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   29-MAY-2024, entry version 164.
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; 10090-ENSMUSP00000091898; -.
DR   ProteomicsDB; 295913; -.
DR   Antibodypedia; 22273; 109 antibodies from 19 providers.
DR   DNASU; 22652; -.
DR   Ensembl; ENSMUST00000094340.4; ENSMUSP00000091898.4; ENSMUSG00000070527.4.
DR   GeneID; 22652; -.
DR   KEGG; mmu:22652; -.
DR   UCSC; uc009hfi.1; mouse.
DR   AGR; MGI:2181178; -.
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; HGEICDM; -.
DR   OrthoDB; 2906101at2759; -.
DR   PhylomeDB; Q60764; -.
DR   TreeFam; TF315108; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 22652; 3 hits in 80 CRISPR screens.
DR   PRO; PR:Q60764; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q60764; Protein.
DR   Bgee; ENSMUSG00000070527; Expressed in medial ganglionic eminence and 106 other cell types or tissues.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd16730; RING-HC_MKRN1_3; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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:SF38; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-3-RELATED; 1.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   Pfam; PF15815; MKRN1_C; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF14608; zf-CCCH_2; 2.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
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
//