STX12_PONAB
ID STX12_PONAB Reviewed; 276 AA.
AC Q5RBW6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Syntaxin-12;
GN Name=STX12;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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. Interacts with NSG1
CC (By similarity). Interacts with TPC1 (By similarity).
CC {ECO:0000250|UniProtKB:G3V7P1, ECO:0000250|UniProtKB:Q86Y82,
CC ECO:0000250|UniProtKB:Q9ER00}.
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; CR858517; CAH90744.1; -; mRNA.
DR RefSeq; NP_001125416.1; NM_001131944.1.
DR AlphaFoldDB; Q5RBW6; -.
DR SMR; Q5RBW6; -.
DR STRING; 9601.ENSPPYP00000001911; -.
DR GeneID; 100172323; -.
DR KEGG; pon:100172323; -.
DR CTD; 23673; -.
DR eggNOG; KOG0811; Eukaryota.
DR InParanoid; Q5RBW6; -.
DR OrthoDB; 1204812at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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 2: Evidence at transcript 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..276
FT /note="Syntaxin-12"
FT /id="PRO_0000210225"
FT TOPO_DOM 2..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..276
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 COILED 33..131
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:0000250|UniProtKB:Q86Y82"
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"
SQ SEQUENCE 276 AA; 31588 MW; B021386C95F8FAD1 CRC64;
MSYGPLDMYR NPGPSGPQLR DFSSIIQTCS GNIQRISQAT AQIKNSMSQL GTKQDSSKLQ
ENLQQLQHST NQLAKETNEL LKELGSLPLP LSTSEQRQQR LQKERLMNDF SAALNNFQAV
QRRVSEKEKE SIARARAGSR LSAEERQREE QLVSFDSHEE WNQMQSQDDE VAITEQDLEL
IKERETAIRQ LEADILDVNQ IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERATEQLQRA
AYYQKKSRKK MCILVLVLSV IIVILGLIIW LVYKTK
