MKRN1_DANRE
ID MKRN1_DANRE Reviewed; 439 AA.
AC Q4VBT5; Q1L8F6; Q9DFG7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable E3 ubiquitin-protein ligase makorin-1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000305};
GN Name=mkrn1 {ECO:0000312|ZFIN:ZDB-GENE-020213-1};
GN ORFNames=si:ch211-9f20.3, zgc:110403;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:CAK05024.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larval eye {ECO:0000312|EMBL:AAH95243.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG27598.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-439.
RX PubMed=11597136; DOI=10.1006/geno.2001.6627;
RA Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.;
RT "Phylogenetic conservation of the makorin-2 gene, encoding a multiple zinc-
RT finger protein, antisense to the raf1 proto-oncogene.";
RL Genomics 77:119-126(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG27598.1; Type=Miscellaneous discrepancy; Note=Possible contaminating sequence. The N-terminal 7 residues do not match the underlying genomic sequence.; Evidence={ECO:0000305};
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DR EMBL; CR792454; CAK05024.2; -; Genomic_DNA.
DR EMBL; CT826375; CAK05024.2; JOINED; Genomic_DNA.
DR EMBL; BC095243; AAH95243.1; -; mRNA.
DR EMBL; AF277173; AAG27598.1; ALT_SEQ; mRNA.
DR RefSeq; NP_694510.1; NM_152978.1.
DR AlphaFoldDB; Q4VBT5; -.
DR STRING; 7955.ENSDARP00000061069; -.
DR PaxDb; Q4VBT5; -.
DR Ensembl; ENSDART00000061070; ENSDARP00000061069; ENSDARG00000041665.
DR GeneID; 170782; -.
DR KEGG; dre:170782; -.
DR CTD; 23608; -.
DR ZFIN; ZDB-GENE-020213-1; mkrn1.
DR eggNOG; KOG1039; Eukaryota.
DR GeneTree; ENSGT00950000183077; -.
DR HOGENOM; CLU_040815_4_1_1; -.
DR InParanoid; Q4VBT5; -.
DR OMA; HNRECLE; -.
DR OrthoDB; 1388677at2759; -.
DR PhylomeDB; Q4VBT5; -.
DR TreeFam; TF315108; -.
DR Reactome; R-DRE-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-DRE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4VBT5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000041665; Expressed in muscle tissue and 25 other tissues.
DR ExpressionAtlas; Q4VBT5; baseline.
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; IPR045072; MKRN-like.
DR InterPro; IPR031644; MKRN1_C.
DR InterPro; IPR041367; Znf-CCCH_4.
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; 1.
DR Pfam; PF15815; MKRN1_C; 1.
DR Pfam; PF18044; zf-CCCH_4; 3.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
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..439
FT /note="Probable E3 ubiquitin-protein ligase makorin-1"
FT /id="PRO_0000361045"
FT ZN_FING 18..45
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 48..74
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 163..190
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 236..290
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 319..348
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 73..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..218
FT /note="Makorin-type Cys-His"
FT /evidence="ECO:0000255"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 295
FT /note="F -> L (in Ref. 3; AAG27598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49700 MW; 3F4C6D5C248EC4A5 CRC64;
MAEAAAASTA APAVIGGWTK HVTCRYFMHG LCKEGENCRY SHDLSSCKQT MICKFFQKGC
CAFGDRCRYE HTKPSKQDEV PSSKPSMPLT AAPLAGTPEP VSDGPGGTTG AQEKPQGSGA
VDWVNAAEFV PGQPYCGRAD PVLCEGPGPL IEEEYEKEQA NKEMKKQLCP YAAVGECRYG
LNCAYLHGDV CDMCGLQVLH PSDTSQRSQH IRACIEAHEK DMEISFAIQR SKDMMCGVCM
EVVFEKTNPS ERRFGILSNC CHCYCLKCIR KWRSAKQFES KIIKSCPECR ITSNFVIPSE
YWVEDKEEKQ QLIQKYKDGM GTKPCRYFDE GRGTCPFGAN CFYKHAFPDG RLEEPQPQRR
QNGSNGRNRN TRRTHLWDLL DERENSDSFD NEDEEMVRFE LSEMLLMLLA AGTDDDVTDS
EDEWDLFHEE LDDYYELYL
