ID M3WKZ0_FELCA Unreviewed; 1359 AA.
AC M3WKZ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ubiquitin conjugation factor E4 {ECO:0000256|RuleBase:RU369083};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369083};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 {ECO:0000256|RuleBase:RU369083};
GN Name=UBE4B {ECO:0000313|Ensembl:ENSFCAP00000013530.4,
GN ECO:0000313|VGNC:VGNC:66772};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000013530.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013530.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013530.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000013530.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013530.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000013530.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013530.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. Also functions
CC as an E4 ligase mediating the assembly of polyubiquitin chains on
CC substrates ubiquitinated by another E3 ubiquitin ligase. Mediates 'Lys-
CC 48'-linked polyubiquitination of substrates.
CC {ECO:0000256|RuleBase:RU369083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU369083};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU369083}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000256|RuleBase:RU369083}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000256|ARBA:ARBA00007434, ECO:0000256|RuleBase:RU369083}.
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DR EMBL; AANG04003082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006934329.1; XM_006934267.3.
DR PaxDb; 9685-ENSFCAP00000021778; -.
DR Ensembl; ENSFCAT00000014591.6; ENSFCAP00000013530.4; ENSFCAG00000014587.6.
DR GeneID; 101095271; -.
DR CTD; 10277; -.
DR VGNC; VGNC:66772; UBE4B.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_2_0_1; -.
DR OrthoDB; 1554at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000014587; Expressed in embryonic head and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR CDD; cd16658; RING-Ubox_UBE4B; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369083};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transferase {ECO:0000256|RuleBase:RU369083};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369083}.
FT DOMAIN 1284..1357
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 151616 MW; 55A86095A5FC3260 CRC64;
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPLGP PIAASAPGPS QSLGLNVHNM
TPATSPIGAS GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
DVDSGIENME VDENDRREKR SVSDKEPSSG SEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIAAARSPDR
NLLLTTGSNP GASPMFCGVG SFGASSLSSL YETSPAPSTS FWSSVPVPSP SVASSPCRAA
SQPAAPSVTL SPHGAASGAA AGSQPSSPRY RPYTVAHPWG PSASAPRSPG ISTLSSSPGR
PALASSPQAV PASSPSQRPS SLGPPLLAAS PSAASRRPSS LRTSPSMHDS PFSFLFLALS
GDSSDDDEED DDDGDDGDDE GGGGGDEFSC VQFGSSLGAS GGTGTWDSYS DHFTIETCKE
TDMLNYLIEC FDRVGIEEKK APKMCSQPAV SQLLSNIRSQ CISHTALVLQ GSLTQPRSVL
QPSFLVPYML CRNLPYGFMQ ELVRTTHQDE EVFKQIFIPI LQGLALAAKE CSLDSDYFKY
PLMALGELCE TKFGKTHPVC NLVASLPLWL PKSLSPGSGR ELQRLSYLGA FFSFSVFAED
DAKVVEKYFS GPAITLENTR VVSQSLQHYL ELGRQELFKI LHSILLNGET REAALGYMAA
VVNANMKKAQ MQTDDRLVST DGFMLNFLWV LQQLSTKIKL ETVDPTYIFH PRCRITLPND
ETRVNATMED VNDWLAELYG DQPPFSEPKF PTECFFLTLH AHHLSILPSC RRYIRRLRAI
RELNRTVEDL KNNESQWKDS PLATRHREML KRCKTQLKKL VRCKACADAG LLDESFLRRC
LNFYGLLIQL LLRILDPAYP DITLPLNSDV PKVFAALPEF YVEDVAEFLF FIVQYSPQVL
YEPCTQDIVM FLVVMLCNQN YIRNPYLVAK LVEVMFMTNP AVQPRTQKFF EMIENHPLST
KLLVPSLMKF YTDVEHTGAT SEFYDKFTIR YHISTIFKSL WQNIAHHGTF MEEFNSGKQF
VRYINMLIND TTFLLDESLE SLKRIHEVQE EMKNKDQWDQ LPRDQQQARQ SQLAQDERVS
RSYLALATET VDMFHILTKQ VQKPFLRPEL GPRLAAMLNF NLQQLCGPKC RDLKVENPEK
YGFEPKKLLD QLTDIYLQLD CARFAKAIAD DQRSYSKELF EEVISKMRKA GIKSTIAIEK
FKLLAEKVEE IVAKNARAEI DYSDAPDEFR DPLMDTLMTD PVRLPSGTIM DRSIILRHLL
NSPTDPFNRQ MLTESMLEPV PELKEQIHAW MREKQNSDH
//
