STX7A_DICDI
ID STX7A_DICDI Reviewed; 356 AA.
AC Q54JY7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Syntaxin-7A;
GN Name=syn7A {ECO:0000312|EMBL:EAL63513.1};
GN Synonyms=syn7 {ECO:0000312|dictyBase:DDB_G0287733}; ORFNames=DDB_G0287733;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL63513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NSFA; SNPA AND SNPC.
RX PubMed=10978342; DOI=10.1074/jbc.m006710200;
RA Bogdanovic A., Bruckert F., Morio T., Satre M.;
RT "A syntaxin 7 homologue is present in Dictyostelium discoideum endosomes
RT and controls their homotypic fusion.";
RL J. Biol. Chem. 275:36691-36697(2000).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN SNARE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=12175335; DOI=10.1042/bj20020845;
RA Bogdanovic A., Bennett N., Kieffer S., Louwagie M., Morio T., Garin J.,
RA Satre M., Bruckert F.;
RT "Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane
RT protein 7) form an active SNARE complex for early macropinocytic
RT compartment fusion in Dictyostelium discoideum.";
RL Biochem. J. 368:29-39(2002).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane during transport of proteins from the early
CC endosome to the lysosome. Required for fusion of late endosomes with
CC lysosomes and homotypic lysosomal fusion. May be involved in protein
CC trafficking from the plasma membrane to the early endosome (EE) as well
CC as in homotypic fusion of endocytic organelles.
CC {ECO:0000250|UniProtKB:O15400, ECO:0000269|PubMed:10978342,
CC ECO:0000269|PubMed:12175335}.
CC -!- SUBUNIT: Component of the SNARE complex composed of syn7A, syn8A,
CC vamp7A and vti1A. Interacts with nsfA, snpA and snpC.
CC {ECO:0000269|PubMed:10978342, ECO:0000269|PubMed:12175335}.
CC -!- INTERACTION:
CC Q54JY7; Q75JI3: nsfA; NbExp=2; IntAct=EBI-1810238, EBI-1810142;
CC Q54JY7; Q54NW7: vamp7A; NbExp=6; IntAct=EBI-1810238, EBI-1810311;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:10978342,
CC ECO:0000269|PubMed:12175335}; Single-pass membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:10978342,
CC ECO:0000269|PubMed:12175335}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000255}.
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DR EMBL; AAFI02000104; EAL63513.1; -; Genomic_DNA.
DR RefSeq; XP_637015.1; XM_631923.1.
DR AlphaFoldDB; Q54JY7; -.
DR SMR; Q54JY7; -.
DR IntAct; Q54JY7; 8.
DR STRING; 44689.DDB0231537; -.
DR PaxDb; Q54JY7; -.
DR EnsemblProtists; EAL63513; EAL63513; DDB_G0287733.
DR GeneID; 8626270; -.
DR KEGG; ddi:DDB_G0287733; -.
DR dictyBase; DDB_G0287733; syn7A.
DR eggNOG; KOG0811; Eukaryota.
DR HOGENOM; CLU_779444_0_0_1; -.
DR InParanoid; Q54JY7; -.
DR OMA; HMENGLN; -.
DR PhylomeDB; Q54JY7; -.
DR Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q54JY7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0030666; C:endocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:dictyBase.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:dictyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
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; 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 Coiled coil; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..356
FT /note="Syntaxin-7A"
FT /id="PRO_0000319997"
FT TOPO_DOM 1..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Anchor for type IV membrane protein"
FT TOPO_DOM 355..356
FT /note="Vesicular"
FT /evidence="ECO:0000250|UniProtKB:O15400, ECO:0000255"
FT DOMAIN 259..321
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 32..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 40219 MW; E9D26004CC26C54D CRC64;
MYNNNNNFGG GGYNQGGGYN SGGYNNNGGG YNNNNGGYNN NNNNNGGYNN NRPQQQQQQQ
QQYVNNNNNS FDNNGYGGDD DVTNNSDYQS TTRNIQQIQN AVQILTKLVQ LLGTPKDSMD
TREKIRNCVD STTHLISSES GKVKNLTSLA SRSRDSKNKL LYQKLVKEFN NCLQQFKDIA
QVATKKEKTT PLPVAPDHQQ PTTFGRNNNS NNNNQNNHFL NNQQPYYDDD NREDEHQSLM
ESSRRQQLAQ IEAEREYQNS IIQERDEGIR KIEQSIVEIN EIFVDLSGLV AEQGVMINTI
EASLESTTIN TKEGVNHLRE ASKNQKSSRN KMCWIVLILL IVCAVLGVIL FFTLRK
