UFD2_SCHPO
ID UFD2_SCHPO Reviewed; 1010 AA.
AC Q9HE05; O60009; Q9P7A3; Q9UTT4; Q9UU63;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ubiquitin conjugation factor E4;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P54860};
DE AltName: Full=Ubiquitin fusion degradation protein 2;
DE Short=UB fusion protein 2;
GN Name=ufd2; ORFNames=SPAC145.04, SPAC20H4.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Jang Y.-J., Yoo H.-S.;
RT "The characterization of ubiquitin fusion degradation protein-2 (UFD2)
RT homolog in Schizosaccahromyces pombe.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 81-651, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 896-1010.
RA Kawamukai M.;
RT "S. pombe ufd2 homolog.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E4 ubiquitin chain-elongation enzyme specifically involved in
CC polyubiquitin chain assembly. Binds to cdc48 and elongates mono- and
CC diubiquitinated ERAD substrates presented by the ufd1-npl4-cdc48 (UNC)
CC AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties.
CC Delivers these polyubiquitinated substrates to downstream ERAD
CC components, which target them to the proteasome. Enhances
CC ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety.
CC {ECO:0000250|UniProtKB:P54860}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P54860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus
CC {ECO:0000269|PubMed:10759889}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:P54860}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC80427.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF059906; AAC80427.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAC19740.1; -; Genomic_DNA.
DR EMBL; AB027791; BAA87095.1; -; Genomic_DNA.
DR EMBL; AB032715; BAA84654.1; -; mRNA.
DR PIR; T43725; T43725.
DR RefSeq; NP_593630.1; NM_001019061.2.
DR AlphaFoldDB; Q9HE05; -.
DR SMR; Q9HE05; -.
DR BioGRID; 278506; 136.
DR IntAct; Q9HE05; 3.
DR MINT; Q9HE05; -.
DR STRING; 4896.SPAC20H4.10.1; -.
DR iPTMnet; Q9HE05; -.
DR MaxQB; Q9HE05; -.
DR PaxDb; Q9HE05; -.
DR PRIDE; Q9HE05; -.
DR EnsemblFungi; SPAC20H4.10.1; SPAC20H4.10.1:pep; SPAC20H4.10.
DR GeneID; 2542023; -.
DR KEGG; spo:SPAC20H4.10; -.
DR PomBase; SPAC20H4.10; ufd2.
DR VEuPathDB; FungiDB:SPAC20H4.10; -.
DR eggNOG; KOG2042; Eukaryota.
DR HOGENOM; CLU_003224_2_1_1; -.
DR InParanoid; Q9HE05; -.
DR OMA; EHDTSTQ; -.
DR PhylomeDB; Q9HE05; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9HE05; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931; PTHR13931; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1010
FT /note="Ubiquitin conjugation factor E4"
FT /id="PRO_0000194996"
FT DOMAIN 930..1004
FT /note="U-box"
FT REGION 13..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 80..86
FT /note="WMHFITC -> MDAFYNS (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="N -> D (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..332
FT /note="ST -> LS (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="E -> Y (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..531
FT /note="ML -> YC (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="V -> W (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="A -> T (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="G -> A (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="Q -> P (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="E -> A (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="K -> T (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 809..811
FT /note="AFC -> PFV (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 890..891
FT /note="TS -> PG (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="N -> P (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 907..909
FT /note="IKE -> LKA (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 912..914
FT /note="NRV -> HRA (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="E -> Q (in Ref. 1; AAC80427)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="E -> D (in Ref. 4; BAA84654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 115276 MW; 60A3E5B5E790FE6E CRC64;
MSDLEKIRLK RLAKLQQTNS EANSSKEPKE SNIAPEPKKP DLKKRFIGSK ATTSNSEQKE
ISPPVTSGAP KHRLFSKDEW MHFITCQALN ITLSETDSSK YYLEGFKKDL EEEGSPLLFN
ENNVDSALLS RLSTTGNNTF SYLLQSWSFL YQYKKRLPKD ENQDFKIHYL SLLKSLLVSY
AGIVVMLPDT FNSETIDLAE VLIGAEGIPL EFLSEFVQRF EHENLDELFI PVLESLSLKI
GLMNVDTVQM NVMQIILQLV SLKPIALLLP KLPSWNPTNN AGEIEYKTFL GRISSLSVFT
QDVASRYFSN STERSAQNIS SSISSLKLTM STYQDVLFQI FNTLIRTSTS LRESVLDFFA
MVVNANHKRQ SIQVNHFDIT SDACMLNFSH VLSRLSEPFL DIGCSKIDRV QVEYFRRNPR
VDIKEETKLN ADQKASESFY SKPAEGSNNF ISDIFFLNLA FHHYGVNATF KALEQLVQSI
RDSEKLKERL ETEQQNMSGS FQATRLTAQL SRLDQRLDLD RSFVHCYEIM LTQTSDTSRS
FSFLNFVAIW LSRLADGQSS TYPKMPLSLP FNENAPEAFK CLPEYFIETI TDYMLSLFKT
SSSTLTLHSL EPLCEFCVSF LTQANYIKNP YLRAKLAEIL YFGVQTHVGR SELLLDVVRT
SKVATRWLLP ALMAFYIEIE STGQSTQFYD KFNIRFYICE VFRTIWKQPA YFGKLEQEQK
TNLPFFVKFV ALMLNDATYL LDEALLKLTE IHNLQSLLAD AISNSNSNQN VQESQSNLAA
AERQASTYCQ LGNETIFMLK LFTSSIPKAF CAVEIVDRLA AMLNYNLQAL CGPKCSNLKV
EDPTKYHFNA KTLLSIIFDV YLNLCNEPAF VEAVAHDGRS YSKEIFERAT SIMTKHNLKS
SFDIEAIKEF VNRVEAFRLQ EATEEEDMGD IPDYFLDPLM FTIMKDPVVL PRSGISIDRS
TIKAHLLSDA TDPFNRTPLT LDDVTPNDTL REEINTFLKS KRNKHSRNSE
