STX11_MOUSE
ID STX11_MOUSE Reviewed; 287 AA.
AC Q9D3G5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Syntaxin-11;
GN Name=Stx11;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: SNARE that acts to regulate protein transport between late
CC endosomes and the trans-Golgi network. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SNARE proteins SNAP-23 and VAMP.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AK017897; BAB30994.1; -; mRNA.
DR CCDS; CCDS48500.1; -.
DR RefSeq; NP_083351.1; NM_029075.1.
DR AlphaFoldDB; Q9D3G5; -.
DR SMR; Q9D3G5; -.
DR IntAct; Q9D3G5; 1.
DR STRING; 10090.ENSMUSP00000046243; -.
DR iPTMnet; Q9D3G5; -.
DR PhosphoSitePlus; Q9D3G5; -.
DR SwissPalm; Q9D3G5; -.
DR EPD; Q9D3G5; -.
DR MaxQB; Q9D3G5; -.
DR PaxDb; Q9D3G5; -.
DR PRIDE; Q9D3G5; -.
DR ProteomicsDB; 254606; -.
DR GeneID; 74732; -.
DR KEGG; mmu:74732; -.
DR CTD; 8676; -.
DR MGI; MGI:1921982; Stx11.
DR eggNOG; KOG0810; Eukaryota.
DR InParanoid; Q9D3G5; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q9D3G5; -.
DR BioGRID-ORCS; 74732; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q9D3G5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D3G5; protein.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0043316; P:cytotoxic T cell degranulation; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0043320; P:natural killer cell degranulation; IMP:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0043312; P:neutrophil degranulation; IMP:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd15878; SNARE_syntaxin11; 1.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028672; STX11.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR042781; Syntaxin11_SNARE.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF30; PTHR19957:SF30; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 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 Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..287
FT /note="Syntaxin-11"
FT /id="PRO_0000210222"
FT DOMAIN 204..266
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 41..71
FT /evidence="ECO:0000255"
SQ SEQUENCE 287 AA; 33369 MW; FD5D10842B7C5415 CRC64;
MKDRLAELQE LSRSYDQQFP DGDNDFDAPR EDIVFETDNI LESLYRVIQD IQDENQLLLI
DVRRLGRQNV RFLTSMRRLS SIKRDTNSIA KAIKTRGEGI HQKLRSMKEL SEQAEARHGA
HSAVARISHA QYSALARAFQ QAMYEYNQAE MKQRDNCKIR IQRQLEIMGK DMSGEQIEDM
FEQGKWDVFS ENLLADLKGA RAALNEIESR HRELLRLEGR IRDVHELFLQ MAVLVEKQED
TLNVIELNVQ KTLDYTGEAK AQVRKAVQYK KKNPCRTICC FCCPCVN
