RNF12_XENTR
ID RNF12_XENTR Reviewed; 639 AA.
AC Q07G42;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=E3 ubiquitin-protein ligase RNF12;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 12;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF12 {ECO:0000305};
GN Name=rnf12 {ECO:0000312|EMBL:CAL49424.1}; ORFNames=TGas054b08.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAL49424.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:CAL49424.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase specific for ldb1,
CC mediating ubiquitination and proteasome-dependent degradation of excess
CC ldb1 in a RING-dependent manner. Does not degrade ldb1 bound to
CC lhx1/lim1, nor lim1 itself and thus contributes to the establishment of
CC proper ldb1-lhx1/lim1 stoichiometry and the formation of a ldb1-
CC lhx1/lim1 complex. Interferes with Spemann organizer function and
CC suppresses secondary axis formation induced by ldb1 and lhx1/lim1.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms homodimers through the C-terminal region. The N-terminus
CC interacts with the homeobox of LIM/homeobox factor lhx1/lim1, with
CC lhx3/lim3 and lhx5/lim5, and with the N-terminus of ldb1 (By
CC similarity). {ECO:0000250|UniProtKB:Q641J8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
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DR EMBL; CR762181; CAL49424.1; -; mRNA.
DR RefSeq; NP_001016091.1; NM_001016091.2.
DR AlphaFoldDB; Q07G42; -.
DR SMR; Q07G42; -.
DR STRING; 8364.ENSXETP00000009955; -.
DR PaxDb; Q07G42; -.
DR GeneID; 548845; -.
DR KEGG; xtr:548845; -.
DR CTD; 51132; -.
DR Xenbase; XB-GENE-492020; rlim.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; Q07G42; -.
DR OrthoDB; 1487241at2759; -.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0060816; P:random inactivation of X chromosome; IBA:GO_Central.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..639
FT /note="E3 ubiquitin-protein ligase RNF12"
FT /id="PRO_0000314058"
FT ZN_FING 585..626
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 636..639
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 70700 MW; 88CFC8B4E2EB7828 CRC64;
MESADSAGKG STEQSESQRQ SQMDRLDREE AFYQFVNNLN EDDYRLMRDN NLLGTPGEIT
KEELLRRLQQ IKEGPPQPST EGTRGDPVSA SGDPAEDSSN GDSIIDWLNS VRQTGNTTRS
GQRGNQSWRA VSRTNPNSGD FRFSLEINVN RTSGNPSMPS LEQSSEMPGA EDMEVSSQGE
NENEPEPVAP RVAQAEVTEE APVQRGQRRA RSRSPDQRRT RARTDRSRSP LHQAVEPPIR
RAQHSSSQTV DASSTEEAEG SSRTRHHVSS QMQNSSSSNE TEGSSRTRQH ITARQQALGT
EGQSQSQTQT QSQSQTQTQS QTQSQSTVHL SNPESRSSSQ PPQTDSSSNA ETTGTGQRPP
TIVLDLQVRR VRPGDYRQRD SIANRTRSRS QTPNNTVTYE SERGGFRRTF SRSERAGVRT
YVSTIRIPIR RILNTGLSET TSVAIQTMLR QIMTGFGELS YFMYNDNDTD PNNPTPVSPP
AAVPGEAQNL VSPEPPAPIV EPPEPVAPVE SEEGSNVSTS SARREGRNSR GGVTFEESGS
LPFLSLAQFF LLNEDDDDQP RGLTKEQIDN LSTRNFGEND ALKTCSVCIT EYTEGNKLRK
LPCSHEYHVH CIDRWLSENS TCPICRRAVL VAGNRESIV
