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Database: UniProt
Entry: A0A3B4VMC3_SERDU
LinkDB: A0A3B4VMC3_SERDU
Original site: A0A3B4VMC3_SERDU 
ID   A0A3B4VMC3_SERDU        Unreviewed;       343 AA.
AC   A0A3B4VMC3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Syntaxin-18 {ECO:0000256|ARBA:ARBA00019409};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000031747.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000031747.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4VMC3; -.
DR   STRING; 41447.ENSSDUP00000031747; -.
DR   Ensembl; ENSSDUT00000032298.1; ENSSDUP00000031747.1; ENSSDUG00000022822.1.
DR   GeneTree; ENSGT00390000014853; -.
DR   OMA; PVNLWEE; -.
DR   Proteomes; UP000261420; Unplaced.
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; IPR010989; SNARE.
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   SUPFAM; SSF47661; t-snare proteins; 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   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        320..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..110
FT                   /note="SNARE-complex protein Syntaxin-18 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10496"
FT   REGION          180..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..267
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   343 AA;  39443 MW;  BA03D6A22806F3DA CRC64;
     MTLSLGDVSV CLQRCSCTNM AVDITLLFKA SVKTVKTRNK AIGIGFDSTK DEIFKRSRPK
     SGFSPKAKEV ITNITKLKDF LLQHRKDYVS AGSLISSDLT RMTDSERDQI DQDAQIFMRT
     CSEAIKQLRN EAEKKVTSAQ IKEHRGAVLD LIEMYLKGVC KLYSEQRAIR VKRMVDKKRM
     SRLAPEHHSH VEKTREVEPT EEKTVKEESS EKSVSEVLDN TVEHLWEEGR VEDELSPEEI
     QMFEQENQRL VSEMNSLVDE VRQIEGKVVE ISRLQEIFAE KVLQQETEID SIHQLVVGAT
     ENVKEGNEDI REAIKNNAGF RVWILFFLVM CSFSLLFLDW YDS
//
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