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RYL2_YARLI
ID   RYL2_YARLI              Reviewed;         209 AA.
AC   P41925; Q6CHV9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Ras-like GTP-binding protein RYL2;
GN   Name=RYL2; OrderedLocusNames=YALI0A04367g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RA   Pertuiset B., Beckerich J.-M., Gaillardin C.;
RT   "RYL2 a new member of Ras/Rho/Ypt1-like gene family.";
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; L06970; AAA35246.1; -; Genomic_DNA.
DR   EMBL; CR382127; CAG83676.1; -; Genomic_DNA.
DR   RefSeq; XP_499752.1; XM_499752.1.
DR   AlphaFoldDB; P41925; -.
DR   SMR; P41925; -.
DR   STRING; 4952.CAG83676; -.
DR   EnsemblFungi; CAG83676; CAG83676; YALI0_A04367g.
DR   GeneID; 2906287; -.
DR   KEGG; yli:YALI0A04367g; -.
DR   VEuPathDB; FungiDB:YALI0_A04367g; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P41925; -.
DR   OMA; HRYVKNA; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..209
FT                   /note="Ras-like GTP-binding protein RYL2"
FT                   /id="PRO_0000121317"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           208
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           209
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        79
FT                   /note="S -> T (in Ref. 1; AAA35246)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  23768 MW;  2A9D9517D494844A CRC64;
     MESMDAKIVL LGAQGVGKTC FVTRYVNNKF QAGQASTIGA SFSRKRVVVN DTTVRLQIWD
     TAGQERFRSM APIYYRSASC GILCYDVTSR ASFDAMHLWL LELKQNLSSD IIIHIVGTKV
     DLVKDEPSLR EVPFEQCVEY ASEWLQDDSC CHEISAKDDE GVEEVFEVII TKLLDKREAD
     EQQKHNSQRQ RQSVVYLHTD EDEQKSSCC
 
 
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