STX3_CAEEL
ID STX3_CAEEL Reviewed; 306 AA.
AC Q20024;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative syntaxin-3;
GN Name=syx-3 {ECO:0000312|WormBase:F35C8.4};
GN Synonyms=syn-1 {ECO:0000312|WormBase:F35C8.4};
GN ORFNames=F35C8.4 {ECO:0000312|WormBase:F35C8.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, REGION, AND MUTAGENESIS
RP OF GLY-123 AND 177-ILE-GLU-178.
RX PubMed=19028454; DOI=10.1016/j.bbrc.2008.11.064;
RA Yamashita M., Iwasaki K., Doi M.;
RT "The non-neuronal syntaxin SYN-1 regulates defecation behavior and neural
RT activity in C. elegans through interaction with the Munc13-like protein
RT AEX-1.";
RL Biochem. Biophys. Res. Commun. 378:404-408(2009).
CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones (By similarity). Acts in the intestine to
CC regulate anterior body muscle contractions (aBOC) and the expulsion
CC steps during the defecation motor program (DMP).
CC {ECO:0000250|UniProtKB:P32851, ECO:0000269|PubMed:19028454}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19028454};
CC Single-pass type IV membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall, pharyngeal, vulval and
CC enteric muscles and in some head neurons.
CC {ECO:0000269|PubMed:19028454}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; BX284606; CCD62783.2; -; Genomic_DNA.
DR PIR; T16252; T16252.
DR RefSeq; NP_508909.2; NM_076508.5.
DR AlphaFoldDB; Q20024; -.
DR SMR; Q20024; -.
DR BioGRID; 533189; 2.
DR STRING; 6239.F35C8.4; -.
DR EPD; Q20024; -.
DR PaxDb; Q20024; -.
DR PeptideAtlas; Q20024; -.
DR PRIDE; Q20024; -.
DR EnsemblMetazoa; F35C8.4.1; F35C8.4.1; WBGene00006371.
DR UCSC; F35C8.4.2; c. elegans.
DR WormBase; F35C8.4; CE29788; WBGene00006371; syx-3.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01050000244948; -.
DR HOGENOM; CLU_042423_0_2_1; -.
DR InParanoid; Q20024; -.
DR OrthoDB; 1187933at2759; -.
DR PhylomeDB; Q20024; -.
DR Reactome; R-CEL-449836; Other interleukin signaling.
DR PRO; PR:Q20024; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006371; Expressed in embryo and 3 other tissues.
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:0005886; C:plasma membrane; IDA:UniProtKB.
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:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; ISS:WormBase.
DR GO; GO:2000294; P:positive regulation of defecation; IMP:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR GO; GO:0016081; P:synaptic vesicle docking; ISS:UniProtKB.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
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 Cell membrane; Coiled coil; Membrane; Neurotransmitter transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Putative syntaxin-3"
FT /id="PRO_0000210239"
FT TOPO_DOM 1..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 204..266
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 40..180
FT /note="Required for the regulation of the defecation motor
FT program"
FT /evidence="ECO:0000269|PubMed:19028454"
FT MUTAGEN 123
FT /note="G->E: In tg94; severe reduction in anterior body
FT wall muscle contraction (aBOC) and expulsion during the
FT defecation motor program."
FT /evidence="ECO:0000269|PubMed:19028454"
FT MUTAGEN 177..178
FT /note="IE->AA: 50 percent reduction in anterior body wall
FT muscle contraction (aBOC) and expulsion during the
FT defecation motor program."
FT /evidence="ECO:0000269|PubMed:19028454"
SQ SEQUENCE 306 AA; 34856 MW; FB5CEDABDF576936 CRC64;
MPRDRLKELQ EKATVNTIHA YNYDPPARKY DVESQPLINQ DADFEMFLER CSNIRGGLKS
LEEDYDAVVQ LHGALLSTPG ADSENSNKLK SHNQMFFSKA EQIKNSLKIL SEETSRIPTT
ACGIMRAKSD QVKSIYKTFE NIMLNFNREQ DEYKEKAKRK IVDYLKIRNM QLSDEEIENA
VSSGNLSEVT KGVMLALNEK KALYDEVKSR ADELKNLERQ MGELAQMFHD LHIMVVSQAK
MVDSIVNSVE NATEYAKQAR GNVEEARNLQ KRARKMKVCI IIGSIIAVLI LILFIQSAVC
HFTPIC
