YRB30_YEAST
ID YRB30_YEAST Reviewed; 440 AA.
AC P53107; D6VTY7; Q6LDS2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ran-specific GTPase-activating protein 30;
DE AltName: Full=Ran-binding protein 30;
DE Short=RANBP30;
GN Name=YRB30; OrderedLocusNames=YGL164C; ORFNames=G1817;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-440.
RX PubMed=3052856; DOI=10.1016/0092-8674(88)90229-2;
RA Fuerst P., Hu S., Hackett R., Hamer D.;
RT "Copper activates metallothionein gene transcription by altering the
RT conformation of a specific DNA binding protein.";
RL Cell 55:705-717(1988).
RN [5]
RP FUNCTION, INTERACTION WITH GSP1, AND SUBCELLULAR LOCATION.
RX PubMed=12578832; DOI=10.1074/jbc.m210630200;
RA Braunwarth A., Fromont-Racine M., Legrain P., Bischoff F.R.,
RA Gerstberger T., Hurt E., Kuenzler M.;
RT "Identification and characterization of a novel RanGTP-binding protein in
RT the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:15397-15405(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Important for the export of protein containing nuclear export
CC signal (NES) out of the nucleus. Stimulates the GTPase activity of
CC GSP1. {ECO:0000269|PubMed:12578832}.
CC -!- SUBUNIT: Interacts with GSP1. {ECO:0000269|PubMed:12578832}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12578832}. Nucleus
CC {ECO:0000269|PubMed:12578832}. Note=Shuttles between the nucleus and
CC cytoplasm.
CC -!- MISCELLANEOUS: Present with 3670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72686; CAA96876.1; -; Genomic_DNA.
DR EMBL; M22580; AAA66315.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07948.1; -; Genomic_DNA.
DR PIR; S60423; S60423.
DR RefSeq; NP_011351.1; NM_001181029.1.
DR AlphaFoldDB; P53107; -.
DR SMR; P53107; -.
DR BioGRID; 33089; 62.
DR IntAct; P53107; 2.
DR MINT; P53107; -.
DR STRING; 4932.YGL164C; -.
DR iPTMnet; P53107; -.
DR MaxQB; P53107; -.
DR PaxDb; P53107; -.
DR PRIDE; P53107; -.
DR EnsemblFungi; YGL164C_mRNA; YGL164C; YGL164C.
DR GeneID; 852712; -.
DR KEGG; sce:YGL164C; -.
DR SGD; S000003132; YRB30.
DR VEuPathDB; FungiDB:YGL164C; -.
DR eggNOG; ENOG502R7I3; Eukaryota.
DR HOGENOM; CLU_014536_0_0_1; -.
DR InParanoid; P53107; -.
DR OMA; WKETYAR; -.
DR BioCyc; YEAST:G3O-30653-MON; -.
DR PRO; PR:P53107; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53107; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR008812; Ran_GTP-bd-rel.
DR PANTHER; PTHR31010; PTHR31010; 2.
DR Pfam; PF05508; Ran-binding; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..440
FT /note="Ran-specific GTPase-activating protein 30"
FT /id="PRO_0000213672"
FT DOMAIN 1..314
FT /note="RanBD1"
FT REGION 341..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..372
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 440 AA; 50296 MW; DE4505C39F17AA3C CRC64;
MDEILAKAGS QAVTFAIKSG ISIASTYALK TITNFVVQIP KDDARRIDQL KFKLESRMAI
VSSAIDLIKL VAARGNTNLQ ITLRLTKDLK EEIDRFDEKI NEMTQKVEGS RSAKTQNEAI
KAVENYIKDL LLRIEEITPF INLSLTTSGA NLNSALPYQL SPGLLLKASD FVSENNRKYE
KAMKSNEKGT GDKEILKVQV GPTFEVTLFS IFYNLTSENN GQSGIVWKED MKRAKARIYR
LNSTGRKYDY FMKIEQDFND GRYHEDDDKE DTPQELAIDL NHIKKLFFSV SGKLLRLEEQ
DSPVLVLKID RSDDKENESS EGDKGLLDDI TWYAVSGYEA IEEDEEEDEE EDEEEGKDGE
ERKEEEEEEN KLEDKDSSIT LLEYIIRLTS LQSNDQKSIL EVSDERLSIY LNDENTNSRK
DRISNSTIEE TEKKLKNLKL
