ID B3S4L5_TRIAD Unreviewed; 293 AA.
AC B3S4L5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Syntaxin 1.2 {ECO:0000313|EMBL:EDV22652.1};
GN ORFNames=TRIADDRAFT_66400 {ECO:0000313|EMBL:EDV22652.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22652.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV22652.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22652.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC {ECO:0000256|ARBA:ARBA00009063, ECO:0000256|RuleBase:RU003858}.
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; DS985249; EDV22652.1; -; Genomic_DNA.
DR RefSeq; XP_002115196.1; XM_002115160.1.
DR AlphaFoldDB; B3S4L5; -.
DR SMR; B3S4L5; -.
DR STRING; 10228.B3S4L5; -.
DR GeneID; 6756408; -.
DR KEGG; tad:TRIADDRAFT_66400; -.
DR CTD; 6756408; -.
DR eggNOG; KOG0810; Eukaryota.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; B3S4L5; -.
DR OrthoDB; 2876074at2759; -.
DR PhylomeDB; B3S4L5; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; 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:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.70; -; 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; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF307; SYNTAXIN-1A; 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; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..255
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 293 AA; 33799 MW; DDF4D130FAD63C7E CRC64;
MKDKLAALKQ FRHDRNEYLN GDEEEYGYMD EFFEQVEEIR QGIEKITYNV EQANKTQIII
LTDPRMEKEA EGRLIDLTSE IKRFANRIKA RLKVMEQDIQ QQETMDGLSA DVRIKKSQCT
ALSKNYIDVM SEYNMQQIEY KEKCKARLET QLKITQQKVS EEDIDEMLES GGPAPRIFTS
GLMIDSAEAK RTLSLIESRH KEIMKLEKNL SDLAELFQDM GQLISVQGEM IDRIEYNVAQ
TTDYVERAKE DTKKATKYQS KARRKKVIII VCIIILALVI AGVFGGIFGS RGV
//
