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YKT6_DICDI
ID   YKT6_DICDI              Reviewed;         202 AA.
AC   Q54ES8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative synaptobrevin homolog YKT6;
DE            EC=2.3.1.-;
DE   AltName: Full=Putative prenylated SNARE protein ykt6;
DE   Flags: Precursor;
GN   Name=ykt6; ORFNames=DDB_G0291656;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE)
CC       mediating vesicle docking and fusion to a specific acceptor cellular
CC       compartment. Functions in endoplasmic reticulum to Golgi transport and
CC       in early/recycling endosome to TGN transport as part of a SNARE
CC       complex. Has a S-palmitoyl transferase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: May be found in 2 different SNARE complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic
CC       vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-
CC       anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic
CC       vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Lipid-
CC       anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Probably
CC       cycles through vesicles between Golgi and endosomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; AAFI02000177; EAL61812.1; -; Genomic_DNA.
DR   RefSeq; XP_635162.1; XM_630070.1.
DR   AlphaFoldDB; Q54ES8; -.
DR   SMR; Q54ES8; -.
DR   STRING; 44689.DDB0238214; -.
DR   PaxDb; Q54ES8; -.
DR   EnsemblProtists; EAL61812; EAL61812; DDB_G0291656.
DR   GeneID; 8628108; -.
DR   KEGG; ddi:DDB_G0291656; -.
DR   dictyBase; DDB_G0291656; ykt6.
DR   eggNOG; KOG0861; Eukaryota.
DR   HOGENOM; CLU_074848_2_1_1; -.
DR   InParanoid; Q54ES8; -.
DR   OMA; ITDHEYP; -.
DR   PhylomeDB; Q54ES8; -.
DR   PRO; PR:Q54ES8; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd14824; Longin; 1.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR010908; Longin_dom.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   SMART; SM01270; Longin; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endosome; ER-Golgi transport;
KW   Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW   Prenylation; Protein transport; Reference proteome; Transferase; Transport.
FT   CHAIN           1..199
FT                   /note="Putative synaptobrevin homolog YKT6"
FT                   /id="PRO_0000328314"
FT   PROPEP          200..202
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396668"
FT   DOMAIN          7..129
FT                   /note="Longin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT   DOMAIN          142..202
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   MOD_RES         199
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           198
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           199
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  22771 MW;  D31A9B37848DE5C4 CRC64;
     MKVYSIGLFK VVPGNKPVLL NIVYELSSFG FFQRGSVKEV SLFVSRETVG RTNVGERVSM
     EHTQTQKVCH TTVDSKGLGC SVLTDSEYPG RVAHTLIRIC LEEFYKVHPE SEWRGLQSDV
     ELQTPALDQL LLKYQNPETA DPMMNLQKNL DETITIVKKT VEQLGQRGEK LDDLAAKSDD
     LSFQSKAFMN NAERMNKCCG YV
 
 
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