STX6_HUMAN
ID STX6_HUMAN Reviewed; 255 AA.
AC O43752; B2R652; B4DR17; Q5VY08; Q6FH83;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Syntaxin-6;
GN Name=STX6;
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] (ISOFORM 1).
RX PubMed=10080545; DOI=10.1002/jlb.65.3.397;
RA Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.;
RT "Co-expression of several human syntaxin genes in neutrophils and
RT differentiating HL-60 cells: variant isoforms and detection of syntaxin
RT 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOPC.
RX PubMed=11384996; DOI=10.1074/jbc.m104137200;
RA Charest A., Lane K., McMahon K., Housman D.E.;
RT "Association of a novel PDZ domain-containing peripheral Golgi protein with
RT the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF)
RT attachment protein receptor) protein syntaxin 6.";
RL J. Biol. Chem. 276:29456-29465(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP INTERACTION WITH UHRF1BP1L.
RX PubMed=20163565; DOI=10.1111/j.1600-0854.2010.01049.x;
RA Otto G.P., Razi M., Morvan J., Stenner F., Tooze S.A.;
RT "A novel syntaxin 6-interacting protein, SHIP164, regulates syntaxin 6-
RT dependent sorting from early endosomes.";
RL Traffic 11:688-705(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP INTERACTION WITH MARCHF2, AND SUBCELLULAR LOCATION.
RX PubMed=23818989; DOI=10.1371/journal.pone.0068001;
RA Cheng J., Guggino W.;
RT "Ubiquitination and degradation of CFTR by the E3 ubiquitin ligase MARCH2
RT through its association with adaptor proteins CAL and STX6.";
RL PLoS ONE 8:e68001-e68001(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INTERACTION WITH BAIAP3.
RX PubMed=28626000; DOI=10.1083/jcb.201702099;
RA Zhang X., Jiang S., Mitok K.A., Li L., Attie A.D., Martin T.F.J.;
RT "BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-
RT core vesicles in neuroendocrine cells.";
RL J. Cell Biol. 216:2151-2166(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH STX12;
RP VTI1A AND VAMP4, AND SUBUNIT.
RX PubMed=17159904; DOI=10.1038/sj.emboj.7601467;
RA Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C.,
RA Jahn R.;
RT "Early endosomal SNAREs form a structurally conserved SNARE complex and
RT fuse liposomes with multiple topologies.";
RL EMBO J. 26:9-18(2007).
CC -!- FUNCTION: Involved in intracellular vesicle trafficking.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and
CC VTI1A (PubMed:17159904). Binds EEA1 (By similarity). Interacts with
CC VPS45A (By similarity). Interacts with MARCHF2; the interaction
CC promotes MARCHF2-mediated ubiquitination and degradation of CFTR
CC (PubMed:23818989). Interacts with MARCHF3 (By similarity). Interacts
CC with GOPC (PubMed:11384996). Interacts with UHRF1BP1L (via C-terminal
CC coiled-coil domain) (PubMed:20163565). Interacts with BAIAP3; this
CC interaction is increased in the presence of calcium (PubMed:28626000).
CC {ECO:0000250|UniProtKB:Q63635, ECO:0000250|UniProtKB:Q9JKK1,
CC ECO:0000269|PubMed:11384996, ECO:0000269|PubMed:17159904,
CC ECO:0000269|PubMed:20163565, ECO:0000269|PubMed:23818989,
CC ECO:0000269|PubMed:28626000}.
CC -!- INTERACTION:
CC O43752; P05067: APP; NbExp=3; IntAct=EBI-2695795, EBI-77613;
CC O43752; Q13520: AQP6; NbExp=3; IntAct=EBI-2695795, EBI-13059134;
CC O43752; Q8IUR7-6: ARMC8; NbExp=3; IntAct=EBI-2695795, EBI-11942961;
CC O43752; Q15125: EBP; NbExp=3; IntAct=EBI-2695795, EBI-3915253;
CC O43752; P00533: EGFR; NbExp=3; IntAct=EBI-2695795, EBI-297353;
CC O43752; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-2695795, EBI-18938272;
CC O43752; O14653: GOSR2; NbExp=3; IntAct=EBI-2695795, EBI-4401517;
CC O43752; Q9H400: LIME1; NbExp=3; IntAct=EBI-2695795, EBI-2830566;
CC O43752; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2695795, EBI-16439278;
CC O43752; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2695795, EBI-6163737;
CC O43752; Q49AM1: MTERF2; NbExp=3; IntAct=EBI-2695795, EBI-17857560;
CC O43752; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2695795, EBI-3923617;
CC O43752; Q9H115: NAPB; NbExp=4; IntAct=EBI-2695795, EBI-3921185;
CC O43752; P25788: PSMA3; NbExp=3; IntAct=EBI-2695795, EBI-348380;
CC O43752; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2695795, EBI-17247926;
CC O43752; O95721: SNAP29; NbExp=3; IntAct=EBI-2695795, EBI-490676;
CC O43752; P27105: STOM; NbExp=3; IntAct=EBI-2695795, EBI-1211440;
CC O43752; Q16623: STX1A; NbExp=3; IntAct=EBI-2695795, EBI-712466;
CC O43752; P32856-2: STX2; NbExp=3; IntAct=EBI-2695795, EBI-11956649;
CC O43752; Q12846: STX4; NbExp=8; IntAct=EBI-2695795, EBI-744942;
CC O43752; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2695795, EBI-6268651;
CC O43752; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2695795, EBI-8638294;
CC O43752; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-2695795, EBI-6269551;
CC O43752; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2695795, EBI-2548832;
CC O43752; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-2695795, EBI-723976;
CC O43752; O75379: VAMP4; NbExp=2; IntAct=EBI-2695795, EBI-744953;
CC O43752; Q9UID3-1: VPS51; NbExp=8; IntAct=EBI-2695795, EBI-16067837;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23818989}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43752-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43752-2; Sequence=VSP_054763;
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AJ002078; CAA05177.1; -; mRNA.
DR EMBL; CR541856; CAG46654.1; -; mRNA.
DR EMBL; CR541873; CAG46671.1; -; mRNA.
DR EMBL; AK299063; BAG61129.1; -; mRNA.
DR EMBL; AK312440; BAG35349.1; -; mRNA.
DR EMBL; AL356267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91091.1; -; Genomic_DNA.
DR EMBL; BC009944; AAH09944.1; -; mRNA.
DR CCDS; CCDS1341.1; -. [O43752-1]
DR CCDS; CCDS65738.1; -. [O43752-2]
DR RefSeq; NP_001273139.1; NM_001286210.1. [O43752-2]
DR RefSeq; NP_005810.1; NM_005819.5. [O43752-1]
DR RefSeq; XP_016855496.1; XM_017000007.1. [O43752-2]
DR PDB; 2NPS; X-ray; 2.50 A; D=169-234.
DR PDB; 4J2C; X-ray; 1.80 A; A/C=3-110.
DR PDBsum; 2NPS; -.
DR PDBsum; 4J2C; -.
DR AlphaFoldDB; O43752; -.
DR SMR; O43752; -.
DR BioGRID; 115522; 441.
DR CORUM; O43752; -.
DR DIP; DIP-44224N; -.
DR IntAct; O43752; 81.
DR MINT; O43752; -.
DR STRING; 9606.ENSP00000258301; -.
DR TCDB; 1.F.1.1.5; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; O43752; -.
DR PhosphoSitePlus; O43752; -.
DR SwissPalm; O43752; -.
DR BioMuta; STX6; -.
DR EPD; O43752; -.
DR jPOST; O43752; -.
DR MassIVE; O43752; -.
DR MaxQB; O43752; -.
DR PaxDb; O43752; -.
DR PeptideAtlas; O43752; -.
DR PRIDE; O43752; -.
DR ProteomicsDB; 49149; -. [O43752-1]
DR ProteomicsDB; 4918; -.
DR Antibodypedia; 34430; 304 antibodies from 38 providers.
DR DNASU; 10228; -.
DR Ensembl; ENST00000258301.6; ENSP00000258301.5; ENSG00000135823.14. [O43752-1]
DR Ensembl; ENST00000542060.5; ENSP00000440188.1; ENSG00000135823.14. [O43752-2]
DR GeneID; 10228; -.
DR KEGG; hsa:10228; -.
DR MANE-Select; ENST00000258301.6; ENSP00000258301.5; NM_005819.6; NP_005810.1.
DR UCSC; uc010pnr.4; human. [O43752-1]
DR CTD; 10228; -.
DR DisGeNET; 10228; -.
DR GeneCards; STX6; -.
DR HGNC; HGNC:11441; STX6.
DR HPA; ENSG00000135823; Low tissue specificity.
DR MIM; 603944; gene.
DR neXtProt; NX_O43752; -.
DR OpenTargets; ENSG00000135823; -.
DR PharmGKB; PA36238; -.
DR VEuPathDB; HostDB:ENSG00000135823; -.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00940000157639; -.
DR HOGENOM; CLU_061883_2_1_1; -.
DR InParanoid; O43752; -.
DR OMA; EHDPYRF; -.
DR OrthoDB; 1563292at2759; -.
DR PhylomeDB; O43752; -.
DR TreeFam; TF313254; -.
DR PathwayCommons; O43752; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; O43752; -.
DR BioGRID-ORCS; 10228; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; STX6; human.
DR EvolutionaryTrace; O43752; -.
DR GeneWiki; STX6; -.
DR GenomeRNAi; 10228; -.
DR Pharos; O43752; Tbio.
DR PRO; PR:O43752; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43752; protein.
DR Bgee; ENSG00000135823; Expressed in secondary oocyte and 189 other tissues.
DR Genevisible; O43752; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:BHF-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:MGI.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; IEA:Ensembl.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IPI:UniProtKB.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF09177; Syntaxin-6_N; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..255
FT /note="Syntaxin-6"
FT /id="PRO_0000210208"
FT TOPO_DOM 2..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 163..225
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 41..74
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054763"
FT CONFLICT 77
FT /note="K -> R (in Ref. 2; CAG46654)"
FT /evidence="ECO:0000305"
FT HELIX 7..33
FT /evidence="ECO:0007829|PDB:4J2C"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4J2C"
FT HELIX 40..73
FT /evidence="ECO:0007829|PDB:4J2C"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:4J2C"
FT HELIX 82..107
FT /evidence="ECO:0007829|PDB:4J2C"
FT HELIX 173..229
FT /evidence="ECO:0007829|PDB:2NPS"
SQ SEQUENCE 255 AA; 29176 MW; CC05C025DE1FE89E CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR DMKDQMSTSS VQALAERKNR
QALLGDSGSQ NWSTGTTDKY GRLDRELQRA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLLVVLI LFLVL
