RN212_MOUSE
ID RN212_MOUSE Reviewed; 307 AA.
AC F6TQD1; Q8BN46;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Probable E3 SUMO-protein ligase RNF212;
DE EC=2.3.2.-;
DE AltName: Full=Probable E3 SUMO-protein transferase RNF212 {ECO:0000305};
DE AltName: Full=RING finger protein 212;
GN Name=Rnf212;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23396135; DOI=10.1038/ng.2541;
RA Reynolds A., Qiao H., Yang Y., Chen J.K., Jackson N., Biswas K.,
RA Holloway J.K., Baudat F., de Massy B., Wang J., Hoog C., Cohen P.E.,
RA Hunter N.;
RT "RNF212 is a dosage-sensitive regulator of crossing-over during mammalian
RT meiosis.";
RL Nat. Genet. 45:269-278(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24390283; DOI=10.1038/ng.2858;
RA Qiao H., Prasada Rao H.B., Yang Y., Fong J.H., Cloutier J.M., Deacon D.C.,
RA Nagel K.E., Swartz R.K., Strong E., Holloway J.K., Cohen P.E.,
RA Schimenti J., Ward J., Hunter N.;
RT "Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212
RT regulate meiotic recombination.";
RL Nat. Genet. 46:194-199(2014).
CC -!- FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over
CC during meiosis: required to couple chromosome synapsis to the formation
CC of crossover-specific recombination complexes. Localizes to
CC recombination sites and stabilizes meiosis-specific recombination
CC factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11.
CC May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to
CC enhance their binding to recombination sites. Acts as a limiting factor
CC for crossover designation and/or reinforcement and plays an antagonist
CC role with CCNB1IP1/HEI10 in the regulation of meiotic recombination.
CC {ECO:0000269|PubMed:23396135, ECO:0000269|PubMed:24390283}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the
CC synaptonemal complex. Localizes to a minority of double-strand breaks
CC (DSBs) sites. Marks crossover sites during midpachynema.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F6TQD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F6TQD1-2; Sequence=VSP_046302, VSP_046303;
CC -!- TISSUE SPECIFICITY: Specifically expressed in meiocytes of the gonads.
CC {ECO:0000269|PubMed:23396135}.
CC -!- DEVELOPMENTAL STAGE: In spermatocytes, first detected at the transition
CC from leptonema to zygonema, localizing specifically to initial sites of
CC homolog synapsis. The number of synaptonemal complex-associated Rnf212
CC increases as synapsis proceeds. Excluded from unsynapsed homolog. In
CC early pachynema, as cells complete synapsis, detected as a punctate
CC pattern of irregular foci along the synaptonemal complexes. Also
CC localizes to the synapsed pseudoautosomal regions of the X-Y
CC chromosomes. After early pachynema, protein levels strongly drop. By
CC midpachynema, Rnf212 foci only remain at sites where crossovers form.
CC Remaining foci disappear in late pachynema before the disassembly of
CC synaptonemal complexes at diplonema and are not detected in early
CC diplotene-stage cells in which homologs begin to desynapse. Pattern in
CC fetal oocytes is very similar, except that the late-stage Rnf212 foci
CC are still detected in nuclei in both the late-pachytene and early
CC diplotene stages (at protein level). {ECO:0000269|PubMed:23396135,
CC ECO:0000269|PubMed:24390283}.
CC -!- DISRUPTION PHENOTYPE: Both male and female mice are sterile. Males do
CC not make sperm and have much smaller testes, a characteristic of
CC mutants with meiotic defects. Testes show an absence of post-anaphase I
CC cells, indicating loss of spermatocytes at this stage (stage XII
CC seminiferous tubules). In females, ovary size is similar to that of
CC wild-type animals, and high numbers of oocytes are present in mature
CC animals. Complete synapsis is achieved but crossover complexes are
CC absent. Rnf212 is haploinsufficient: although herozygous males are
CC fertile and have wild-type sperm counts, they show significantly fewer
CC Mlh1 foci and fewer chiasmata. Haploinsufficiency suggests that Rnf212
CC is a limiting factor for crossover designation and/or reinforcement.
CC {ECO:0000269|PubMed:23396135}.
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DR EMBL; AK089585; BAC40927.1; -; mRNA.
DR EMBL; AC123743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS89962.1; -. [F6TQD1-1]
DR AlphaFoldDB; F6TQD1; -.
DR SMR; F6TQD1; -.
DR STRING; 10090.ENSMUSP00000063525; -.
DR iPTMnet; F6TQD1; -.
DR PhosphoSitePlus; F6TQD1; -.
DR PaxDb; F6TQD1; -.
DR PRIDE; F6TQD1; -.
DR ProteomicsDB; 300539; -. [F6TQD1-1]
DR Antibodypedia; 22203; 127 antibodies from 25 providers.
DR Ensembl; ENSMUST00000196652; ENSMUSP00000143556; ENSMUSG00000055385. [F6TQD1-2]
DR Ensembl; ENSMUST00000212212; ENSMUSP00000148758; ENSMUSG00000055385. [F6TQD1-1]
DR UCSC; uc008ypb.1; mouse. [F6TQD1-1]
DR UCSC; uc008ypc.1; mouse. [F6TQD1-2]
DR MGI; MGI:3645767; Rnf212.
DR VEuPathDB; HostDB:ENSMUSG00000055385; -.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR InParanoid; F6TQD1; -.
DR OMA; VCCNSCF; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:F6TQD1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; F6TQD1; protein.
DR Bgee; ENSMUSG00000055385; Expressed in bone marrow and 28 other tissues.
DR ExpressionAtlas; F6TQD1; baseline and differential.
DR GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; IMP:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0006311; P:meiotic gene conversion; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22663; PTHR22663; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Meiosis; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..307
FT /note="Probable E3 SUMO-protein ligase RNF212"
FT /id="PRO_0000421995"
FT ZN_FING 7..46
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 164..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..124
FT /evidence="ECO:0000255"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046302"
FT VAR_SEQ 217..307
FT /note="VPPLQMPYKELSPPPASQLSSRATQGPSPSVSSSWTGPPRQPISISGLLQRQ
FT CAGSASPRGMDTEKMSPFLPSTPTNLRSVASPWHACVHR -> ISIP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046303"
SQ SEQUENCE 307 AA; 33898 MW; C0C47B8D8179DBCD CRC64;
MASWVFCNRC FQSPHRKSSF SLTSCGHVYC HSCLLKGTKN ECVICQAPCQ TVLLSKHTNS
NIQTFFLGID GLCKKYSQET SQISEFQEKH RRRLVAFYQE KISQLEESLR KSVLQIKQLQ
SMRSSQQPAF NKIKNSVSTK PNGYLFLPPN SSLPDRIESM DIDLTPPARK PEMSAGPSRI
SVISPPQDGR MGSVTCRGPQ HLSLTPSHAS MTKASRVPPL QMPYKELSPP PASQLSSRAT
QGPSPSVSSS WTGPPRQPIS ISGLLQRQCA GSASPRGMDT EKMSPFLPST PTNLRSVASP
WHACVHR
