STX12_RAT
ID STX12_RAT Reviewed; 274 AA.
AC G3V7P1; O70319; O88385;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Syntaxin-12;
DE AltName: Full=Syntaxin-13;
GN Name=Stx12; Synonyms=Stx13;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NAPA AND SNAP23, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9507000; DOI=10.1074/jbc.273.12.6944;
RA Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.;
RT "Syntaxin 12, a member of the syntaxin family localized to the endosome.";
RL J. Biol. Chem. 273:6944-6950(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
RA Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R.,
RA Yoo J.-S., Scheller R.H.;
RT "Seven novel mammalian SNARE proteins localize to distinct membrane
RT compartments.";
RL J. Biol. Chem. 273:10317-10324(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP COMPLEX FORMATION WITH GRIP1; GRIA2 AND NSG1, AND FUNCTION.
RX PubMed=16037816; DOI=10.1038/sj.emboj.7600755;
RA Steiner P., Alberi S., Kulangara K., Yersin A., Sarria J.C., Regulier E.,
RA Kasas S., Dietler G., Muller D., Catsicas S., Hirling H.;
RT "Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and
RT recycling of the glutamate receptor subunit GluR2.";
RL EMBO J. 24:2873-2884(2005).
RN [7]
RP INTERACTION WITH GRIPAP1, AND SUBCELLULAR LOCATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 184-251 N COMPLEX WITH STX6; VTI1A
RP AND VAMP4, FUNCTION, AND SUBUNIT.
RX PubMed=17159904; DOI=10.1038/sj.emboj.7601467;
RA Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C.,
RA Jahn R.;
RT "Early endosomal SNAREs form a structurally conserved SNARE complex and
RT fuse liposomes with multiple topologies.";
RL EMBO J. 26:9-18(2007).
CC -!- FUNCTION: SNARE that acts to regulate protein transport between
CC endosomes and the trans-Golgi network (By similarity). The SNARE
CC complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion
CC (in vitro). 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
CC (PubMed:16037816). {ECO:0000250, ECO:0000269|PubMed:16037816,
CC ECO:0000269|PubMed:17159904}.
CC -!- SUBUNIT: Associates with the BLOC-1 complex. Interacts with BLOC1S6 (By
CC similarity). Interacts with NAPA and SNAP23 (PubMed:9507000).
CC Identified in a complex containing STX6, STX12, VAMP4 and VTI1A
CC (PubMed:17159904). Interacts with GRIPAP1 (PubMed:20098723). Forms a
CC complex with GRIP1, GRIA2 and NSG1; controls the intracellular fate of
CC AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling
CC and membrane targeting (PubMed:16037816). Interacts with NSG1
CC (PubMed:12070131). Interacts with TPC1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ER00, ECO:0000269|PubMed:12070131,
CC ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:17159904,
CC ECO:0000269|PubMed:20098723, ECO:0000269|PubMed:9507000}.
CC -!- INTERACTION:
CC G3V7P1; Q63666: Vamp1; NbExp=3; IntAct=EBI-915654, EBI-2029956;
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane
CC protein {ECO:0000269|PubMed:9553086}. Golgi apparatus membrane; Single-
CC pass type IV membrane protein {ECO:0000269|PubMed:9553086}.
CC Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC {ECO:0000269|PubMed:20098723}; Single-pass type IV membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:20098723, ECO:0000269|PubMed:9553086}; Single-pass
CC type IV membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain.
CC {ECO:0000269|PubMed:9507000, ECO:0000269|PubMed:9553086}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18967.1; Type=Frameshift; Evidence={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; AF035632; AAC23484.1; -; mRNA.
DR EMBL; AF044581; AAC18967.1; ALT_FRAME; mRNA.
DR EMBL; CH473968; EDL80653.1; -; Genomic_DNA.
DR RefSeq; NP_075228.2; NM_022939.2.
DR PDB; 2NPS; X-ray; 2.50 A; B=184-251.
DR PDBsum; 2NPS; -.
DR AlphaFoldDB; G3V7P1; -.
DR SMR; G3V7P1; -.
DR BioGRID; 249226; 4.
DR CORUM; G3V7P1; -.
DR IntAct; G3V7P1; 5.
DR MINT; G3V7P1; -.
DR STRING; 10116.ENSRNOP00000017227; -.
DR iPTMnet; G3V7P1; -.
DR PhosphoSitePlus; G3V7P1; -.
DR SwissPalm; G3V7P1; -.
DR jPOST; G3V7P1; -.
DR PaxDb; G3V7P1; -.
DR PRIDE; G3V7P1; -.
DR Ensembl; ENSRNOT00000017227; ENSRNOP00000017227; ENSRNOG00000011804.
DR GeneID; 65033; -.
DR KEGG; rno:65033; -.
DR UCSC; RGD:620977; rat.
DR CTD; 23673; -.
DR RGD; 620977; Stx12.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR InParanoid; G3V7P1; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; G3V7P1; -.
DR TreeFam; TF315607; -.
DR PRO; PR:G3V7P1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000011804; Expressed in stomach and 20 other tissues.
DR ExpressionAtlas; G3V7P1; baseline and differential.
DR Genevisible; G3V7P1; RN.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0000407; C:phagophore assembly site; ISO:RGD.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
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; IDA:SynGO.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
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:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; IDA:SynGO.
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 DisProt; DP01501; -.
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 3D-structure; Acetylation; 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:Q86Y82"
FT CHAIN 2..274
FT /note="Syntaxin-12"
FT /id="PRO_0000415499"
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..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..80
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:0000250|UniProtKB:Q9ER00"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER00"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER00"
FT CONFLICT 14..19
FT /note="PSGPQP -> RRSL (in Ref. 1; AAC23484)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="PQ -> LR (in Ref. 2; AAC18967)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="N -> S (in Ref. 1; AAC23484)"
FT /evidence="ECO:0000305"
FT HELIX 184..245
FT /evidence="ECO:0007829|PDB:2NPS"
SQ SEQUENCE 274 AA; 31187 MW; D5D551B57776E195 CRC64;
MSYGPLDMYR NPGPSGPQPR DFNSIIQTCS GNIQRISQAT AQIKNLMSQL GTKQDSSKLQ
ENLQQFQHST NQLAKETNEL LKELGSLPLP LSASEQRQQK LQKERLMNDF SSALNNFQVV
QRKVSEKEKE SIARARAGSR LSAEDRQREE QLVSFDSHEE WNQMQSQEEE AAITEQDLEL
IKERETAIQQ LEADILDVNQ IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERASDQLQRA
AYYQKKSRKK MCILVLVLSV IVTVLVVVIW VASK
