G2E3_MACFA
ID G2E3_MACFA Reviewed; 706 AA.
AC Q4R9C4; Q4R7E7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=G2/M phase-specific E3 ubiquitin-protein ligase;
DE EC=2.3.2.26;
DE AltName: Full=G2/M phase-specific HECT-type E3 ubiquitin transferase;
GN Name=G2E3; ORFNames=QtsA-15505;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Essential in
CC early embryonic development to prevent apoptotic death.
CC {ECO:0000250|UniProtKB:Q7L622}.
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=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q7L622}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7L622}. Note=Shuttles between the nucleus and
CC the cytoplasm. In the nucleus, delocalizes from the nucleolus to the
CC nucleoplasm in response to DNA damage. {ECO:0000250|UniProtKB:Q7L622}.
CC -!- DOMAIN: Ubiquitin ligase activity is mediated by two distinct domains,
CC PHD-type zinc fingers 2 and 3. The use of these distinct domains may
CC allow ubiquitination of different targets by each domain. The HECT
CC domain is catalytically inactive and does not contribute to this
CC activity. {ECO:0000250|UniProtKB:Q7L622}.
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DR EMBL; AB168872; BAE00975.1; -; mRNA.
DR EMBL; AB168172; BAE00297.1; -; mRNA.
DR RefSeq; NP_001274208.1; NM_001287279.1.
DR RefSeq; XP_005561068.1; XM_005561011.1.
DR RefSeq; XP_015308755.1; XM_015453269.1.
DR RefSeq; XP_015308756.1; XM_015453270.1.
DR RefSeq; XP_015308757.1; XM_015453271.1.
DR AlphaFoldDB; Q4R9C4; -.
DR SMR; Q4R9C4; -.
DR STRING; 9541.XP_005561067.1; -.
DR GeneID; 102142778; -.
DR KEGG; mcf:102142778; -.
DR CTD; 55632; -.
DR eggNOG; KOG1084; Eukaryota.
DR OrthoDB; 199998at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd15669; ePHD_PHF7_G2E3_like; 1.
DR CDD; cd15496; PHD_PHF7_G2E3_like; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR042013; PHF7/G2E3_ePHD.
DR InterPro; IPR042012; PHF7/G2E3_PHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF56204; SSF56204; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..706
FT /note="G2/M phase-specific E3 ubiquitin-protein ligase"
FT /id="PRO_0000248344"
FT DOMAIN 371..698
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ZN_FING 11..51
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 79..128
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 143..193
FT /note="PHD-type 2; degenerate"
FT ZN_FING 237..286
FT /note="PHD-type 3"
FT CONFLICT 30
FT /note="K -> R (in Ref. 1; BAE00975)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> R (in Ref. 1; BAE00975)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="S -> N (in Ref. 1; BAE00297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 80334 MW; 77CE7FD639B40142 CRC64;
MNENKPGDSQ NLACVFCRKN DDCPNKYGEK KTKEKWNLTV HYYCLLMSSG IWQRGKEEEG
VYGFLIEDIR KEVNRASKLK CCVCKKNGAS IGCVAPRCKR SYHFPCGLQR ECIFQFTGNF
ASFCWNHRPV QIITSNNYRE SLPCTICLEF IEPIPSYNIL RSPCCKNAWF HRDCLQVQAI
NAGVFFFRCT ICSNSDIFQK EMLRMGIHIP EKDASWELEE NAYQELLQHH ERCDVRRCRC
KEGRDYNAPD SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRGIIY NSGEFQKAKK
HVLPNSNNVG ITDCLLEESS PKLPRQSPGS QSKDLLRQGS KFRRNVSTLL IELGFQIKKK
TKRLYINKAN IWTSALDAFR NRNFNPSYAI EVAYVIENDN FGSEHPGSKQ EFLSLLMQHL
ENSSLFEGSL SKNLSLNSQA LKENLYYEAG KMLAISLVHG GPSPGFFSKT LFNCLVYGPE
NTQPILDDVS DFDVAQIIIR INTATTVADL KSVINECYNY LELIGCLRLI TTLSDKYMLV
KDILVYHVIQ RVQAPFESFK QGLKTLGVLE KIQAYPEAFC SILCHKPESL SAKILSDLFT
VHTLPDVKAL GFWNSYLQAV EDGKSTTTME DILIFATGCS SIPPAGFKPT PSIECLPVDF
PVGNKCNNCL AIPVTNTYKE FQENMDFTIR NTLKLEKEES SHYIGH
