STX7_RAT
ID STX7_RAT Reviewed; 261 AA.
AC O70257; Q5U337;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Syntaxin-7;
GN Name=Stx7;
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], AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=9417091; DOI=10.1074/jbc.273.1.375;
RA Wong S.H., Xu Y., Zhang T., Hong W.;
RT "Syntaxin 7, a novel syntaxin member associated with the early endosomal
RT compartment.";
RL J. Biol. Chem. 273:375-380(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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: May be involved in protein trafficking from the plasma
CC membrane to the early endosome (EE) as well as in homotypic fusion of
CC endocytic organelles. Mediates the endocytic trafficking from early
CC endosomes to late endosomes and lysosomes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VPS11, VPS16 and VPS18. Interacts with VPS33A
CC (By similarity). Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of the
CC SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required
CC for heterotypic fusion of late endosomes with lysosomes. Interacts with
CC TPC1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O70439}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues tested. Highest expression
CC is found in kidney followed by lung, spleen, heart and brain. Lower
CC expression, in skeletal muscle, liver and testis.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF031430; AAC17131.1; -; mRNA.
DR EMBL; BC085737; AAH85737.1; -; mRNA.
DR RefSeq; NP_068641.2; NM_021869.2.
DR RefSeq; XP_017445133.1; XM_017589644.1.
DR RefSeq; XP_017445134.1; XM_017589645.1.
DR RefSeq; XP_017445135.1; XM_017589646.1.
DR AlphaFoldDB; O70257; -.
DR SMR; O70257; -.
DR BioGRID; 248851; 3.
DR CORUM; O70257; -.
DR DIP; DIP-37411N; -.
DR IntAct; O70257; 6.
DR STRING; 10116.ENSRNOP00000021318; -.
DR iPTMnet; O70257; -.
DR PhosphoSitePlus; O70257; -.
DR SwissPalm; O70257; -.
DR jPOST; O70257; -.
DR PaxDb; O70257; -.
DR PRIDE; O70257; -.
DR GeneID; 60466; -.
DR KEGG; rno:60466; -.
DR CTD; 8417; -.
DR RGD; 619747; Stx7.
DR VEuPathDB; HostDB:ENSRNOG00000015670; -.
DR eggNOG; KOG0811; Eukaryota.
DR HOGENOM; CLU_059257_1_1_1; -.
DR InParanoid; O70257; -.
DR OMA; HMENGLN; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; O70257; -.
DR TreeFam; TF315607; -.
DR PRO; PR:O70257; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015670; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; O70257; baseline and differential.
DR Genevisible; O70257; RN.
DR GO; GO:0042582; C:azurophil granule; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
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: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:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0070820; C:tertiary granule; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0019905; F:syntaxin binding; 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:0070925; P:organelle assembly; ISO:RGD.
DR GO; GO:0051640; P:organelle localization; ISO:RGD.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISO:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; TAS: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 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 Acetylation; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT CHAIN 2..261
FT /note="Syntaxin-7"
FT /id="PRO_0000210216"
FT TOPO_DOM 2..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..261
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 165..227
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..68
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70439"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70439"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT CONFLICT 139
FT /note="E -> A (in Ref. 1; AAC17131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29851 MW; 42D23BA7EC5F5F09 CRC64;
MSYTPGIGGD PAQLAQRISS NIQKITQCSA EIQRTLNQLG TPQDTPELRQ QLQQEQQYTN
QLAKETDKYI KEFGFLPTTP SEQRQRKIQK DRLVAEFTTA LTNFQKVQRQ AAEREKEFVA
RVRASSRVSG GFPEDSSKEK NFVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
DIMDINEIFK DLGMMIHEQG DVIDSIEANV ESAEVHVQQA NQQLSRAANY QRKSRKTLCI
IILILVVGIV IIFFIVWGLK G
