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PFD3_YEAST
ID   PFD3_YEAST              Reviewed;         199 AA.
AC   P48363; D6VUL0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Prefoldin subunit 3;
DE   AltName: Full=Genes involved in microtubule biogenesis protein 2;
DE   AltName: Full=Gim complex subunit 2;
DE            Short=GimC subunit 2;
GN   Name=PAC10; Synonyms=GIM2, PFD3; OrderedLocusNames=YGR078C;
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].
RA   Geiser J.R., Hoyt M.A.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9463374; DOI=10.1093/emboj/17.4.952;
RA   Geissler S., Siegers K., Schiebel E.;
RT   "A novel protein complex promoting formation of functional alpha- and
RT   gamma-tubulin.";
RL   EMBO J. 17:952-966(1998).
RN   [6]
RP   IDENTIFICATION IN THE PREFOLDIN COMPLEX.
RX   PubMed=9878052; DOI=10.1093/emboj/18.1.75;
RA   Siegers K., Waldmann T., Leroux M.R., Grein K., Shevchenko A., Schiebel E.,
RA   Hartl F.U.;
RT   "Compartmentation of protein folding in vivo: sequestration of non-native
RT   polypeptide by the chaperonin-GimC system.";
RL   EMBO J. 18:75-84(1999).
RN   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC       transfers target proteins to it. Binds to nascent polypeptide chain and
CC       promotes folding in an environment in which there are many competing
CC       pathways for nonnative proteins.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. {ECO:0000269|PubMed:9878052}.
CC   -!- INTERACTION:
CC       P48363; P53900: GIM3; NbExp=3; IntAct=EBI-13239, EBI-13246;
CC       P48363; Q04493: GIM5; NbExp=5; IntAct=EBI-13239, EBI-13253;
CC       P48363; P52553: YKE2; NbExp=5; IntAct=EBI-13239, EBI-13260;
CC   -!- MISCELLANEOUS: Present with 6550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; U29137; AAA70038.1; -; Genomic_DNA.
DR   EMBL; Z72863; CAA97080.1; -; Genomic_DNA.
DR   EMBL; AY557774; AAS56100.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08171.1; -; Genomic_DNA.
DR   PIR; S59741; S59741.
DR   RefSeq; NP_011592.3; NM_001181207.3.
DR   AlphaFoldDB; P48363; -.
DR   SMR; P48363; -.
DR   BioGRID; 33320; 642.
DR   ComplexPortal; CPX-1671; Prefoldin co-chaperone complex.
DR   DIP; DIP-6837N; -.
DR   IntAct; P48363; 10.
DR   MINT; P48363; -.
DR   STRING; 4932.YGR078C; -.
DR   iPTMnet; P48363; -.
DR   MaxQB; P48363; -.
DR   PaxDb; P48363; -.
DR   PRIDE; P48363; -.
DR   EnsemblFungi; YGR078C_mRNA; YGR078C; YGR078C.
DR   GeneID; 852969; -.
DR   KEGG; sce:YGR078C; -.
DR   SGD; S000003310; PAC10.
DR   VEuPathDB; FungiDB:YGR078C; -.
DR   eggNOG; KOG3313; Eukaryota.
DR   GeneTree; ENSGT00390000018904; -.
DR   HOGENOM; CLU_083737_0_0_1; -.
DR   InParanoid; P48363; -.
DR   OMA; DEQHSKY; -.
DR   BioCyc; YEAST:G3O-30790-MON; -.
DR   PRO; PR:P48363; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P48363; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005844; C:polysome; IDA:SGD.
DR   GO; GO:0016272; C:prefoldin complex; IPI:SGD.
DR   GO; GO:0015631; F:tubulin binding; IDA:SGD.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IC:ComplexPortal.
DR   GO; GO:0007021; P:tubulin complex assembly; IMP:SGD.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR016655; PFD3.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12409; PTHR12409; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Prefoldin subunit 3"
FT                   /id="PRO_0000153659"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   199 AA;  23115 MW;  884D7449C7AD6233 CRC64;
     MDTLFNSTEK NARGIPQAPF IENVNEIIKD PSDFELCFNK FQERLSKYKF MQESKLATIK
     QLKTRIPDLE NTLKICQSLR NHSDEGDESD EPILLHYQLN DTLYTKAQVD IPEDRADLKV
     GLWLGADVML EYPIDEAIEL LKKKLADSEQ SLTVSTEDVE FLRENITTME VNCARLYNWD
     VQRRQDLKQA QEGTKNLKI
 
 
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