STX18_MOUSE
ID STX18_MOUSE Reviewed; 334 AA.
AC Q8VDS8; Q3TDJ0; Q9D8T6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Syntaxin-18;
GN Name=Stx18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Syntaxin that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VDS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDS8-2; Sequence=VSP_017902;
CC Name=3;
CC IsoId=Q8VDS8-3; Sequence=VSP_017903, VSP_017904;
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AK007700; BAB25198.1; -; mRNA.
DR EMBL; AK169273; BAE41033.1; -; mRNA.
DR EMBL; AK170165; BAE41611.1; -; mRNA.
DR EMBL; BC021362; AAH21362.1; -; mRNA.
DR CCDS; CCDS19250.1; -. [Q8VDS8-1]
DR CCDS; CCDS71583.1; -. [Q8VDS8-3]
DR CCDS; CCDS80270.1; -. [Q8VDS8-2]
DR RefSeq; NP_001276464.1; NM_001289535.1. [Q8VDS8-3]
DR RefSeq; NP_001276465.1; NM_001289536.1. [Q8VDS8-2]
DR RefSeq; NP_081235.2; NM_026959.3. [Q8VDS8-1]
DR AlphaFoldDB; Q8VDS8; -.
DR SMR; Q8VDS8; -.
DR STRING; 10090.ENSMUSP00000109761; -.
DR iPTMnet; Q8VDS8; -.
DR PhosphoSitePlus; Q8VDS8; -.
DR EPD; Q8VDS8; -.
DR MaxQB; Q8VDS8; -.
DR PaxDb; Q8VDS8; -.
DR PeptideAtlas; Q8VDS8; -.
DR PRIDE; Q8VDS8; -.
DR ProteomicsDB; 257468; -. [Q8VDS8-1]
DR ProteomicsDB; 257469; -. [Q8VDS8-2]
DR ProteomicsDB; 257470; -. [Q8VDS8-3]
DR Antibodypedia; 727; 136 antibodies from 25 providers.
DR DNASU; 71116; -.
DR Ensembl; ENSMUST00000031008; ENSMUSP00000031008; ENSMUSG00000029125. [Q8VDS8-3]
DR Ensembl; ENSMUST00000042146; ENSMUSP00000038205; ENSMUSG00000029125. [Q8VDS8-2]
DR Ensembl; ENSMUST00000114126; ENSMUSP00000109761; ENSMUSG00000029125. [Q8VDS8-1]
DR GeneID; 71116; -.
DR KEGG; mmu:71116; -.
DR UCSC; uc008xfx.2; mouse. [Q8VDS8-3]
DR UCSC; uc008xfy.2; mouse. [Q8VDS8-1]
DR UCSC; uc008xfz.2; mouse. [Q8VDS8-2]
DR CTD; 53407; -.
DR MGI; MGI:1918366; Stx18.
DR VEuPathDB; HostDB:ENSMUSG00000029125; -.
DR eggNOG; KOG3894; Eukaryota.
DR GeneTree; ENSGT00390000014853; -.
DR HOGENOM; CLU_071402_1_0_1; -.
DR InParanoid; Q8VDS8; -.
DR OMA; WEESRVE; -.
DR OrthoDB; 1141750at2759; -.
DR PhylomeDB; Q8VDS8; -.
DR TreeFam; TF105868; -.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 71116; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Stx18; mouse.
DR PRO; PR:Q8VDS8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VDS8; protein.
DR Bgee; ENSMUSG00000029125; Expressed in calcareous tooth and 271 other tissues.
DR ExpressionAtlas; Q8VDS8; baseline and differential.
DR Genevisible; Q8VDS8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IPI:AgBase.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:1902117; P:positive regulation of organelle assembly; ISO:MGI.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
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 Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..334
FT /note="Syntaxin-18"
FT /id="PRO_0000210232"
FT TOPO_DOM 1..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 242..304
FT /note="t-SNARE coiled-coil homology"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 118..144
FT /note="AHKEIHSQQVKEHRTAVLDFVDDYLKR -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017902"
FT VAR_SEQ 304..308
FT /note="AIKNN -> LAHQG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017903"
FT VAR_SEQ 309..334
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017904"
FT CONFLICT 112
FT /note="H -> Q (in Ref. 2; AAH21362)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> V (in Ref. 2; AAH21362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38381 MW; 17351A82343475F0 CRC64;
MAVDITLLFR ASVKTVKTRN KALGVAVGGG ADGSRDELFR RSPRPKGDFS SRAREVISHI
GKLRDFLLEH RKEYINAYSH TMSDYGRMTD TERDQIDQDA QIFIRTCSEA IHQLRTEAHK
EIHSQQVKEH RTAVLDFVDD YLKRVCKLYS EQRAIRVKRV VDKKRLSKLE PEPHTKRKDS
TSEKAPQNAS QDSEGKPAAE ELPEKPLAES QPELGTWGDG KGEDELSPEE IQMFEQENQR
LIGEMNSLFD EVRQIEGKVV EISRLQEIFT EKVLQQETEI DSIHQLVVGA TENIKEGNED
IREAIKNNAG FRVWILFFLV MCSFSLLFLD WYDS
