ID F7HI26_CALJA Unreviewed; 1208 AA.
AC F7HI26; U3D458;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=DZIP3 {ECO:0000313|EMBL:JAB26782.1,
GN ECO:0000313|Ensembl:ENSCJAP00000009543.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000009543.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000009543.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB26782.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebral cortex {ECO:0000313|EMBL:JAB26782.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000009543.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; GAMR01007150; JAB26782.1; -; mRNA.
DR RefSeq; XP_002758891.1; XM_002758845.4.
DR RefSeq; XP_008980765.1; XM_008982517.2.
DR RefSeq; XP_008980766.1; XM_008982518.2.
DR Ensembl; ENSCJAT00000010087.5; ENSCJAP00000009543.5; ENSCJAG00000005143.5.
DR GeneID; 100407623; -.
DR KEGG; cjc:100407623; -.
DR CTD; 9666; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000161692; -.
DR HOGENOM; CLU_007762_0_0_1; -.
DR OMA; KETICSF; -.
DR OrthoDB; 5256194at2759; -.
DR TreeFam; TF333981; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008225; Chromosome 15.
DR Bgee; ENSCJAG00000005143; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR CDD; cd16460; RING-H2_DZIP3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033103; DZIP3_RING-H2_finger.
DR InterPro; IPR041249; HEPN_DZIP3.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15727:SF4; E3 UBIQUITIN-PROTEIN LIGASE DZIP3; 1.
DR PANTHER; PTHR15727; RING FINGER PROTEIN 214; 1.
DR Pfam; PF18738; HEPN_DZIP3; 1.
DR Pfam; PF19179; TTC3_DZIP3_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1148..1188
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 806..844
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 138223 MW; F204C18A3FC82A43 CRC64;
MDSLPEEFFV SHPHVEDQRK EETENKPEKS SVQLDKQEKD VPTDLVPVNL LLEVKKLLSA
INTLPKGVVP HVKKFLQEDF SFQTMQREVA ANSQSGEEIV PALTLRFLIT QLEAALRNIQ
ATNYTARQIN VGYYLTLLFL YGVALTERGK KEDYTEAENK FLVMKMVIQE NEICENFMSL
VYFGRGLLRC AQKRYNGGLL EFHKGLQEIG DINDHWFDID PTEDEDLPTT FKDLLNNFIK
TTESNIMKQT ICSYLDCERS CEADILKNTS YKGFFQLMCS KNCCVYFHKI CWKRFKNLKY
PGENDQSFIA KKCLKEGCTG DMARMLQCDV PGIVKILFEV VRKDEYITIE NLGASYKKLV
SLKIADTDIR PKISLKFNTK DEMPIFKLDY NYFYHLLHII IISGTDVVRQ IFDEAMPPPL
LRKELLIHKN VLESYYNHLW TNHPLGGSWH LLFPPNKELP QSKQFDLCLL LALIQHLNVF
PAPKNGWNME PPSSDISKSA DILRLCKYRD ILLSEILMNG LTESQFNSIW KEVSDILLRL
GMKQEDIDKV KENPIENISL DYHQLSIYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRTE
IEELQNEEEE LSPPIMEYNI NVKSNPEIQF AEINKDGASI PSESSTESLK DLQEVKSKQR
KKKKTKNKKN TDSKEEQVPY VVENEEQLKK EQANPQSVGG FLKDDASDIQ EDSATEDKFY
SLDELHILDM IEQGSAGKVT TDYGETEKER LARQRQLYKL HYQCEDFKRQ LRTVTFRWQE
NQMQIKKKDK IISSLNQQVA FGINKVSKLQ RQIHAKDNEI KNLKEQLSMK RSQWEMEKHN
LESTMKTYVG KLNTETSRAL TAEVYFLQCR RDFGLLHLEQ TEKECLNQLA RVTHMAASNL
ESLQLKAAVD SWNAIVADVR NKIAFLRTQY NEQINKVKQG FALSTLPPVQ LPPPPPSPEI
LMQQFLGRPL VKESFFRPIL TVPQMPAVCP GVISATGQPR APLMTGIAWT LPVPVGDAVP
PSAGLGSDPS MMNWERITDR LKTAFPQQTR KELTDFLRKL KDAHGKSLSG LTFDEIVCKI
SQFIDPKKSQ SQGKSVSNGN CVSPSHSPSQ PNAAQPPKPA WRPLTSQSSA TWEGANKPDE
EEEEEEPCVI CHENLSPENL SVLPCAHKFH AQCIRPWLMQ QGTCPTCRLH VLLPEEFPGH
PSRQLPKI
//
