STX8_MOUSE
ID STX8_MOUSE Reviewed; 236 AA.
AC O88983;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Syntaxin-8;
DE AltName: Full=Syntaxin-like protein 3I35;
GN Name=Stx8;
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 [MRNA].
RA Thoreau V., Bilan F., Kitzis A., Chomel J.-C.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Subramaniam V.N., Loh E., Hong W.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RA Nakamura N., Wada Y., Futai M.;
RT "Mouse syntaxin8.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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 [7]
RP INTERACTION WITH HECTD3, AND UBIQUITINATION.
RX PubMed=18821010; DOI=10.1007/s10571-008-9303-0;
RA Zhang L., Kang L., Bond W., Zhang N.;
RT "Interaction between syntaxin 8 and HECTd3, a HECT domain ligase.";
RL Cell. Mol. Neurobiol. 29:115-121(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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).
RN [10]
RP INTERACTION WITH TPC1.
RX PubMed=28855648; DOI=10.1038/s41598-017-10607-4;
RA Castonguay J., Orth J.H.C., Mueller T., Sleman F., Grimm C.,
RA Wahl-Schott C., Biel M., Mallmann R.T., Bildl W., Schulte U., Klugbauer N.;
RT "The two-pore channel TPC1 is required for efficient protein processing
RT through early and recycling endosomes.";
RL Sci. Rep. 7:10038-10038(2017).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the early
CC secretory pathway, possibly by mediating retrograde transport from cis-
CC Golgi membranes to the ER. {ECO:0000250}.
CC -!- SUBUNIT: Forms a SNARE complex with STX7, VTI1B and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Part of the SNARE
CC core complex containing STX7, VAMP8 and VTI1B. Interacts with VAMP8 (By
CC similarity). Interacts with HECTD3. Interacts with TPC1
CC (PubMed:28855648). {ECO:0000250, ECO:0000269|PubMed:18821010,
CC ECO:0000269|PubMed:28855648}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV
CC membrane protein {ECO:0000250}. Note=Preferentially associated with the
CC early endosome. To a lesser extent, also present in late endosome, the
CC plasma membrane and coated pits (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by HECTD3. {ECO:0000269|PubMed:18821010}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF093064; AAC64149.1; -; mRNA.
DR EMBL; AF036716; AAC95286.1; -; mRNA.
DR EMBL; AB040054; BAB20500.1; -; mRNA.
DR EMBL; AK003297; BAB22698.1; -; mRNA.
DR EMBL; AL663076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048167; AAH48167.1; -; mRNA.
DR EMBL; BC048479; AAH48479.1; -; mRNA.
DR CCDS; CCDS24863.1; -.
DR RefSeq; NP_061238.1; NM_018768.2.
DR AlphaFoldDB; O88983; -.
DR SMR; O88983; -.
DR BioGRID; 207739; 5.
DR CORUM; O88983; -.
DR IntAct; O88983; 1.
DR STRING; 10090.ENSMUSP00000021285; -.
DR TCDB; 1.F.1.1.4; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; O88983; -.
DR PhosphoSitePlus; O88983; -.
DR SwissPalm; O88983; -.
DR EPD; O88983; -.
DR jPOST; O88983; -.
DR PaxDb; O88983; -.
DR PeptideAtlas; O88983; -.
DR PRIDE; O88983; -.
DR ProteomicsDB; 257370; -.
DR Antibodypedia; 726; 194 antibodies from 27 providers.
DR DNASU; 55943; -.
DR Ensembl; ENSMUST00000021285; ENSMUSP00000021285; ENSMUSG00000020903.
DR GeneID; 55943; -.
DR KEGG; mmu:55943; -.
DR UCSC; uc007jnj.1; mouse.
DR CTD; 9482; -.
DR MGI; MGI:1890156; Stx8.
DR VEuPathDB; HostDB:ENSMUSG00000020903; -.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00390000007779; -.
DR HOGENOM; CLU_099972_1_0_1; -.
DR InParanoid; O88983; -.
DR OMA; CGYWIVI; -.
DR OrthoDB; 1455798at2759; -.
DR PhylomeDB; O88983; -.
DR TreeFam; TF323262; -.
DR BioGRID-ORCS; 55943; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Stx8; mouse.
DR PRO; PR:O88983; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88983; protein.
DR Bgee; ENSMUSG00000020903; Expressed in vestibular membrane of cochlear duct and 247 other tissues.
DR ExpressionAtlas; O88983; baseline and differential.
DR Genevisible; O88983; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR CDD; cd15852; SNARE_Syntaxin8; 1.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR041875; Syntaxin-8_SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..236
FT /note="Syntaxin-8"
FT /id="PRO_0000210218"
FT TOPO_DOM 1..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..232
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..236
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 145..207
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 42..65
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
SQ SEQUENCE 236 AA; 26925 MW; EAE1D9D150C2EF2D CRC64;
MAPDPWFSTY DSTCQIAQEI AEKIQERNQC ERRGEKTPKL TLTIRTLLKN LKVKIDLLKD
LLLRAVSTRQ ITQLEGDRRQ NLLDDLVTRE RLLLASFKNE GAEPDLIRSS LMSEEAKRGT
PNPWLCEEPE ETRGLGFDEI RQQQQKIIQE QDAGLDALSS IISRQKQMGQ EIGNELDEQN
EIIDDLANLV ENTDEKLRTE ARRVTLVDRK STSCGMIMVI LLLLVAIVVV AVWPTN
