STX6_MOUSE
ID STX6_MOUSE Reviewed; 255 AA.
AC Q9JKK1; Q9D3A1; Q9D729;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Syntaxin-6;
GN Name=Stx6;
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 Low D.Y.H., Tang B.L., Hong W.;
RT "Mouse syntaxin 6.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Testis, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [4]
RP IDENTIFICATION IN SNARE COMPLEX WITH VTI1A, AND SUBCELLULAR LOCATION.
RX PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment
RT protein receptor (Vti1-rp2) implicated in protein trafficking in the
RT secretory pathway.";
RL J. Biol. Chem. 273:21783-21789(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: Involved in intracellular vesicle trafficking.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12 and VAMP4 (By
CC similarity). This complex also includes VTI1A (PubMed:9705316). Binds
CC EEA1 (By similarity). Interacts with VPS45A and GOPC (By similarity).
CC Interacts with MARCHF2; the interaction promotes MARCHF2-mediated
CC ubiquitination and degradation of CFTR (By similarity). Interacts with
CC MARCHF3 (By similarity). Interacts with UHRF1BP1L (via C-terminal
CC coiled-coil domain) (By similarity). Interacts with BAIAP3; this
CC interaction is increased in the presence of calcium (By similarity).
CC {ECO:0000250|UniProtKB:O43752, ECO:0000250|UniProtKB:Q63635,
CC ECO:0000269|PubMed:9705316}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O43752}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JKK1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKK1-2; Sequence=VSP_016138;
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF237814; AAF40221.1; -; mRNA.
DR EMBL; AK009690; BAB26441.1; -; mRNA.
DR EMBL; AK019106; BAB31549.1; -; mRNA.
DR EMBL; AK031673; BAC27505.1; -; mRNA.
DR EMBL; AK044905; BAC32135.1; -; mRNA.
DR EMBL; AK049124; BAC33556.1; -; mRNA.
DR EMBL; BC029205; AAH29205.1; -; mRNA.
DR CCDS; CCDS35741.1; -. [Q9JKK1-1]
DR RefSeq; NP_067408.1; NM_021433.3. [Q9JKK1-1]
DR AlphaFoldDB; Q9JKK1; -.
DR SMR; Q9JKK1; -.
DR BioGRID; 208415; 11.
DR CORUM; Q9JKK1; -.
DR IntAct; Q9JKK1; 4.
DR MINT; Q9JKK1; -.
DR STRING; 10090.ENSMUSP00000027743; -.
DR iPTMnet; Q9JKK1; -.
DR PhosphoSitePlus; Q9JKK1; -.
DR SwissPalm; Q9JKK1; -.
DR EPD; Q9JKK1; -.
DR jPOST; Q9JKK1; -.
DR MaxQB; Q9JKK1; -.
DR PaxDb; Q9JKK1; -.
DR PRIDE; Q9JKK1; -.
DR ProteomicsDB; 258769; -. [Q9JKK1-1]
DR ProteomicsDB; 258770; -. [Q9JKK1-2]
DR Antibodypedia; 34430; 304 antibodies from 38 providers.
DR DNASU; 58244; -.
DR Ensembl; ENSMUST00000027743; ENSMUSP00000027743; ENSMUSG00000026470. [Q9JKK1-1]
DR Ensembl; ENSMUST00000195302; ENSMUSP00000142089; ENSMUSG00000026470. [Q9JKK1-2]
DR GeneID; 58244; -.
DR KEGG; mmu:58244; -.
DR UCSC; uc007dbb.1; mouse. [Q9JKK1-1]
DR UCSC; uc007dbc.1; mouse. [Q9JKK1-2]
DR CTD; 10228; -.
DR MGI; MGI:1926235; Stx6.
DR VEuPathDB; HostDB:ENSMUSG00000026470; -.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00940000157639; -.
DR HOGENOM; CLU_061883_1_0_1; -.
DR InParanoid; Q9JKK1; -.
DR OMA; EHDPYRF; -.
DR OrthoDB; 1563292at2759; -.
DR PhylomeDB; Q9JKK1; -.
DR TreeFam; TF313254; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 58244; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Stx6; mouse.
DR PRO; PR:Q9JKK1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JKK1; protein.
DR Bgee; ENSMUSG00000026470; Expressed in external carotid artery and 250 other tissues.
DR ExpressionAtlas; Q9JKK1; baseline and differential.
DR Genevisible; Q9JKK1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IMP:AgBase.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:MGI.
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:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:MGI.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO:MGI.
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:AgBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; 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 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 Acetylation; Alternative splicing; 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_0000210209"
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:0000250|UniProtKB:O43752"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
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 VAR_SEQ 231..255
FT /note="DRRQWCAIAILFAVLVVVLILFLVL -> GNDVRQVKIQYLLFIWRLLPGER
FT KT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016138"
SQ SEQUENCE 255 AA; 28997 MW; 2CD91C02D23D28DE CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQGPSAATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQIVR DMKDQMSASS VQALAERKNR
QALLGDSSSQ SWNAGVADRY GRLDRELQLA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LDDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLVVVLI LFLVL
