RF12A_XENLA
ID RF12A_XENLA Reviewed; 622 AA.
AC Q641J8; Q7T038;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase RNF12-A;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 12-A;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF12-A {ECO:0000305};
DE AltName: Full=XRnf12;
GN Name=rnf12-a; Synonyms=rnf12 {ECO:0000303|PubMed:12874135};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC81441.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH LDB1;
RP LHX1; LHX3 AND LHX5, HOMODIMERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF HIS-591 AND CYS-594.
RC TISSUE=Gastrula {ECO:0000269|PubMed:12874135};
RX PubMed=12874135; DOI=10.1242/dev.00621;
RA Hiratani I., Yamamoto N., Mochizuki T., Ohmori S.-Y., Taira M.;
RT "Selective degradation of excess Ldb1 by Rnf12/RLIM confers proper Ldb1
RT expression levels and Xlim-1/Ldb1 stoichiometry in Xenopus organizer
RT functions.";
RL Development 130:4161-4175(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH82339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH82339.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) 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:0000269|PubMed:12874135}.
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.
CC {ECO:0000269|PubMed:12874135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q641J8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12874135};
CC IsoId=Q641J8-2; Sequence=VSP_052632;
CC -!- TISSUE SPECIFICITY: Shows overlapping expression with lhx1/lim1 and
CC ldb1 in the gastrula mesoderm, and expression overlaps with ldb1
CC throughout early embryogenesis. After gastrulation, expression is
CC gradually restricted to tissues originated from the ectoderm, the
CC neuroectoderm, neural crest and epidermis, and subsequently to the
CC neural tube as well as the head and tailbud region.
CC {ECO:0000269|PubMed:12874135}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at the cleavage stage, with expression disappearing at the
CC gastrula stage. {ECO:0000269|PubMed:12874135}.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
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DR EMBL; AB114039; BAC81441.1; -; mRNA.
DR EMBL; BC082339; AAH82339.1; -; mRNA.
DR RefSeq; NP_001082725.1; NM_001089256.1. [Q641J8-1]
DR RefSeq; XP_018087398.1; XM_018231909.1. [Q641J8-1]
DR RefSeq; XP_018087399.1; XM_018231910.1. [Q641J8-2]
DR AlphaFoldDB; Q641J8; -.
DR SMR; Q641J8; -.
DR BioGRID; 100010; 1.
DR MaxQB; Q641J8; -.
DR DNASU; 398680; -.
DR GeneID; 398680; -.
DR KEGG; xla:398680; -.
DR CTD; 398680; -.
DR Xenbase; XB-GENE-866117; rlim.S.
DR OMA; HHNISSQ; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 398680; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..622
FT /note="E3 ubiquitin-protein ligase RNF12-A"
FT /id="PRO_0000314056"
FT ZN_FING 568..609
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 619..622
FT /note="PDZ-binding"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:12874135"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 85..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12874135"
FT /id="VSP_052632"
FT MUTAGEN 591
FT /note="H->A: Almost completely abolishes suppression of
FT secondary axis formation and organizer function, and
FT disrupts ldb1 ubiquitination; when associated with A-594."
FT /evidence="ECO:0000269|PubMed:12874135"
FT MUTAGEN 594
FT /note="C->A: Almost completely abolishes suppression of
FT secondary axis formation and organizer function, and
FT disrupts ldb1 ubiquitination; when associated with A-591."
FT /evidence="ECO:0000269|PubMed:12874135"
SQ SEQUENCE 622 AA; 68901 MW; 34F224E534698C3A CRC64;
MESADSTGKG SIEQSESQRQ SQMDRLDREE AFYQFVNNLN EDDYRLMRDN NLLGTPGEIT
KEELLRRLQQ IKEGPPQPST EETRGDSVST GGDPAEDSSN GDSIIDWLNS VRQTGNTTRS
GQRGNQSWRA VSRTNPNSGD FRFSLEINVN RTSGNPSMPS LDQSAEMPGA EDMEVSSQGE
AENEPEPIPI ATRSAPAEVT VEEAPIQRGQ RRARSRSPDQ RRTRARTDRS RSPLHHAVDP
PIRRAPHSSS QTVDTSNTEE AEGSSRTRHH VSSQVQNSSS SNETEGSSRT RQHIPARQQV
LGTEGQSQST VHLSNPETRS SSQTPQTDSS TNAETTGTGQ RPPTIVLDLQ VRRVRPGDYR
QRDSIANRTR SRSQTPNNTV TYESERGGFR RTFSRSERAG VRTYVSTIRI PIRRILNTGL
SETTSVAIQT MLRQIMTGFG ELSYFMYNDN DTDPNNPTAV SPTAAVPGEA QNNANAEVRA
PSAEPTEPVA PVETDEGSNV STTATRREGR NSRGAVTFEE SGSLPFLSLA QFFLLNEDDD
DQPRGLTKEQ IDNLSTRNFG ENDALKTCSV CITEYTEGNK LRKLPCSHEY HIHCIDRWLS
ENSTCPICRR AVLVASNRES IV
