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Syntaxin-1A homolog (Uncoordinated protein 64)

 STX1A_CAEEL             Reviewed;         291 AA.
O16000; O18657; O61526; Q9TZZ0;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Syntaxin-1A homolog;
AltName: Full=Uncoordinated protein 64;
Name=unc-64 {ECO:0000312|WormBase:F56A8.7b}; ORFNames=F56A8.7;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:BAA23584.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, INTERACTION
WITH UNC-18, AND TISSUE SPECIFICITY.
PubMed=9442061; DOI=10.1074/jbc.273.4.2192;
Ogawa H., Harada S., Sassa T., Yamamoto H., Hosono R.;
"Functional properties of the unc-64 gene encoding a Caenorhabditis
elegans syntaxin.";
J. Biol. Chem. 273:2192-2198(1998).
[2] {ECO:0000305, ECO:0000312|EMBL:AAD10538.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
265-291 (ISOFORM A), NUCLEOTIDE SEQUENCE [MRNA] OF 265-291 (ISOFORM
C), AND TISSUE SPECIFICITY.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD10538.1};
PubMed=9614171; DOI=10.1091/mbc.9.6.1235;
Saifee O., Wei L., Nonet M.L.;
"The Caenorhabditis elegans unc-64 locus encodes a syntaxin that
interacts genetically with synaptobrevin.";
Mol. Biol. Cell 9:1235-1252(1998).
[3] {ECO:0000312|EMBL:CAB05747.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB05747.1};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=1945043; DOI=10.1016/0304-3940(91)90270-4;
Hosono R., Kamiya Y.;
"Additional genes which result in an elevation of acetylcholine levels
by mutations in Caenorhabditis elegans.";
Neurosci. Lett. 128:243-244(1991).
[5] {ECO:0000305}
FUNCTION, MUTAGENESIS OF ALA-248, AND DISRUPTION PHENOTYPE.
PubMed=10377425; DOI=10.1073/pnas.96.13.7394;
Ailion M., Inoue T., Weaver C.I., Holdcraft R.W., Thomas J.H.;
"Neurosecretory control of aging in Caenorhabditis elegans.";
Proc. Natl. Acad. Sci. U.S.A. 96:7394-7397(1999).
[6]
FUNCTION, AND MUTAGENESIS OF ALA-248.
PubMed=17891142; DOI=10.1038/nn1981;
Van Buskirk C., Sternberg P.W.;
"Epidermal growth factor signaling induces behavioral quiescence in
Caenorhabditis elegans.";
Nat. Neurosci. 10:1300-1307(2007).
-!- FUNCTION: Plays a critical role in several secretory processes,
including cuticle secretion and neurotransmitter release, and
probably assists in neuronal membrane maturation or the final
stages of neuronal differentiation (PubMed:1945043,
PubMed:9442061). Essential for embryonic viability and
development. Has a role in dauer formation and adult life span
(PubMed:10377425). Required for locomotion (PubMed:10377425).
Probably by regulating neuronal transmission downstream of lin-3
and receptor lin-23 and phospholipase plc-3 and upstream of
innexin unc-7 and egl-4/PKG in ALA neurons, involved in the
decrease in pharyngeal pumping during the quiescent state that
precedes each larval molt (PubMed:17891142).
{ECO:0000269|PubMed:10377425, ECO:0000269|PubMed:17891142,
ECO:0000269|PubMed:1945043, ECO:0000269|PubMed:9442061}.
-!- SUBUNIT: Interacts with unc-18. {ECO:0000269|PubMed:9442061}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type IV
membrane protein {ECO:0000250|UniProtKB:P32851, ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=b {ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171,
ECO:0000269|PubMed:9851916};
IsoId=O16000-1; Sequence=Displayed;
Name=a {ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171,
ECO:0000269|PubMed:9851916}; Synonyms=syn1a
{ECO:0000269|PubMed:9442061};
IsoId=O16000-2; Sequence=VSP_052630;
Name=c {ECO:0000269|PubMed:9614171};
IsoId=O16000-3; Sequence=VSP_052631;
-!- TISSUE SPECIFICITY: Expressed throughout the head ganglion, nerve
ring, ventral cord, dorsal cord, intestine, vulva and spermatheca.
{ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171}.
-!- DISRUPTION PHENOTYPE: Worms exhibit defects in locomotion and
postembryonic development. All mutants are resistant to the
acetylcholinesterase inhibitor aldicarb indicating impaired
cholinergic transmission. {ECO:0000269|PubMed:10377425,
ECO:0000269|PubMed:1945043}.
-!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AB008842; BAA23584.1; -; mRNA.
EMBL; AB008843; BAA23585.1; -; mRNA.
EMBL; AB008844; BAA23586.1; -; mRNA.
EMBL; AF047885; AAD10538.1; -; mRNA.
EMBL; AF047886; AAD10539.1; -; mRNA.
EMBL; AF047887; AAD10540.1; -; mRNA.
EMBL; Z83230; CAB05747.1; -; Genomic_DNA.
EMBL; Z83230; CAC42303.1; -; Genomic_DNA.
PIR; T37265; T37265.
PIR; T37266; T37266.
PIR; T42641; T42641.
RefSeq; NP_001022614.1; NM_001027443.3. [O16000-2]
RefSeq; NP_001022615.1; NM_001027444.3. [O16000-1]
UniGene; Cel.18377; -.
ProteinModelPortal; O16000; -.
SMR; O16000; -.
BioGrid; 41914; 2.
DIP; DIP-25166N; -.
DIP; DIP-29202N; -.
IntAct; O16000; 5.
MINT; MINT-1119100; -.
STRING; 6239.F56A8.7b; -.
TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
EPD; O16000; -.
PaxDb; O16000; -.
PeptideAtlas; O16000; -.
PRIDE; O16000; -.
EnsemblMetazoa; F56A8.7b; F56A8.7b; WBGene00006798. [O16000-1]
GeneID; 176743; -.
KEGG; cel:CELE_F56A8.7; -.
UCSC; F56A8.7b; c. elegans. [O16000-1]
CTD; 176743; -.
WormBase; F56A8.7a; CE16127; WBGene00006798; unc-64. [O16000-2]
WormBase; F56A8.7b; CE28035; WBGene00006798; unc-64. [O16000-1]
eggNOG; KOG0810; Eukaryota.
eggNOG; COG5074; LUCA.
GeneTree; ENSGT00760000119200; -.
HOGENOM; HOG000286023; -.
InParanoid; O16000; -.
KO; K04560; -.
OMA; AELHQMF; -.
OrthoDB; EOG091G0EUK; -.
PhylomeDB; O16000; -.
Reactome; R-CEL-449836; Other interleukin signaling.
PRO; PR:O16000; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00006798; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
GO; GO:0030425; C:dendrite; IDA:WormBase.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IC:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
GO; GO:0051087; F:chaperone binding; IPI:WormBase.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0040011; P:locomotion; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0007269; P:neurotransmitter secretion; IMP:UniProtKB.
GO; GO:0017157; P:regulation of exocytosis; IEA:InterPro.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
InterPro; IPR010989; SNARE.
InterPro; IPR028669; STX1A.
InterPro; IPR006012; Syntaxin/epimorphin_CS.
InterPro; IPR006011; Syntaxin_N.
InterPro; IPR000727; T_SNARE_dom.
PANTHER; PTHR19957:SF210; PTHR19957:SF210; 1.
Pfam; PF05739; SNARE; 1.
Pfam; PF00804; Syntaxin; 1.
SMART; SM00503; SynN; 1.
SMART; SM00397; t_SNARE; 1.
SUPFAM; SSF47661; SSF47661; 1.
PROSITE; PS00914; SYNTAXIN; 1.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cuticle;
Developmental protein; Differentiation; Membrane; Neurogenesis;
Neurotransmitter transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 291 Syntaxin-1A homolog.
/FTId=PRO_0000314061.
TOPO_DOM 1 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 288 291 Extracellular. {ECO:0000255}.
DOMAIN 193 255 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
COILED 69 95 {ECO:0000255}.
VAR_SEQ 265 291 KKICILVTGVILITGLIIFILFYAKVL -> MKCYIFVLIV
VIILVIVIAVVIWVIVANASTSVVLPSKTSSSSTSNTSSQR
FRVR (in isoform c).
{ECO:0000303|PubMed:9614171}.
/FTId=VSP_052631.
VAR_SEQ 268 291 CILVTGVILITGLIIFILFYAKVL -> IILIVVTILIGFV
SLWLIQYIPGI (in isoform a).
{ECO:0000303|PubMed:9442061,
ECO:0000303|PubMed:9614171,
ECO:0000303|PubMed:9851916}.
/FTId=VSP_052630.
MUTAGEN 248 248 A->V: In e246; causes constitutive dauer
formation, defects in locomotion and
increases life span. Restores pharyngeal
pumping in animals overexpressing lin-3.
{ECO:0000269|PubMed:10377425,
ECO:0000269|PubMed:17891142}.
SEQUENCE 291 AA; 33253 MW; A1EC04D6F04A3613 CRC64;
MTKDRLSALK AAQSEDEQDD DMHMDTGNAQ YMEEFFEQVE EIRGSVDIIA NNVEEVKKKH
SAILSNPVND QKTKEELDEL MAVIKRAANK VRGKLKLIEN AIDHDEQGAG NADLRIRKTQ
HSTLSRRFVE VMTDYNKTQT DYRERCKGRI QRQLDIAGKQ VGDEDLEEMI ESGNPGVFTQ
GIITDTQQAK QTLADIEARH NDIMKLESSI RELHDMFMDM AMLVESQGEM VDRIEYNVEH
AKEFVDRAVA DTKKAVQYQS KARRKKICIL VTGVILITGL IIFILFYAKV L


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