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 27-MAR-2024, entry version 161. 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, RC 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 [6] RP INTERACTION WITH BLTP3B. RX PubMed=35499567; DOI=10.1083/jcb.202111018; RA Hanna M.G., Suen P.H., Wu Y., Reinisch K.M., De Camilli P.; RT "SHIP164 is a chorein motif lipid transfer protein that controls endosome- RT Golgi membrane traffic."; RL J. Cell Biol. 221:0-0(2022). CC -!- FUNCTION: SNARE promoting movement of transport vesicles to target CC membranes. Targets endosomes to the trans-Golgi network, and may CC therefore function in retrograde trafficking. Together with SNARE CC STX12, promotes movement of vesicles from endosomes to the cell CC membrane, and may therefore function in the endocytic recycling CC pathway. {ECO:0000250|UniProtKB:Q63635}. 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 BLTP3B (via C-terminal coiled- CC coil domain) (PubMed:35499567). Interacts with BAIAP3; this interaction CC is increased in the presence of calcium (By similarity). Interacts with CC VPS13B (By similarity). {ECO:0000250|UniProtKB:O43752, CC ECO:0000250|UniProtKB:Q63635, ECO:0000269|PubMed:35499567, 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}. Golgi apparatus, trans-Golgi network membrane CC {ECO:0000250|UniProtKB:Q63635}; Single-pass type IV membrane protein CC {ECO:0000255}. Recycling endosome membrane CC {ECO:0000250|UniProtKB:Q63635}; Single-pass type IV membrane protein CC {ECO:0000255}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 12. 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; 10090-ENSMUSP00000027743; -. DR ProteomicsDB; 258769; -. [Q9JKK1-1] DR ProteomicsDB; 258770; -. [Q9JKK1-2] DR Pumba; Q9JKK1; -. DR Antibodypedia; 34430; 330 antibodies from 38 providers. DR DNASU; 58244; -. DR Ensembl; ENSMUST00000027743.13; ENSMUSP00000027743.8; ENSMUSG00000026470.15. [Q9JKK1-1] DR Ensembl; ENSMUST00000195302.6; ENSMUSP00000142089.2; ENSMUSG00000026470.15. [Q9JKK1-2] DR GeneID; 58244; -. DR KEGG; mmu:58244; -. DR UCSC; uc007dbb.1; mouse. [Q9JKK1-1] DR UCSC; uc007dbc.1; mouse. [Q9JKK1-2] DR AGR; MGI:1926235; -. 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; 588552at2759; -. 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 79 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 254 other cell types or tissues. DR ExpressionAtlas; Q9JKK1; baseline and differential. 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: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; ISS:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031201; C:SNARE complex; ISO:MGI. DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; 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; ISS:UniProtKB. DR GO; GO:0007032; P:endosome organization; IMP: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; ISS:UniProtKB. 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 CDD; cd21447; SNARE_NTD_STX6; 1. DR CDD; cd15851; SNARE_Syntaxin6; 1. DR Gene3D; 1.20.5.110; -; 1. DR Gene3D; 1.20.58.90; -; 1. 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; SYNTAXIN; 1. DR PANTHER; PTHR19957:SF104; SYNTAXIN-6; 1. DR Pfam; PF05739; SNARE; 1. DR Pfam; PF09177; Syntaxin-6_N; 1. DR SMART; SM00397; t_SNARE; 1. DR SUPFAM; SSF58038; SNARE fusion complex; 1. DR SUPFAM; SSF47661; t-snare proteins; 1. DR PROSITE; PS00914; SYNTAXIN; 1. DR PROSITE; PS50192; T_SNARE; 1. DR Genevisible; Q9JKK1; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Endosome; Golgi apparatus; KW Membrane; Phosphoprotein; Protein transport; Reference proteome; KW Transmembrane; 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 REGION 2..168 FT /note="Required for interaction with VPS51" FT /evidence="ECO:0000250|UniProtKB:Q63635" 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 //