ID   MKRN2_TAKRU             Reviewed;         402 AA.
AC   Q5NU13;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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};
GN   Name=mkrn2 {ECO:0000312|EMBL:BAD80900.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary {ECO:0000312|EMBL:BAD80900.1};
RA   Abe S., Kobayashi Y.;
RT   "Takifugu rubripes mRNA for MKRN2, complete CDS.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Although the makorin-type Cys-His region lacks the final His
CC       residue, the following Asp residue may be able to coordinate Zn(2+).
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB182270; BAD80900.1; -; mRNA.
DR   RefSeq; NP_001072101.1; NM_001078633.1.
DR   AlphaFoldDB; Q5NU13; -.
DR   STRING; 31033.ENSTRUP00000007391; -.
DR   GeneID; 778013; -.
DR   KEGG; tru:778013; -.
DR   CTD; 23609; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   InParanoid; Q5NU13; -.
DR   OrthoDB; 1388677at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005226; Unplaced.
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; IPR041686; Znf-CCCH_3.
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:SF17; PTHR11224:SF17; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF15663; zf-CCCH_3; 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; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..402
FT                   /note="E3 ubiquitin-protein ligase makorin-2"
FT                   /id="PRO_0000361048"
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         141..168
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         214..268
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         297..326
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          169..198
FT                   /note="Makorin-type Cys-His"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   402 AA;  44990 MW;  AD13478CA2A02B27 CRC64;
     MTTKQVTCRY FLHGVCREGN HCQFSHDPSS SKPSTICKFY QRGTCAYGER CRYDHVKLSS
     RGGGAFDMAG VGGARDGAST RGAAKKTFVH QERENMFRAP AESFGADVMA PAPHTYVDAI
     RTGLSSSSQD HTPPTMAGVN QDLPRLCPYA AVGHCYYEEN CIYLHGDKCE VCGLQVLDPH
     NPEQRSMHEK MCLLAFEADM EKAFAVQLSQ EKVCSICMEV VVQKMNPSDR RFGILSSCCH
     VFCLACIRKW RCTRNFSNKI IKSCPECRVA SEFVIPSVYW EENQEDKVHL IELFKSGVGK
     KPCKYFDQGR GSCPFGGKCL YLHALPDGSR AEPEQPRKQL GSEGNIRFMN SVRLWDFIEE
     REQHSAPPLQ AFADDISELR ELFVQMSGPS PDEGESQSRS AP