STX18_HUMAN
ID STX18_HUMAN Reviewed; 335 AA.
AC Q9P2W9; Q596L3; Q5TZP5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Syntaxin-18;
DE AltName: Full=Cell growth-inhibiting gene 9 protein;
GN Name=STX18; ORFNames=GIG9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10788491; DOI=10.1074/jbc.275.18.13713;
RA Hatsuzawa K., Hirose H., Tani K., Yamamoto A., Scheller R.H., Tagaya M.;
RT "Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum,
RT intermediate compartment, and cis-Golgi vesicle trafficking.";
RL J. Biol. Chem. 275:13713-13720(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human growth inhibiting gene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN A COMPLEX WITH USE1L; SEC22B; RINT1 AND ZW10.
RX PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT "Implication of ZW10 in membrane trafficking between the endoplasmic
RT reticulum and Golgi.";
RL EMBO J. 23:1267-1278(2004).
RN [6]
RP INTERACTION WITH BNIP1.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Syntaxin that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER.
CC {ECO:0000269|PubMed:15029241}.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L, and SEC22B. RINT1/TIP20L and ZW10 are associated with the
CC complex through interaction with BNIP1/SEC20L. Interacts directly with
CC USE1L and BNIP1/SEC20L. {ECO:0000269|PubMed:15029241,
CC ECO:0000269|PubMed:15272311}.
CC -!- INTERACTION:
CC Q9P2W9; O75396: SEC22B; NbExp=3; IntAct=EBI-725334, EBI-1058865;
CC Q9P2W9; Q9NZ43: USE1; NbExp=8; IntAct=EBI-725334, EBI-742842;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:15029241}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:15029241}. Golgi apparatus membrane {ECO:0000305};
CC Single-pass type IV membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AB028741; BAA95213.1; -; mRNA.
DR EMBL; AY453396; AAS47513.1; -; mRNA.
DR EMBL; BT007150; AAP35814.1; -; mRNA.
DR EMBL; BT020135; AAV38937.1; -; mRNA.
DR EMBL; BC014613; AAH14613.1; -; mRNA.
DR CCDS; CCDS3377.1; -.
DR RefSeq; NP_001333210.1; NM_001346281.1.
DR RefSeq; NP_001333211.1; NM_001346282.1.
DR RefSeq; NP_001333229.1; NM_001346300.1.
DR RefSeq; NP_058626.1; NM_016930.3.
DR AlphaFoldDB; Q9P2W9; -.
DR SMR; Q9P2W9; -.
DR BioGRID; 119782; 160.
DR DIP; DIP-37617N; -.
DR IntAct; Q9P2W9; 47.
DR MINT; Q9P2W9; -.
DR STRING; 9606.ENSP00000305810; -.
DR iPTMnet; Q9P2W9; -.
DR PhosphoSitePlus; Q9P2W9; -.
DR BioMuta; STX18; -.
DR DMDM; 17369347; -.
DR EPD; Q9P2W9; -.
DR jPOST; Q9P2W9; -.
DR MassIVE; Q9P2W9; -.
DR MaxQB; Q9P2W9; -.
DR PaxDb; Q9P2W9; -.
DR PeptideAtlas; Q9P2W9; -.
DR PRIDE; Q9P2W9; -.
DR ProteomicsDB; 83906; -.
DR Antibodypedia; 727; 136 antibodies from 25 providers.
DR DNASU; 53407; -.
DR Ensembl; ENST00000306200.7; ENSP00000305810.2; ENSG00000168818.10.
DR GeneID; 53407; -.
DR KEGG; hsa:53407; -.
DR MANE-Select; ENST00000306200.7; ENSP00000305810.2; NM_016930.4; NP_058626.1.
DR UCSC; uc003gic.4; human.
DR CTD; 53407; -.
DR DisGeNET; 53407; -.
DR GeneCards; STX18; -.
DR HGNC; HGNC:15942; STX18.
DR HPA; ENSG00000168818; Tissue enhanced (cervix).
DR MIM; 606046; gene.
DR neXtProt; NX_Q9P2W9; -.
DR OpenTargets; ENSG00000168818; -.
DR PharmGKB; PA38061; -.
DR VEuPathDB; HostDB:ENSG00000168818; -.
DR eggNOG; KOG3894; Eukaryota.
DR GeneTree; ENSGT00390000014853; -.
DR HOGENOM; CLU_071402_1_0_1; -.
DR InParanoid; Q9P2W9; -.
DR OMA; WEESRVE; -.
DR OrthoDB; 1141750at2759; -.
DR PhylomeDB; Q9P2W9; -.
DR TreeFam; TF105868; -.
DR PathwayCommons; Q9P2W9; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q9P2W9; -.
DR BioGRID-ORCS; 53407; 691 hits in 1083 CRISPR screens.
DR GenomeRNAi; 53407; -.
DR Pharos; Q9P2W9; Tbio.
DR PRO; PR:Q9P2W9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P2W9; protein.
DR Bgee; ENSG00000168818; Expressed in right uterine tube and 178 other tissues.
DR ExpressionAtlas; Q9P2W9; baseline and differential.
DR Genevisible; Q9P2W9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:1902117; P:positive regulation of organelle assembly; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR InterPro; IPR019529; Syntaxin-18_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR Pfam; PF10496; Syntaxin-18_N; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..335
FT /note="Syntaxin-18"
FT /id="PRO_0000210231"
FT TOPO_DOM 1..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..335
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 243..305
FT /note="t-SNARE coiled-coil homology"
FT REGION 168..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 32
FT /note="D -> Y (in dbSNP:rs13134070)"
FT /id="VAR_052250"
FT VARIANT 51
FT /note="S -> G (in dbSNP:rs36109375)"
FT /id="VAR_052251"
FT VARIANT 228
FT /note="S -> T (in dbSNP:rs33952588)"
FT /id="VAR_052252"
FT CONFLICT 11
FT /note="A -> V (in Ref. 3; AAV38937)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="N -> D (in Ref. 2; AAS47513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38674 MW; D89B3B52407D77FF CRC64;
MAVDITLLFR ASVKTVKTRN KALGVAVGGG VDGSRDELFR RSPRPKGDFS SRAREVISHI
GKLRDFLLEH RKDYINAYSH TMSEYGRMTD TERDQIDQDA QIFMRTCSEA IQQLRTEAHK
EIHSQQVKEH RTAVLDFIED YLKRVCKLYS EQRAIRVKRV VDKKRLSKLE PEPNTKTRES
TSSEKVSQSP SKDSEENPAT EERPEKILAE TQPELGTWGD GKGEDELSPE EIQMFEQENQ
RLIGEMNSLF DEVRQIEGRV VEISRLQEIF TEKVLQQEAE IDSIHQLVVG ATENIKEGNE
DIREAIKNNA GFRVWILFFL VMCSFSLLFL DWYDS
