ID H0VN42_CAVPO Unreviewed; 1028 AA.
AC H0VN42;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
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=UBE4A {ECO:0000313|Ensembl:ENSCPOP00000011851.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011851.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000011851.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011851.3};
RG Ensembl;
RL Submitted (NOV-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 -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. May also
CC function as an E4 ligase mediating the assembly of polyubiquitin chains
CC on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC 'Lys-48'-linked polyubiquitination of substrates.
CC {ECO:0000256|ARBA:ARBA00037624}.
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|ARBA:ARBA00000900,
CC 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; AAKN02024820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0VN42; -.
DR Ensembl; ENSCPOT00000013291.3; ENSCPOP00000011851.3; ENSCPOG00000013164.4.
DR VEuPathDB; HostDB:ENSCPOG00000013164; -.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_1_0_1; -.
DR TreeFam; TF300802; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000013164; Expressed in testis and 12 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; cd16657; RING-Ubox_UBE4A; 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:SF16; UBIQUITIN CONJUGATION FACTOR E4 A; 1.
DR PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 2.
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:UP000005447};
KW Transferase {ECO:0000256|RuleBase:RU369083};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369083}.
FT DOMAIN 949..1023
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 118165 MW; FA3C0A4213CE4B03 CRC64;
MTDQENNNNI SSNPFAALFG SLADAKQFAA IQKEQLKQQS DELPASPDDS DNSVSESLDE
FDYSVAEISR SFRSQQEICE QLNINHMIQR IFLITLDNSD PSMKSGNGIP SRCVYLEEMA
VELEDQDWLD MSNVEQAIFA RLLLQDPGNH LINMTSSTTL NLSADRDAGE RHIFCYLYFC
FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMLEAIQGA
HFEDVTEFLE GVIEALVLDE EVRTFPEVMI PVFDILLGRI KDLELCQILL YAYLDILLYF
TRQKDMAKVF VEYIQPKDPS NGQMYQKTLL GVILNISCLL KTPGVVENHG YFLNPSRSSP
QEIKVQEANI HQFMAQFHEK IYQMLKNLLQ LSPETKHCIL SWLGNCLHAN AGRTKIWANQ
MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCALKEL NDEERKIKNV
HMRGLDKETC LIPAVQEPKF PQNYNLVTEN LALTEYTLYL GFHRLHDQMV KINQNLHRLQ
VAWRDAQQSS SPAADNLREQ FERLMTIYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI
GNEGSQPVEL TFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFADDILETS ADSLEHVLHF
ITIFTGSIER MKNPHLRAKL AEVLEAVMPH LDQTPNPLVS SVFHRKRVFC NFPYAPQLAE
ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILRYMWGTDS YRESIKYLSK IKIQQIEKDR
GEWDNLSPEA RREKEAGLQM FGQLARFHNI MSNETIGTLT FLTSEIKSLF VHPFLAERII
SMLNYFLQHL VGPKMGALKV KDFSEFDFKP QQLVSDICTI YLNLGDEENF CATVPKDGRS
YSPTLFAQTV RVLKKINKPG NMIVAFSNLA ERIKSLADLQ QQEEETYADA CDEFLDPIMS
TLMSDPVVLP SSRVTVDRST IARHLLSDQT DPFNRSPLTM DQIRPNTELK EKIQRWLAER
KQQKEQLE
//
