RF12B_XENLA
ID RF12B_XENLA Reviewed; 757 AA.
AC Q7T037;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=E3 ubiquitin-protein ligase RNF12-B;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 12-B;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF12-B {ECO:0000305};
DE AltName: Full=XRnf12B;
GN Name=rnf12-b;
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:BAC81442.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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 (By
CC similarity). {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 -!- 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 levels remaining
CC constant throughout early embryogenesis, with a slight increase at the
CC late gastrula stage. {ECO:0000269|PubMed:12874135}.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
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DR EMBL; AB114040; BAC81442.1; -; mRNA.
DR RefSeq; NP_001108244.1; NM_001114772.1.
DR AlphaFoldDB; Q7T037; -.
DR SMR; Q7T037; -.
DR GeneID; 100137618; -.
DR KEGG; xla:100137618; -.
DR CTD; 100137618; -.
DR Xenbase; XB-GENE-6256130; rlim.L.
DR OrthoDB; 789313at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 100137618; 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; 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: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: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; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..757
FT /note="E3 ubiquitin-protein ligase RNF12-B"
FT /id="PRO_0000314057"
FT REPEAT 197..202
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 203..208
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 209..214
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 215..220
FT /note="4"
FT /evidence="ECO:0000255"
FT REPEAT 221..226
FT /note="5"
FT /evidence="ECO:0000255"
FT REPEAT 227..232
FT /note="6"
FT /evidence="ECO:0000255"
FT REPEAT 237..242
FT /note="7"
FT /evidence="ECO:0000255"
FT REPEAT 243..248
FT /note="8"
FT /evidence="ECO:0000255"
FT REPEAT 249..254
FT /note="9"
FT /evidence="ECO:0000255"
FT REPEAT 255..260
FT /note="10"
FT /evidence="ECO:0000255"
FT REPEAT 261..266
FT /note="11"
FT /evidence="ECO:0000255"
FT REPEAT 267..272
FT /note="12"
FT /evidence="ECO:0000255"
FT REPEAT 273..278
FT /note="13"
FT /evidence="ECO:0000255"
FT REPEAT 279..284
FT /note="14"
FT /evidence="ECO:0000255"
FT REPEAT 285..290
FT /note="15"
FT /evidence="ECO:0000255"
FT REPEAT 291..296
FT /note="16"
FT /evidence="ECO:0000255"
FT REPEAT 297..302
FT /note="17"
FT /evidence="ECO:0000255"
FT REPEAT 303..308
FT /note="18"
FT /evidence="ECO:0000255"
FT REPEAT 309..314
FT /note="19"
FT /evidence="ECO:0000255"
FT REPEAT 315..320
FT /note="20"
FT /evidence="ECO:0000255"
FT REPEAT 321..326
FT /note="21"
FT /evidence="ECO:0000255"
FT ZN_FING 703..744
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..326
FT /note="21 X 6 AA approximate repeats of P-[EV]-S-V-[PA]-
FT [EV]"
FT /evidence="ECO:0000255"
FT REGION 588..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 754..757
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 92..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 82892 MW; 50E950B17A67F350 CRC64;
MESADSTGKG STEQSESQRQ SQMDRLDREE AFYQFVNNLN DEDYRLMRDN NLLGTPGEIT
KEELLQRLQQ IKEGPPQPST EETRGDSVST GEDPAEDSSN GDSIIDWLNS VRQTGNTTRS
GQRGNQSWRA VSRTNPNSGD FRFSLEINVN RTSGTASMPS LDQSAEMPGP EDMEVSSQGE
AENVPEPETV PESIREPESV DEPVSVAEPV SVAEPVSVAE PESVAEPESV AASVPVPESV
PEPESVPEPE SVPEPESVPE PESVPEPESV PEPESVPEPE SVPEPESVPE PESVPEPESV
PEPESVPEPE SIAEPESVPV PESVPVATRP APVEVTVEEA PIQRGQRRAR SRSPDQRRTR
ARTDRSRSPL YQTVDPPIRR AQHSSSQTVD ASNTEEAEGS SRTRHHVSSQ VHSSSSNETE
GSSRTRQHIT ARQQALGTEG QSQSTVHLSN PESRSSSQTP QTDSPSNAET TGTGQRPPTI
VLDLQVRRVR PGDYRQRDSI ANRTRSRSQT PNNTVTYESE RGGFRRTFSR SERAGVRTYV
STIRIPIRRI LNTGLSETTS VAIQTMLRQI MTGFGELSYF MYNDNDADPN NPTAVSPPAA
VPGEVQNNPS AEVRAPIAEP AEPVAPVESD EGSNVATSAT RREGRNSRGG VTLEESGSLP
FLSLAQFFLL NEDDDDQPRG LTKEQIDNLS TRNYGENDAL KTCSVCITEY TEGNKLRKLP
CSHEYHIHCI DRWLSENSTC PICRRAVLVA GNRESIV
