or Golgi in a calcium-dependent fashion. {ECO:0000250\|UniProtKB:Q50L43}.
Tissue specificity:		Expressed in stratified squamous epithelia, such as those in skin and cervix, but not in other tissues (PubMed:14709560). Strongly expressed in the upper spinous layer of the psoriatic epidermis, expressed weakly and discontinuously in atopic dermatitis and mycosis fungoides, and not detected in the epidermis of normal skin (PubMed:14709560). {ECO:0000269\|PubMed:14709560}.
Domain:		The N-terminal C2 domain mediates the association with lipid membranes upon calcium binding (Probable). An additional second C2 domain may stand in between the C2 domain and the PLA2c domain (Probable). {ECO:0000305\|PubMed:14709560}.
Miscellaneous:		[Isoform 2]: May be due to an intron retention. {ECO:0000305}.
Sequence caution:		Sequence=AAH34571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};