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Database: UniProt
Entry: W5M4S1_LEPOC
LinkDB: W5M4S1_LEPOC
Original site: W5M4S1_LEPOC 
ID   W5M4S1_LEPOC            Unreviewed;       288 AA.
AC   W5M4S1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Syntaxin-1B {ECO:0000256|ARBA:ARBA00040532};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003379.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000003379.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the
CC       interaction is Ca(2+)-dependent. {ECO:0000256|ARBA:ARBA00038802}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063, ECO:0000256|RuleBase:RU003858}.
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DR   EMBL; AHAT01038747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015201626.1; XM_015346140.1.
DR   AlphaFoldDB; W5M4S1; -.
DR   STRING; 7918.ENSLOCP00000003379; -.
DR   Ensembl; ENSLOCT00000003386.1; ENSLOCP00000003379.1; ENSLOCG00000002864.1.
DR   GeneID; 102682902; -.
DR   KEGG; loc:102682902; -.
DR   CTD; 112755; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   GeneTree; ENSGT01030000234627; -.
DR   HOGENOM; CLU_042423_2_2_1; -.
DR   InParanoid; W5M4S1; -.
DR   OMA; ANIEQKG; -.
DR   OrthoDB; 2876074at2759; -.
DR   Proteomes; UP000018468; Linkage group LG5.
DR   Bgee; ENSLOCG00000002864; Expressed in camera-type eye and 8 other cell types or tissues.
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:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0060025; P:regulation of synaptic activity; IEA:Ensembl.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   CDD; cd15880; SNARE_syntaxin1; 1.
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:SF334; SYNTAXIN-1B; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        265..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..253
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..105
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   288 AA;  33299 MW;  EC6B7992DBC34CCF CRC64;
     MKDRTQELRS AKDSDDDEEV VQVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI
     LAAPNPDEKT KQELEDLTAD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS
     TLSRKFVEVM TEYNTTQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI
     KMDSQMTKQA LNEIETRHNE IIKLENSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV
     DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGF
//
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