STX12_MOUSE
ID STX12_MOUSE Reviewed; 274 AA.
AC Q9ER00; Q3UIV9; Q921T9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Syntaxin-12;
GN Name=Stx12;
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].
RC STRAIN=C57BL/6J;
RA Nakamura N., Wada Y., Futai M.;
RT "Mouse syntaxin12.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Cecum, and Kidney;
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].
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 INTERACTION WITH NSG1.
RX PubMed=12070131; DOI=10.1083/jcb.200202022;
RA Steiner P., Sarria J.C., Glauser L., Magnin S., Catsicas S., Hirling H.;
RT "Modulation of receptor cycling by neuron-enriched endosomal protein of 21
RT kD.";
RL J. Cell Biol. 157:1197-1209(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; SER-142; SER-218 AND
RP SER-225, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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 [7]
RP INTERACTION WITH GRIPAP1.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
RN [8]
RP INTERACTION WITH TPC1.
RX PubMed=28855648; DOI=10.1038/s41598-017-10607-4;
RA Castonguay J., Orth J.H.C., Mueller T., Sleman F., Grimm C.,
RA Wahl-Schott C., Biel M., Mallmann R.T., Bildl W., Schulte U., Klugbauer N.;
RT "The two-pore channel TPC1 is required for efficient protein processing
RT through early and recycling endosomes.";
RL Sci. Rep. 7:10038-10038(2017).
CC -!- FUNCTION: SNARE that acts to regulate protein transport between late
CC endosomes and the trans-Golgi network. The SNARE complex containing
CC STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By
CC similarity). Through complex formation with GRIP1, GRIA2 and NSG1
CC controls the intracellular fate of AMPAR and the endosomal sorting of
CC the GRIA2 subunit toward recycling and membrane targeting (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:G3V7P1}.
CC -!- SUBUNIT: Associates with the BLOC-1 complex. Interacts with BLOC1S6.
CC Interacts with NAPA and SNAP23. Identified in a complex containing
CC STX6, STX12, VAMP4 and VTI1A (By similarity). Interacts with GRIPAP1
CC (PubMed:20098723). Forms a complex with GRIP1, GRIA2 and NSG1; controls
CC the intracellular fate of AMPAR and the endosomal sorting of the GRIA2
CC subunit toward recycling and membrane targeting (By similarity).
CC Interacts with NSG1 (PubMed:12070131). Interacts with TPC1
CC (PubMed:28855648). {ECO:0000250, ECO:0000250|UniProtKB:G3V7P1,
CC ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:20098723,
CC ECO:0000269|PubMed:28855648}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane
CC protein {ECO:0000250|UniProtKB:G3V7P1}. Golgi apparatus membrane;
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}.
CC Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:G3V7P1}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AB019211; BAB20282.1; -; mRNA.
DR EMBL; AK077678; BAC36951.1; -; mRNA.
DR EMBL; AK078948; BAC37473.1; -; mRNA.
DR EMBL; AK146544; BAE27249.1; -; mRNA.
DR EMBL; AK146735; BAE27397.1; -; mRNA.
DR EMBL; AK167087; BAE39244.1; -; mRNA.
DR EMBL; BC010669; AAH10669.1; -; mRNA.
DR CCDS; CCDS18737.1; -.
DR RefSeq; NP_598648.1; NM_133887.4.
DR AlphaFoldDB; Q9ER00; -.
DR SMR; Q9ER00; -.
DR BioGRID; 221409; 18.
DR IntAct; Q9ER00; 6.
DR STRING; 10090.ENSMUSP00000030698; -.
DR iPTMnet; Q9ER00; -.
DR PhosphoSitePlus; Q9ER00; -.
DR SwissPalm; Q9ER00; -.
DR EPD; Q9ER00; -.
DR jPOST; Q9ER00; -.
DR MaxQB; Q9ER00; -.
DR PaxDb; Q9ER00; -.
DR PeptideAtlas; Q9ER00; -.
DR PRIDE; Q9ER00; -.
DR ProteomicsDB; 254607; -.
DR Antibodypedia; 30837; 193 antibodies from 28 providers.
DR DNASU; 100226; -.
DR Ensembl; ENSMUST00000030698; ENSMUSP00000030698; ENSMUSG00000028879.
DR GeneID; 100226; -.
DR KEGG; mmu:100226; -.
DR UCSC; uc008vbx.1; mouse.
DR CTD; 23673; -.
DR MGI; MGI:1931027; Stx12.
DR VEuPathDB; HostDB:ENSMUSG00000028879; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_059257_1_1_1; -.
DR InParanoid; Q9ER00; -.
DR OMA; EHRQKLH; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; Q9ER00; -.
DR TreeFam; TF315607; -.
DR BioGRID-ORCS; 100226; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Stx12; mouse.
DR PRO; PR:Q9ER00; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9ER00; protein.
DR Bgee; ENSMUSG00000028879; Expressed in urinary bladder urothelium and 269 other tissues.
DR Genevisible; Q9ER00; MM.
DR GO; GO:0031083; C:BLOC-1 complex; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR GO; GO:0000407; C:phagophore assembly site; ISO:MGI.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO: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:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; 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; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF14523; Syntaxin_2; 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 Acetylation; Coiled coil; Endosome; 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:Q86Y82"
FT CHAIN 2..274
FT /note="Syntaxin-12"
FT /id="PRO_0000210224"
FT TOPO_DOM 2..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..274
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 178..240
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..130
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y82"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 171
FT /note="A -> V (in Ref. 3; AAH10669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 31195 MW; 443A294A1A1E2905 CRC64;
MSYGPLDMYR NPGPSGPQPR DFNSIIQTCS GNIQRISQAT AQIKNLMSQL GTKQDSSKLQ
ENLQQLQHST NQLAKETNEL LKELGSLPLP LSASEQRQQK LQKERLMNDF SSALNNFQVV
QRKVSEKEKE SIARARAGSR LSAEDRQREE QLVSFDSHEE WNQMQSQEEE AAITEQDLEL
IKERETAIRQ LEADILDVNQ IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERATDQLQRA
AYYQKKSRKK MCILVLVLSV IVTVLVVVIW VASK
