STX1A_PONAB
ID STX1A_PONAB Reviewed; 288 AA.
AC Q5R4L2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Syntaxin-1A;
GN Name=STX1A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in hormone and neurotransmitter
CC calcium-dependent exocytosis and endocytosis. Part of the SNARE
CC (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and
CC VAMP2 which mediates the fusion of synaptic vesicles with the
CC presynaptic plasma membrane. STX1A and SNAP25 are localized on the
CC plasma membrane while VAMP2 resides in synaptic vesicles. The pairing
CC of the three SNAREs from the N-terminal SNARE motifs to the C-terminal
CC anchors leads to the formation of the SNARE complex, which brings
CC membranes into close proximity and results in final fusion (By
CC similarity). Participates in the calcium-dependent regulation of
CC acrosomal exocytosis in sperm. Also plays an important role in the
CC exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-
CC 1) (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000250|UniProtKB:P32851}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex constitutes the basic catalytic machinery of the
CC complex neurotransmitter release apparatus. The SNARE complex interacts
CC with CPLX1. Interacts with STXBP1. Interacts (via C-terminus) with
CC KCNB1 (via C-terminus); the interaction increases in a calcium-
CC dependent manner and induces a pore-independent enhancement of
CC exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta
CC cells and from the soma of dorsal root ganglia (DRG) neurons (By
CC similarity). Interacts with SYTL4 (By similarity). Interacts with
CC STXBP6. Interacts with PLCL1 (via C2 domain) (By similarity). Interacts
CC with OTOF. Interacts with LGI3 (By similarity). Interacts with SLC6A4
CC (By similarity). Interacts with SYT6 and SYT8; the interaction is
CC Ca(2+)-dependent (By similarity). Interacts with VAMP8. Interacts with
CC SNAP23 (By similarity). Interacts with VAPA and SYBU (By similarity).
CC Interacts with PRRT2 (By similarity). Interacts with SEPT8 (By
CC similarity). Interacts with STXBP5L (By similarity). Interacts with
CC synaptotagmin-1/SYT1 (By similarity). Interacts with SEPTIN5; in the
CC cerebellar cortex (By similarity). Interacts with SEPTIN4; in the
CC striatum (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000250|UniProtKB:P32851, ECO:0000250|UniProtKB:Q16623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV
CC membrane protein {ECO:0000250|UniProtKB:O35526}. Cell membrane
CC {ECO:0000250|UniProtKB:P32851}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:O35526}. Note=Colocalizes with KCNB1 at the cell
CC membrane. {ECO:0000250|UniProtKB:P32851}.
CC -!- PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1
CC significantly decreases its interaction with STXBP1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Sumoylated, sumoylation is required for regulation of synaptic
CC vesicle endocytosis. {ECO:0000250|UniProtKB:Q16623}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR861234; CAH93304.1; -; mRNA.
DR RefSeq; NP_001126944.1; NM_001133472.1.
DR AlphaFoldDB; Q5R4L2; -.
DR BMRB; Q5R4L2; -.
DR SMR; Q5R4L2; -.
DR STRING; 9601.ENSPPYP00000019613; -.
DR GeneID; 100173962; -.
DR KEGG; pon:100173962; -.
DR CTD; 6804; -.
DR eggNOG; KOG0810; Eukaryota.
DR InParanoid; Q5R4L2; -.
DR OrthoDB; 1033833at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0000149; F:SNARE binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028669; STX1.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF84; PTHR19957:SF84; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Exocytosis;
KW Isopeptide bond; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..288
FT /note="Syntaxin-1A"
FT /id="PRO_0000210188"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 192..254
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 68..109
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35526"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32851"
FT MOD_RES 188
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
SQ SEQUENCE 288 AA; 33007 MW; 8AC787EFCE7EC0A1 CRC64;
MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVIPGIVIA STVGGIFA
