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Database: UniProt
Entry: A0A1S3L997_SALSA
LinkDB: A0A1S3L997_SALSA
Original site: A0A1S3L997_SALSA 
ID   A0A1S3L997_SALSA        Unreviewed;       331 AA.
AC   A0A1S3L997;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Syntaxin-18 {ECO:0000256|ARBA:ARBA00019409};
GN   Name=LOC106565202 {ECO:0000313|RefSeq:XP_013987536.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013987536.1};
RN   [1] {ECO:0000313|RefSeq:XP_013987536.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013987536.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Syntaxin that may be involved in targeting and fusion of
CC       Golgi-derived retrograde transport vesicles with the ER.
CC       {ECO:0000256|ARBA:ARBA00003746}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   RefSeq; XP_013987536.1; XM_014132061.1.
DR   AlphaFoldDB; A0A1S3L997; -.
DR   STRING; 8030.ENSSSAP00000034929; -.
DR   PaxDb; 8030-ENSSSAP00000034929; -.
DR   GeneID; 106565202; -.
DR   KEGG; sasa:106565202; -.
DR   OMA; FLDWYYD; -.
DR   OrthoDB; 3032483at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa12.
DR   Bgee; ENSSSAG00000041913; Expressed in brain and 15 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   CDD; cd15850; SNARE_syntaxin18; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR019529; Syntaxin-18_N.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   PANTHER; PTHR15959; SYNTAXIN-18; 1.
DR   PANTHER; PTHR15959:SF0; SYNTAXIN-18; 1.
DR   Pfam; PF10496; Syntaxin-18_N; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..91
FT                   /note="SNARE-complex protein Syntaxin-18 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10496"
FT   REGION          166..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          228..255
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        166..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  38092 MW;  EE866B98295AF563 CRC64;
     MAVDITVLFK ASVKTVKTRN KAMGVGFDLP KDEIFKKSRP KHGFSPKAKE VISNITKLKD
     FLLQHRKDYV NAGSLISSDL TRMTDNERDQ IDQDAQIFMR TCSEAIKQLR SEAEKQVIPT
     QIREHRGAVL DLIEIYLRGV CKLYSEQRAI RVKRVVDKKR LSRLEPEHHH SRVAVERSSP
     AVLHSEEKTA KEESSSGERS VTEVPENNVS LWEEGQGRVE DELSPEEMQM FEQENQRLVS
     EMSNLVDEVR QIEGKVVEIS RLQEIFAEKV LMQETEIDSI HQLVVGATEN VKEGNEDIRE
     AIKNNAGFRV WILFFLVMCS FSLLFLDWYD S
//
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