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Database: UniProt
Entry: K7EG61_ORNAN
LinkDB: K7EG61_ORNAN
Original site: K7EG61_ORNAN 
ID   K7EG61_ORNAN            Unreviewed;       595 AA.
AC   K7EG61;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RLIM {ECO:0000313|Ensembl:ENSOANP00000032518.1};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000032518.1, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000032518.1, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000032518.1,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000032518.1}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000032518.1};
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RNF12 family.
CC       {ECO:0000256|ARBA:ARBA00038418}.
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DR   RefSeq; XP_001505684.1; XM_001505634.4.
DR   AlphaFoldDB; K7EG61; -.
DR   STRING; 9258.ENSOANP00000032518; -.
DR   Ensembl; ENSOANT00000041766.2; ENSOANP00000032518.1; ENSOANG00000002027.3.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000155753; -.
DR   InParanoid; K7EG61; -.
DR   OMA; HHNISSQ; -.
DR   OrthoDB; 5474929at2759; -.
DR   TreeFam; TF325756; -.
DR   Proteomes; UP000002279; Chromosome 6.
DR   Bgee; ENSOANG00000002027; Expressed in fibroblast and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0060816; P:random inactivation of X chromosome; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd16674; RING-H2_RNF12; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45931:SF4; E3 UBIQUITIN-PROTEIN LIGASE RLIM; 1.
DR   PANTHER; PTHR45931; SI:CH211-59O9.10; 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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          541..582
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  64574 MW;  45E051C68CC18F1E CRC64;
     MESSDANDKG SVDQSEAQRR SQLDRLDREE AFYQFVNNLS EEEYRLMRDN NLLGTPGEIT
     EEELLRRLHQ VKEGPPQQNS DENRGAESTE DVSNGDSIID WLNSVRQTGN TTRSGQRGNQ
     SWRAVSRTNP NSGDFRFSLE INVNRNNGAP NPDHDSEPPV EPSGGEDAES HSQSDIETPR
     SESPSGRQPG SERNGSEEPP ASEPSPQRGL RRARSRSPEQ RRTRARTERS RSPLHPASEA
     PRRAAHHPAS APTLEPPPVS EAEGSSRTRQ HVTLRQPPAG AETPGDGGGV VPSASPEGRG
     AAPGPGSSEA GGAEPTAPGQ RPPTIVLDLQ VRRVRPGEYR QRDSIANRTR SRSQTPNNTV
     TYESERGGFR RTFSRSERAG VRTYVSTIRI PIRRILNTGL SETTSVAIQT MLRQIMTGFG
     ELSYFMYSDS DADPGGPAPA PAGDGAEQPQ GGGSGEGAEA GAEAYEGGHE GGSSSGARRD
     GGRGGRGSVT FEESGSLPFL SLAQFFLLNE DDDDQPRGLT KEQIDNLAMR NFGESDALKT
     CSVCITEYTE GNKLRKLPCS HEYHVHCIDR WLSENSTCPI CRRAVLASGN RESVV
//
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