STX6_RAT
ID STX6_RAT Reviewed; 255 AA.
AC Q63635;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Syntaxin-6;
GN Name=Stx6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8663448; DOI=10.1074/jbc.271.30.17961;
RA Bock J.B., Lin R.C., Scheller R.H.;
RT "A new syntaxin family member implicated in targeting of intracellular
RT transport vesicles.";
RL J. Biol. Chem. 271:17961-17965(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [3]
RP INTERACTION WITH EEA1.
RX PubMed=10506127; DOI=10.1074/jbc.274.41.28857;
RA Simonsen A., Gaullier J.-M., D'Arrigo A., Stenmark H.;
RT "The Rab5 effector EEA1 interacts directly with syntaxin-6.";
RL J. Biol. Chem. 274:28857-28860(1999).
RN [4]
RP INTERACTION WITH MARCHF2.
RX PubMed=15689499; DOI=10.1091/mbc.e04-03-0216;
RA Nakamura N., Fukuda H., Kato A., Hirose S.;
RT "MARCH-II is a syntaxin-6-binding protein involved in endosomal
RT trafficking.";
RL Mol. Biol. Cell 16:1696-1710(2005).
RN [5]
RP INTERACTION WITH MARCHF3.
RX PubMed=16428329; DOI=10.1093/jb/mvj012;
RA Fukuda H., Nakamura N., Hirose S.;
RT "MARCH-III is a novel component of endosomes with properties similar to
RT those of MARCH-II.";
RL J. Biochem. 139:137-145(2006).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-110.
RX PubMed=12082176; DOI=10.1073/pnas.132274599;
RA Misura K.M., Bock J.B., Gonzalez L.C. Jr., Scheller R.H., Weis W.I.;
RT "Three-dimensional structure of the amino-terminal domain of syntaxin 6, a
RT SNAP-25 C homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9184-9189(2002).
CC -!- FUNCTION: Involved in intracellular vesicle trafficking.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and
CC VTI1A (By similarity). Binds EEA1 (PubMed:10506127). Interacts with
CC VPS45A and GOPC (By similarity). Interacts with MARCHF2; the
CC interaction promotes MARCHF2-mediated ubiquitination and degradation of
CC CFTR (PubMed:15689499). Interacts with MARCHF3 (PubMed:16428329).
CC Interacts with UHRF1BP1L (via C-terminal coiled-coil domain)
CC (PubMed:20163565). Interacts with BAIAP3; this interaction is increased
CC in the presence of calcium (By similarity).
CC {ECO:0000250|UniProtKB:O43752, ECO:0000250|UniProtKB:Q9JKK1,
CC ECO:0000269|PubMed:10506127, ECO:0000269|PubMed:15689499,
CC ECO:0000269|PubMed:16428329, ECO:0000269|PubMed:20163565}.
CC -!- INTERACTION:
CC Q63635; Q15075: EEA1; Xeno; NbExp=4; IntAct=EBI-398854, EBI-298113;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O43752}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with relatively higher expression
CC in brain, lung and kidney.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U56815; AAC52709.1; -; mRNA.
DR EMBL; BC081769; AAH81769.1; -; mRNA.
DR RefSeq; NP_113853.1; NM_031665.2.
DR PDB; 1LVF; X-ray; 2.10 A; A/B=1-110.
DR PDBsum; 1LVF; -.
DR AlphaFoldDB; Q63635; -.
DR SMR; Q63635; -.
DR BioGRID; 248852; 3.
DR CORUM; Q63635; -.
DR IntAct; Q63635; 10.
DR MINT; Q63635; -.
DR STRING; 10116.ENSRNOP00000037536; -.
DR iPTMnet; Q63635; -.
DR PhosphoSitePlus; Q63635; -.
DR SwissPalm; Q63635; -.
DR jPOST; Q63635; -.
DR PaxDb; Q63635; -.
DR PRIDE; Q63635; -.
DR Ensembl; ENSRNOT00000099649; ENSRNOP00000080858; ENSRNOG00000003402.
DR GeneID; 60562; -.
DR KEGG; rno:60562; -.
DR CTD; 10228; -.
DR RGD; 61915; Stx6.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00940000157639; -.
DR HOGENOM; CLU_061883_1_0_1; -.
DR InParanoid; Q63635; -.
DR OMA; EHDPYRF; -.
DR OrthoDB; 1563292at2759; -.
DR PhylomeDB; Q63635; -.
DR TreeFam; TF313254; -.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR EvolutionaryTrace; Q63635; -.
DR PRO; PR:Q63635; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003402; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; Q63635; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA: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; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; IDA:SynGO.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:RGD.
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; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT CHAIN 2..255
FT /note="Syntaxin-6"
FT /id="PRO_0000210211"
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 REGION 2..112
FT /note="Interaction with UHRF1BP1L"
FT /evidence="ECO:0000269|PubMed:20163565"
FT COILED 41..74
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT HELIX 6..31
FT /evidence="ECO:0007829|PDB:1LVF"
FT HELIX 40..72
FT /evidence="ECO:0007829|PDB:1LVF"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1LVF"
FT HELIX 82..108
FT /evidence="ECO:0007829|PDB:1LVF"
SQ SEQUENCE 255 AA; 29057 MW; D725FB12C1DCCA74 CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQGPSAATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQIVR DMKDQMSASS VQALAERKNR
QALLGDSSSQ NWDAGVTDRY GRLDRELQLA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LDDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLLVVLT LFLVL
