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   08-NOV-2023, entry version 130.
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; 10090-ENSMUSP00000046243; -.
DR   ProteomicsDB; 254606; -.
DR   Pumba; Q9D3G5; -.
DR   GeneID; 74732; -.
DR   KEGG; mmu:74732; -.
DR   AGR; MGI:1921982; -.
DR   CTD; 8676; -.
DR   MGI; MGI:1921982; Stx11.
DR   eggNOG; KOG0810; Eukaryota.
DR   InParanoid; Q9D3G5; -.
DR   OrthoDB; 2879355at2759; -.
DR   PhylomeDB; Q9D3G5; -.
DR   BioGRID-ORCS; 74732; 4 hits in 75 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: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 type II interferon; 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   CDD; cd15878; SNARE_syntaxin11; 1.
DR   CDD; cd00179; SynN; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
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; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF30; SYNTAXIN-11; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 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
//