STX6_PONAB
ID STX6_PONAB Reviewed; 255 AA.
AC Q5R6Q2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Syntaxin-6;
GN Name=STX6;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in intracellular vesicle trafficking. {ECO:0000250}.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and
CC VTI1A. Binds EEA1. Interacts with VPS45A and GOPC. Interacts with
CC MARCHF2; the interaction promotes MARCHF2-mediated ubiquitination and
CC degradation of CFTR (By similarity). Interacts with MARCHF3 (By
CC similarity). Interacts with UHRF1BP1L (via C-terminal coiled-coil
CC domain). Interacts with BAIAP3; this interaction is increased in the
CC presence of calcium (By similarity). {ECO:0000250|UniProtKB:O43752,
CC ECO:0000250|UniProtKB:Q63635}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O43752}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; CR860434; CAH92558.1; -; mRNA.
DR RefSeq; NP_001126499.1; NM_001133027.1.
DR AlphaFoldDB; Q5R6Q2; -.
DR SMR; Q5R6Q2; -.
DR STRING; 9601.ENSPPYP00000000510; -.
DR PRIDE; Q5R6Q2; -.
DR Ensembl; ENSPPYT00000000531; ENSPPYP00000000510; ENSPPYG00000000446.
DR GeneID; 100173487; -.
DR KEGG; pon:100173487; -.
DR CTD; 10228; -.
DR eggNOG; KOG3202; Eukaryota.
DR GeneTree; ENSGT00940000157639; -.
DR InParanoid; Q5R6Q2; -.
DR OrthoDB; 1563292at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
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:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0090161; P:Golgi ribbon formation; IEA:Ensembl.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR DisProt; DP01500; -.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF09177; Syntaxin-6_N; 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; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT CHAIN 2..255
FT /note="Syntaxin-6"
FT /id="PRO_0000210210"
FT TOPO_DOM 2..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 163..225
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 46..72
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43752"
SQ SEQUENCE 255 AA; 29176 MW; CC05C025DE1FE89E CRC64;
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL RNNLRSIEWD
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR DMKDQMSTSS VQALAERKNR
QALLGDSGSQ NWSTGTTDKY GRLDRELQRA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
GVLKNMSQRI GGELEEQAVM LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
LFAVLLVVLI LFLVL