ID   MKRN2_SERQU             Reviewed;         423 AA.
AC   Q9DD48;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=E3 ubiquitin-protein ligase makorin-2;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9ERV1};
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-2 {ECO:0000305};
DE   AltName: Full=Zinc finger protein YGHLC3HC4;
GN   Name=mkrn2; Synonyms=yghl2, yghlc3hc4;
OS   Seriola quinqueradiata (Five-ray yellowtail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=8161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Gill, and Testis;
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 (By similarity). Inhibits
CC       neurogenesis and axis formation during embryonic development by
CC       modulating the phosphatidylinositol 3-kinase (PI3K) pathway. Acts
CC       downstream of PI3K and akt1 to up-regulate gsk3b mRNA expression.
CC       {ECO:0000250|UniProtKB:B0F0H3, ECO:0000250|UniProtKB:Q9ERV1}.
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; Evidence={ECO:0000250|UniProtKB:Q9ERV1};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9ERV1}.
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DR   EMBL; AB047517; BAB18861.1; -; Genomic_DNA.
DR   EMBL; AB049436; BAB18815.1; -; mRNA.
DR   EMBL; AB049437; BAB39861.1; -; mRNA.
DR   EMBL; AB049438; BAB39862.1; -; mRNA.
DR   EMBL; AB049439; BAB39863.1; -; mRNA.
DR   AlphaFoldDB; Q9DD48; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR026293; Makorin_2.
DR   InterPro; IPR045072; MKRN-like.
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; 1.
DR   PANTHER; PTHR11224:SF17; PTHR11224:SF17; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
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   Cytoplasm; Developmental protein; Differentiation; Metal-binding;
KW   Neurogenesis; Nucleus; Repeat; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..423
FT                   /note="E3 ubiquitin-protein ligase makorin-2"
FT                   /id="PRO_0000055958"
FT   ZN_FING         2..29
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         31..58
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         162..189
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         235..289
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         318..347
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          59..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..219
FT                   /note="Makorin-type Cys-His"
SQ   SEQUENCE   423 AA;  46376 MW;  AFABF7AB14E86997 CRC64;
     MSTKQVTCRY FLHGVCREGS RCLFSHDLNN SKPSTICKFY QRGVCAYGER CRYDHIKPSS
     RGGGGGAPED QAGGGGAGGG GAGIGGAGGG PSVRGGMKKN LVLRDRVLGV DRVDRMFGAP
     ADSMWSDVST AAAPHSYVEA IRTGLDASAQ DQATPPVCGP SQNLPQLCPY AANGHCFYEE
     NCTYLHGDLC EVCGLQVLHP HDSEQRRAHE KMCLAAFEAD MEKAFAAQLS QDKVCSICME
     VVVQKANPSD RRFGILSSCC HTFCLACIRK WRCTRTFSNT IIKSCPECRV VSEFVIPSVY
     WVEDQEDKDH LIDLFKSGVS KKACKYFDQG RGSCPFGGKC LYLHAFPDGT RAEPDRPRKQ
     LSSEGNVRFM NSVRLWDFIE EREQRSVPPL PALDDDMAEL RELFMQMSGP SHDGPETPPT
     ADQ