UBCX_YEAST
ID UBCX_YEAST Reviewed; 183 AA.
AC P29340; D6VUR5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Ubiquitin-conjugating enzyme E2-21 kDa;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme PEX4;
DE AltName: Full=Peroxin-4;
DE AltName: Full=Ubiquitin carrier protein;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=PEX4; Synonyms=PAS2, UBC10; OrderedLocusNames=YGR133W;
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=1326082; DOI=10.1038/359073a0;
RA Wiebel F.F., Kunau W.-H.;
RT "The Pas2 protein essential for peroxisome biogenesis is related to
RT ubiquitin-conjugating enzymes.";
RL Nature 359:73-76(1992).
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 FUNCTION.
RX PubMed=17550898; DOI=10.1074/jbc.m702038200;
RA Williams C., van den Berg M., Sprenger R.R., Distel B.;
RT "A conserved cysteine is essential for Pex4p-dependent ubiquitination of
RT the peroxisomal import receptor Pex5p.";
RL J. Biol. Chem. 282:22534-22543(2007).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Essential for peroxisome biogenesis. Required for UBC4-
CC independent ubiquitination of PEX5. {ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000269|PubMed:17550898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- INTERACTION:
CC P29340; P39718: PEX22; NbExp=10; IntAct=EBI-19784, EBI-20707;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X65470; CAA46467.1; -; Genomic_DNA.
DR EMBL; Z72918; CAA97146.1; -; Genomic_DNA.
DR EMBL; AY557776; AAS56102.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08226.1; -; Genomic_DNA.
DR PIR; S29088; S29088.
DR RefSeq; NP_011649.1; NM_001181262.1.
DR PDB; 2Y9M; X-ray; 2.60 A; A=15-183.
DR PDB; 2Y9P; X-ray; 3.25 A; A=15-183.
DR PDB; 4BWF; X-ray; 3.23 A; A=15-183.
DR PDBsum; 2Y9M; -.
DR PDBsum; 2Y9P; -.
DR PDBsum; 4BWF; -.
DR AlphaFoldDB; P29340; -.
DR SMR; P29340; -.
DR BioGRID; 33381; 201.
DR DIP; DIP-4411N; -.
DR IntAct; P29340; 4.
DR MINT; P29340; -.
DR STRING; 4932.YGR133W; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR MaxQB; P29340; -.
DR PaxDb; P29340; -.
DR PRIDE; P29340; -.
DR EnsemblFungi; YGR133W_mRNA; YGR133W; YGR133W.
DR GeneID; 853034; -.
DR KEGG; sce:YGR133W; -.
DR SGD; S000003365; PEX4.
DR VEuPathDB; FungiDB:YGR133W; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000154349; -.
DR HOGENOM; CLU_030988_13_0_1; -.
DR InParanoid; P29340; -.
DR OMA; PIKRLMT; -.
DR BioCyc; YEAST:G3O-30839-MON; -.
DR BRENDA; 2.3.2.23; 984.
DR UniPathway; UPA00143; -.
DR PRO; PR:P29340; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P29340; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:SGD.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IMP:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..183
FT /note="Ubiquitin-conjugating enzyme E2-21 kDa"
FT /id="PRO_0000082558"
FT DOMAIN 17..179
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 115
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:2Y9M"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2Y9M"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2Y9M"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4BWF"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2Y9M"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:2Y9M"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2Y9M"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2Y9M"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:2Y9M"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:2Y9M"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2Y9M"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:2Y9M"
SQ SEQUENCE 183 AA; 21118 MW; D4E438B689F76CAD CRC64;
MPNFWILENR RSYTSDTCMS RIVKEYKVIL KTLASDDPIA NPYRGIIESL NPIDETDLSK
WEAIISGPSD TPYENHQFRI LIEVPSSYPM NPPKISFMQN NILHCNVKSA TGEICLNILK
PEEWTPVWDL LHCVHAVWRL LREPVCDSPL DVDIGNIIRC GDMSAYQGIV KYFLAERERI
NNH
