MKRN3_MOUSE
ID MKRN3_MOUSE Reviewed; 544 AA.
AC Q60764; Q3UY92; Q7TQE4;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable E3 ubiquitin-protein ligase makorin-3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase makorin-3 {ECO:0000305};
DE AltName: Full=Zinc finger protein 127;
GN Name=Mkrn3; Synonyms=Zfp127, Znf127;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10196368; DOI=10.1093/hmg/8.5.795;
RA Jong M.T.C., Carey A.H., Caldwell K.A., Lau M.H., Handel M.A.,
RA Driscoll D.J., Stewart C.L., Rinchik E.M., Nicholls R.D.;
RT "Imprinting of a RING zinc-finger encoding gene in the mouse chromosome
RT region homologous to the Prader-Willi syndrome genetic region.";
RL Hum. Mol. Genet. 8:795-803(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IMPRINTING.
RX PubMed=10395905; DOI=10.1016/s0378-1119(99)00192-4;
RA Hershko A., Razin A., Shemer R.;
RT "Imprinted methylation and its effect on expression of the mouse Zfp127
RT gene.";
RL Gene 234:323-327(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12971993; DOI=10.1016/s1567-133x(03)00113-3;
RA Lee S., Walker C.L., Wevrick R.;
RT "Prader-Willi syndrome transcripts are expressed in phenotypically
RT significant regions of the developing mouse brain.";
RL Gene Expr. Patterns 3:599-609(2003).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=23738509; DOI=10.1056/nejmoa1302160;
RA Abreu A.P., Dauber A., Macedo D.B., Noel S.D., Brito V.N., Gill J.C.,
RA Cukier P., Thompson I.R., Navarro V.M., Gagliardi P.C., Rodrigues T.,
RA Kochi C., Longui C.A., Beckers D., de Zegher F., Montenegro L.R.,
RA Mendonca B.B., Carroll R.S., Hirschhorn J.N., Latronico A.C., Kaiser U.B.;
RT "Central precocious puberty caused by mutations in the imprinted gene
RT MKRN3.";
RL N. Engl. J. Med. 368:2467-2475(2013).
CC -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC ubiquitin moieties onto substrate proteins. {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 -!- TISSUE SPECIFICITY: Expressed in testis, brain, heart and kidney.
CC Ubiquitously detected at low levels throughout the entire embryo, but
CC expression is highest in the ventricular layers of the brain.
CC {ECO:0000269|PubMed:10196368, ECO:0000269|PubMed:12971993}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the blastocyst stage and the
CC embryonic days 8-17, as well as in undifferentiated and differentiated
CC embryonic stem cells. Expressed in the arcuate nucleus of both male and
CC female animals. Levels of expression are highest on postnatal days 10
CC and 12, begin to decline on day 15, and reaches a nadir by days 18 to
CC 22, at which time expression is 10 to 20% of the levels detected at 10
CC days. The timing of the decline in protein expression correlated with
CC the ages at which arcuate KISS1 and TAC2 have been shown to increase,
CC heralding the onset of puberty. {ECO:0000269|PubMed:10196368,
CC ECO:0000269|PubMed:23738509}.
CC -!- MISCELLANEOUS: Imprinted, expressed from the paternal chromosome only.
CC The maternal methylation is established promptly after fertilization
CC prior to syngamy.
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DR EMBL; U19106; AAA76863.1; -; Genomic_DNA.
DR EMBL; AK134870; BAE22320.1; -; mRNA.
DR EMBL; BC054771; AAH54771.1; -; mRNA.
DR CCDS; CCDS21327.1; -.
DR RefSeq; NP_035876.2; NM_011746.2.
DR AlphaFoldDB; Q60764; -.
DR BioGRID; 204637; 1.
DR STRING; 10090.ENSMUSP00000091898; -.
DR iPTMnet; Q60764; -.
DR PhosphoSitePlus; Q60764; -.
DR MaxQB; Q60764; -.
DR PaxDb; Q60764; -.
DR PRIDE; Q60764; -.
DR ProteomicsDB; 295913; -.
DR Antibodypedia; 22273; 94 antibodies from 18 providers.
DR DNASU; 22652; -.
DR Ensembl; ENSMUST00000094340; ENSMUSP00000091898; ENSMUSG00000070527.
DR GeneID; 22652; -.
DR KEGG; mmu:22652; -.
DR UCSC; uc009hfi.1; mouse.
DR CTD; 7681; -.
DR MGI; MGI:2181178; Mkrn3.
DR VEuPathDB; HostDB:ENSMUSG00000070527; -.
DR eggNOG; KOG1039; Eukaryota.
DR GeneTree; ENSGT00950000183077; -.
DR HOGENOM; CLU_040815_4_1_1; -.
DR InParanoid; Q60764; -.
DR OMA; SEDQWDL; -.
DR OrthoDB; 1388677at2759; -.
DR PhylomeDB; Q60764; -.
DR TreeFam; TF315108; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22652; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q60764; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q60764; protein.
DR Bgee; ENSMUSG00000070527; Expressed in medial ganglionic eminence and 104 other tissues.
DR Genevisible; Q60764; MM.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026294; Makorin_3.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR031644; MKRN1_C.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224; PTHR11224; 2.
DR PANTHER; PTHR11224:SF38; PTHR11224:SF38; 2.
DR Pfam; PF15815; MKRN1_C; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..544
FT /note="Probable E3 ubiquitin-protein ligase makorin-3"
FT /id="PRO_0000055960"
FT ZN_FING 92..119
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 274..301
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 347..401
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 430..459
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..329
FT /note="Makorin-type Cys-His"
FT CONFLICT 154
FT /note="A -> V (in Ref. 1; AAA76863)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="M -> V (in Ref. 1; AAA76863)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="S -> T (in Ref. 1; AAA76863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 59434 MW; AD9DF187A253D69B CRC64;
MEESTAPIEA HAAAGAEAGA EGGEGVSVPP PPQFEAAGAS AGVSSAPLQQ ASGLAPLLVT
PGPAIRRAAS LRPAPAEGGG ARSGPERNSG SWTKQILCRY YLHGQCKEGD NCRYSHDLSG
RRRSRGGQDA QPRASADRGP KMATRWEPPT QEVAEAPPAA SSSSLPLIGS AAERGFTEAE
IDNAGIRSAA ERGFSEAEID NASLAAGAAA GAGAEGWEGA IEFVPGQPYR GRMVPPHGPE
APLQSPAIER EHMAMGMGMP MPVPMPMPVP MPVPMPLPLC RYAARGQCLR GDRCAYPHGE
ICDMCGQQAL HPWDAAQQEA HRRACVEAHE RDMELSFAVQ RSMDKVCGIC MEVVYEKADP
SDRRFGILFS CNHTYCLRCI RRWRSATQFE NRISKSCPQC RVSSGFVIPS EFWVEEEEEK
EKLVQQYKEG MSQKACRYFA GGLGHCPFGE FCFYKHEYPE GWRDQPPRPD GGGSSSAYWH
QVLEPVQLRE GNVLFKSRKK EHSVLRLANQ LLKKLLCLRG SSSFSDDRWL LLQYQLEEYF
SLNL
