UniProt functional annotation for Q7L1I2



	UniProt functional annotation for Q7L1I2

UniProt code: Q7L1I2.

Organism: Homo sapiens (Human).

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

Function: Probably plays a role in the control of regulated secretion in neural and endocrine cells. {ECO:0000250}.

Function: (Microbial infection) Receptor for the C.botulinum neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential but enhances the interaction (PubMed:29649119). Probably also serves as a receptor for the closely related C.botulinum neurotoxin type A1. {ECO:0000269|PubMed:29649119, ECO:0000305|PubMed:29649119}.

Subunit: Interacts with SYT1 in a calcium-independent manner. Forms a complex with SYT1, syntaxin-1 and SNAP25 (By similarity). {ECO:0000250}.

Subunit: (Microbial infection) Interacts with C.botulinum neurotoxin type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is improved by glycosylation of SV2 (PubMed:29649119). {ECO:0000305|PubMed:29649119}.

Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q63564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q63564}. Note=Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin- secreting cells of the pancreas (By similarity). Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (By similarity). {ECO:0000250|UniProtKB:Q63564}.

Ptm: N-glycosylated. {ECO:0000250}.

Ptm: The N-terminal cytoplasmic domain is phosphorylated by CK1. {ECO:0000250}.

Similarity: Belongs to the major facilitator superfamily. {ECO:0000305}.

Sequence caution: Sequence=BAA34455.2; 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:		Probably plays a role in the control of regulated secretion in neural and endocrine cells. {ECO:0000250}.



Function:		(Microbial infection) Receptor for the C.botulinum neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential but enhances the interaction (PubMed:29649119). Probably also serves as a receptor for the closely related C.botulinum neurotoxin type A1. {ECO:0000269\|PubMed:29649119, ECO:0000305\|PubMed:29649119}.


Subunit:		Interacts with SYT1 in a calcium-independent manner. Forms a complex with SYT1, syntaxin-1 and SNAP25 (By similarity). {ECO:0000250}.
Subunit:		(Microbial infection) Interacts with C.botulinum neurotoxin type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is improved by glycosylation of SV2 (PubMed:29649119). {ECO:0000305\|PubMed:29649119}.
Subcellular location:		Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250\|UniProtKB:Q63564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250\|UniProtKB:Q63564}. Note=Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin- secreting cells of the pancreas (By similarity). Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (By similarity). {ECO:0000250\|UniProtKB:Q63564}.
Ptm:		N-glycosylated. {ECO:0000250}.
Ptm:		The N-terminal cytoplasmic domain is phosphorylated by CK1. {ECO:0000250}.
Similarity:		Belongs to the major facilitator superfamily. {ECO:0000305}.
Sequence caution:		Sequence=BAA34455.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};