STX1A_CAEEL
ID STX1A_CAEEL Reviewed; 291 AA.
AC O16000; O18657; O61526; Q9TZZ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Syntaxin-1A homolog;
DE AltName: Full=Uncoordinated protein 64;
GN Name=unc-64 {ECO:0000312|WormBase:F56A8.7b}; ORFNames=F56A8.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA23584.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, INTERACTION WITH
RP UNC-18, AND TISSUE SPECIFICITY.
RX PubMed=9442061; DOI=10.1074/jbc.273.4.2192;
RA Ogawa H., Harada S., Sassa T., Yamamoto H., Hosono R.;
RT "Functional properties of the unc-64 gene encoding a Caenorhabditis elegans
RT syntaxin.";
RL J. Biol. Chem. 273:2192-2198(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD10538.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 265-291 (ISOFORM A), NUCLEOTIDE SEQUENCE [MRNA] OF 265-291 (ISOFORM C), AND
RP TISSUE SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD10538.1};
RX PubMed=9614171; DOI=10.1091/mbc.9.6.1235;
RA Saifee O., Wei L., Nonet M.L.;
RT "The Caenorhabditis elegans unc-64 locus encodes a syntaxin that interacts
RT genetically with synaptobrevin.";
RL Mol. Biol. Cell 9:1235-1252(1998).
RN [3] {ECO:0000312|EMBL:CAB05747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB05747.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1945043; DOI=10.1016/0304-3940(91)90270-4;
RA Hosono R., Kamiya Y.;
RT "Additional genes which result in an elevation of acetylcholine levels by
RT mutations in Caenorhabditis elegans.";
RL Neurosci. Lett. 128:243-244(1991).
RN [5] {ECO:0000305}
RP FUNCTION, MUTAGENESIS OF ALA-248, AND DISRUPTION PHENOTYPE.
RX PubMed=10377425; DOI=10.1073/pnas.96.13.7394;
RA Ailion M., Inoue T., Weaver C.I., Holdcraft R.W., Thomas J.H.;
RT "Neurosecretory control of aging in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7394-7397(1999).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ALA-248.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
CC -!- FUNCTION: Plays a critical role in several secretory processes,
CC including cuticle secretion and neurotransmitter release, and probably
CC assists in neuronal membrane maturation or the final stages of neuronal
CC differentiation (PubMed:1945043, PubMed:9442061). Essential for
CC embryonic viability and development. Has a role in dauer formation and
CC adult life span (PubMed:10377425). Required for locomotion
CC (PubMed:10377425). Probably by regulating neuronal transmission
CC downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and
CC upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the
CC decrease in pharyngeal pumping during the quiescent state that precedes
CC each larval molt (PubMed:17891142). {ECO:0000269|PubMed:10377425,
CC ECO:0000269|PubMed:17891142, ECO:0000269|PubMed:1945043,
CC ECO:0000269|PubMed:9442061}.
CC -!- SUBUNIT: Interacts with unc-18. {ECO:0000269|PubMed:9442061}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type IV
CC membrane protein {ECO:0000250|UniProtKB:P32851, ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171,
CC ECO:0000269|PubMed:9851916};
CC IsoId=O16000-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171,
CC ECO:0000269|PubMed:9851916}; Synonyms=syn1a
CC {ECO:0000269|PubMed:9442061};
CC IsoId=O16000-2; Sequence=VSP_052630;
CC Name=c {ECO:0000269|PubMed:9614171};
CC IsoId=O16000-3; Sequence=VSP_052631;
CC -!- TISSUE SPECIFICITY: Expressed throughout the head ganglion, nerve ring,
CC ventral cord, dorsal cord, intestine, vulva and spermatheca.
CC {ECO:0000269|PubMed:9442061, ECO:0000269|PubMed:9614171}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit defects in locomotion and
CC postembryonic development. All mutants are resistant to the
CC acetylcholinesterase inhibitor aldicarb indicating impaired cholinergic
CC transmission. {ECO:0000269|PubMed:10377425,
CC ECO:0000269|PubMed:1945043}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000255}.
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; AB008842; BAA23584.1; -; mRNA.
DR EMBL; AB008843; BAA23585.1; -; mRNA.
DR EMBL; AB008844; BAA23586.1; -; mRNA.
DR EMBL; AF047885; AAD10538.1; -; mRNA.
DR EMBL; AF047886; AAD10539.1; -; mRNA.
DR EMBL; AF047887; AAD10540.1; -; mRNA.
DR EMBL; Z83230; CAB05747.1; -; Genomic_DNA.
DR EMBL; Z83230; CAC42303.1; -; Genomic_DNA.
DR PIR; T37265; T37265.
DR PIR; T37266; T37266.
DR PIR; T42641; T42641.
DR RefSeq; NP_001022614.1; NM_001027443.3. [O16000-2]
DR RefSeq; NP_001022615.1; NM_001027444.3.
DR AlphaFoldDB; O16000; -.
DR SMR; O16000; -.
DR BioGRID; 41914; 8.
DR DIP; DIP-25166N; -.
DR DIP; DIP-29202N; -.
DR IntAct; O16000; 5.
DR STRING; 6239.F56A8.7a; -.
DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR EPD; O16000; -.
DR PaxDb; O16000; -.
DR PeptideAtlas; O16000; -.
DR EnsemblMetazoa; F56A8.7a.1; F56A8.7a.1; WBGene00006798. [O16000-2]
DR EnsemblMetazoa; F56A8.7a.2; F56A8.7a.2; WBGene00006798. [O16000-2]
DR EnsemblMetazoa; F56A8.7b.1; F56A8.7b.1; WBGene00006798. [O16000-1]
DR GeneID; 176743; -.
DR UCSC; F56A8.7b; c. elegans. [O16000-1]
DR CTD; 176743; -.
DR WormBase; F56A8.7a; CE16127; WBGene00006798; unc-64. [O16000-2]
DR WormBase; F56A8.7b; CE28035; WBGene00006798; unc-64. [O16000-1]
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR InParanoid; O16000; -.
DR OMA; RWICFIL; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; O16000; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-449836; Other interleukin signaling.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-CEL-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:O16000; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006798; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:WormBase.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; IGI:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
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 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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cuticle; Developmental protein;
KW Differentiation; Membrane; Neurogenesis; Neurotransmitter transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Syntaxin-1A homolog"
FT /id="PRO_0000314061"
FT TOPO_DOM 1..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 193..255
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..95
FT /evidence="ECO:0000255"
FT VAR_SEQ 265..291
FT /note="KKICILVTGVILITGLIIFILFYAKVL -> MKCYIFVLIVVIILVIVIAVV
FT IWVIVANASTSVVLPSKTSSSSTSNTSSQRFRVR (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9614171"
FT /id="VSP_052631"
FT VAR_SEQ 268..291
FT /note="CILVTGVILITGLIIFILFYAKVL -> IILIVVTILIGFVSLWLIQYIPGI
FT (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9442061,
FT ECO:0000303|PubMed:9614171, ECO:0000303|PubMed:9851916"
FT /id="VSP_052630"
FT MUTAGEN 248
FT /note="A->V: In e246; causes constitutive dauer formation,
FT defects in locomotion and increases life span. Restores
FT pharyngeal pumping in animals overexpressing lin-3."
FT /evidence="ECO:0000269|PubMed:10377425,
FT ECO:0000269|PubMed:17891142"
SQ 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
