Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Syntaxin-12

Gene

Stx12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

SNARE that acts to regulate protein transport between endosomes and the trans-Golgi network (By similarity). The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-12
Alternative name(s):
Syntaxin-13
Gene namesi
Name:Stx12
Synonyms:Stx13
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620977. Stx12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 250249CytoplasmicSequence analysisAdd
BLAST
Transmembranei251 – 27121Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini272 – 2743VesicularSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 274273Syntaxin-12PRO_0000415499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei142 – 1421PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineBy similarity
Modified residuei225 – 2251PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiG3V7P1.
PRIDEiG3V7P1.

PTM databases

iPTMnetiG3V7P1.
PhosphoSiteiG3V7P1.
SwissPalmiG3V7P1.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in brain.2 Publications

Gene expression databases

ExpressionAtlasiG3V7P1. baseline and differential.
GenevisibleiG3V7P1. RN.

Interactioni

Subunit structurei

Associates with the BLOC-1 complex. Interacts with BLOC1S6 (By similarity). Interacts with NAPA and SNAP23. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Vamp1Q636663EBI-915654,EBI-2029956

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249226. 1 interaction.
IntActiG3V7P1. 5 interactions.
MINTiMINT-5023130.
STRINGi10116.ENSRNOP00000017227.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 24562Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPSX-ray2.50B184-251[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 24063t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili34 – 8047Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0811. Eukaryota.
COG5325. LUCA.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiG3V7P1.
KOiK13813.
OMAiQMQSQEE.
OrthoDBiEOG7B31PS.
PhylomeDBiG3V7P1.
TreeFamiTF315607.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

G3V7P1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYGPLDMYR NPGPSGPQPR DFNSIIQTCS GNIQRISQAT AQIKNLMSQL
60 70 80 90 100
GTKQDSSKLQ ENLQQFQHST NQLAKETNEL LKELGSLPLP LSASEQRQQK
110 120 130 140 150
LQKERLMNDF SSALNNFQVV QRKVSEKEKE SIARARAGSR LSAEDRQREE
160 170 180 190 200
QLVSFDSHEE WNQMQSQEEE AAITEQDLEL IKERETAIQQ LEADILDVNQ
210 220 230 240 250
IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERASDQLQRA AYYQKKSRKK
260 270
MCILVLVLSV IVTVLVVVIW VASK
Length:274
Mass (Da):31,187
Last modified:November 16, 2011 - v1
Checksum:iD5D551B57776E195
GO

Sequence cautioni

The sequence AAC18967.1 differs from that shown. Reason: Frameshift at position 2. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 196PSGPQP → RRSL in AAC23484 (PubMed:9507000).Curated
Sequence conflicti17 – 182PQ → LR in AAC18967 (PubMed:9553086).Curated
Sequence conflicti23 – 231N → S in AAC23484 (PubMed:9507000).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035632 mRNA. Translation: AAC23484.1.
AF044581 mRNA. Translation: AAC18967.1. Frameshift.
CH473968 Genomic DNA. Translation: EDL80653.1.
RefSeqiNP_075228.2. NM_022939.2.
UniGeneiRn.54570.

Genome annotation databases

EnsembliENSRNOT00000017227; ENSRNOP00000017227; ENSRNOG00000011804.
GeneIDi65033.
KEGGirno:65033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035632 mRNA. Translation: AAC23484.1.
AF044581 mRNA. Translation: AAC18967.1. Frameshift.
CH473968 Genomic DNA. Translation: EDL80653.1.
RefSeqiNP_075228.2. NM_022939.2.
UniGeneiRn.54570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPSX-ray2.50B184-251[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249226. 1 interaction.
IntActiG3V7P1. 5 interactions.
MINTiMINT-5023130.
STRINGi10116.ENSRNOP00000017227.

PTM databases

iPTMnetiG3V7P1.
PhosphoSiteiG3V7P1.
SwissPalmiG3V7P1.

Proteomic databases

PaxDbiG3V7P1.
PRIDEiG3V7P1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017227; ENSRNOP00000017227; ENSRNOG00000011804.
GeneIDi65033.
KEGGirno:65033.

Organism-specific databases

CTDi23673.
RGDi620977. Stx12.

Phylogenomic databases

eggNOGiKOG0811. Eukaryota.
COG5325. LUCA.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiG3V7P1.
KOiK13813.
OMAiQMQSQEE.
OrthoDBiEOG7B31PS.
PhylomeDBiG3V7P1.
TreeFamiTF315607.

Miscellaneous databases

PROiG3V7P1.

Gene expression databases

ExpressionAtlasiG3V7P1. baseline and differential.
GenevisibleiG3V7P1. RN.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Syntaxin 12, a member of the syntaxin family localized to the endosome."
    Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.
    J. Biol. Chem. 273:6944-6950(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH WITH NAPA AND SNAP23, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Seven novel mammalian SNARE proteins localize to distinct membrane compartments."
    Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R., Yoo J.-S., Scheller R.H.
    J. Biol. Chem. 273:10317-10324(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies."
    Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C., Jahn R.
    EMBO J. 26:9-18(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 184-251 N COMPLEX WITH STX6; VTI1A AND VAMP4, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiSTX12_RAT
AccessioniPrimary (citable) accession number: G3V7P1
Secondary accession number(s): O70319, O88385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: November 16, 2011
Last modified: July 6, 2016
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.