STX8_RAT
ID STX8_RAT Reviewed; 236 AA.
AC Q9Z2Q7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Syntaxin-8;
GN Name=Stx8;
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].
RC TISSUE=Brain;
RX PubMed=10683148; DOI=10.1242/jcs.113.6.997;
RA Subramaniam V.N., Loh E., Horstmann H., Habermann A., Xu Y., Coe J.,
RA Griffiths G., Hong W.;
RT "Preferential association of syntaxin 8 with the early endosome.";
RL J. Cell Sci. 113:997-1008(2000).
RN [2]
RP SNARE COMPLEX CHARACTERIZATION.
RX PubMed=11101518; DOI=10.1093/emboj/19.23.6453;
RA Antonin W., Holroyd C., Fasshauer D., Pabst S., Fischer von Mollard G.,
RA Jahn R.;
RT "A SNARE complex mediating fusion of late endosomes defines conserved
RT properties of SNARE structure and function.";
RL EMBO J. 19:6453-6464(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 149-209 IN COMPLEX WITH STX7;
RP VAMP8 AND VTI1B, AND INTERACTION WITH VAMP8.
RX PubMed=11786915; DOI=10.1038/nsb746;
RA Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.;
RT "Crystal structure of the endosomal SNARE complex reveals common structural
RT principles of all SNAREs.";
RL Nat. Struct. Biol. 9:107-111(2002).
RN [5]
RP SNARE COMPLEX CHARACTERIZATION.
RX PubMed=15133481; DOI=10.1038/sj.embor.7400150;
RA Pryor P.R., Mullock B.M., Bright N.A., Lindsay M.R., Gray S.R.,
RA Richardson S.C.W., Stewart A., James D.E., Piper R.C., Luzio J.P.;
RT "Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late
RT endocytic fusion events.";
RL EMBO Rep. 5:590-595(2004).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the early
CC secretory pathway, possibly by mediating retrograde transport from cis-
CC Golgi membranes to the ER.
CC -!- SUBUNIT: Part of the SNARE core complex containing STX7, VAMP8 and
CC VTI1B. Interacts with VAMP8. Forms a SNARE complex with STX7, VTI1B and
CC VAMP8 which functions in the homotypic fusion of late endosomes.
CC Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B
CC that is required for heterotypic fusion of late endosomes with
CC lysosomes. Interacts with HECTD3 (By similarity). Interacts with TPC1
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O88983}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.
CC Note=Preferentially associated with the early endosome. To a lesser
CC extent, also present in late endosome, the plasma membrane and coated
CC pits.
CC -!- TISSUE SPECIFICITY: Widely expressed in all tissues examined.
CC -!- PTM: Ubiquitinated by HECTD3. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF033109; AAC70903.1; -; mRNA.
DR RefSeq; NP_113844.1; NM_031656.2.
DR PDB; 1GL2; X-ray; 1.90 A; D=149-209.
DR PDBsum; 1GL2; -.
DR AlphaFoldDB; Q9Z2Q7; -.
DR SMR; Q9Z2Q7; -.
DR BioGRID; 248716; 3.
DR CORUM; Q9Z2Q7; -.
DR DIP; DIP-59284N; -.
DR IntAct; Q9Z2Q7; 1.
DR STRING; 10116.ENSRNOP00000005204; -.
DR iPTMnet; Q9Z2Q7; -.
DR PhosphoSitePlus; Q9Z2Q7; -.
DR SwissPalm; Q9Z2Q7; -.
DR PaxDb; Q9Z2Q7; -.
DR PRIDE; Q9Z2Q7; -.
DR GeneID; 59074; -.
DR KEGG; rno:59074; -.
DR UCSC; RGD:61917; rat.
DR CTD; 9482; -.
DR RGD; 61917; Stx8.
DR VEuPathDB; HostDB:ENSRNOG00000003849; -.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_099972_1_0_1; -.
DR InParanoid; Q9Z2Q7; -.
DR OMA; CGYWIVI; -.
DR OrthoDB; 1455798at2759; -.
DR PhylomeDB; Q9Z2Q7; -.
DR TreeFam; TF323262; -.
DR EvolutionaryTrace; Q9Z2Q7; -.
DR PRO; PR:Q9Z2Q7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003849; Expressed in stomach and 20 other tissues.
DR Genevisible; Q9Z2Q7; RN.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IDA:RGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0019869; F:chloride channel inhibitor activity; 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:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:RGD.
DR CDD; cd15852; SNARE_Syntaxin8; 1.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR041875; Syntaxin-8_SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..236
FT /note="Syntaxin-8"
FT /id="PRO_0000210219"
FT TOPO_DOM 1..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..232
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..236
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 145..207
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 42..65
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88983"
FT HELIX 153..204
FT /evidence="ECO:0007829|PDB:1GL2"
SQ SEQUENCE 236 AA; 26911 MW; E86A9CD14618E197 CRC64;
MAPDPWFSTY DSTCQIAQEI AEKIQERNQC ERRGEKTPKL TLTIRTLLKN LKVKIDLLKD
LLLRAVSTRQ ITQLEGDRRQ NLLDDLVTRE RLLLASFKNE GSEPDLIRSS LMSEEAKRGT
PNPWLCEEPE ETRGLGFDEI RQQQQKIIQE QDAGLDALSS IISRQKQMGQ EIGNELDEQN
EIIDDLANLV ENTDEKLRTE ARRVTLVDRK SASCGMIMVI LLLLVAIVVV AVWPTN
