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MKRN2_XENTR
ID   MKRN2_XENTR             Reviewed;         418 AA.
AC   Q6GLD9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAH74559.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
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 (By
CC       similarity). Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA
CC       expression (By similarity). {ECO:0000250|UniProtKB:B0F0H3,
CC       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}.
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DR   EMBL; BC074559; AAH74559.1; -; mRNA.
DR   RefSeq; NP_001005447.1; NM_001005447.1.
DR   AlphaFoldDB; Q6GLD9; -.
DR   PaxDb; Q6GLD9; -.
DR   DNASU; 448038; -.
DR   GeneID; 448038; -.
DR   KEGG; xtr:448038; -.
DR   CTD; 23609; -.
DR   Xenbase; XB-GENE-5879487; mkrn2.
DR   eggNOG; KOG1039; Eukaryota.
DR   InParanoid; Q6GLD9; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030274; F:LIM domain binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0009798; P:axis specification; ISS:BHF-UCL.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1901485; P:positive regulation of transcription factor catabolic process; ISS:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
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; IPR027370; Znf-RING_LisH.
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; PF00642; zf-CCCH; 1.
DR   Pfam; PF18044; zf-CCCH_4; 2.
DR   Pfam; PF13445; zf-RING_UBOX; 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..418
FT                   /note="E3 ubiquitin-protein ligase makorin-2"
FT                   /id="PRO_0000361050"
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         164..191
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         237..291
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         320..349
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          76..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..221
FT                   /note="Makorin-type Cys-His"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46881 MW;  C3DC5EC3F3ABDC1E CRC64;
     MNTKHVTCRY FLHGVCREGG RCLFSHDLAT SKPSTVCRFY QRGQCAYGAR CRYDHVKPCN
     GSVFYPPQEM APAPLESTPP LLPTQEAAAP VTKSAPQRRE KKSVVLRDRD LCGASVEKAH
     PDPALRPGCA ADPPVSELEA KPHSYLEAIC TGLDETPIPS AYPDAPQQLC PFAQAGGCHY
     GESCPYIHGN VCEICGLQVL HPYDQEQRGH HEKLCMANFE RDMERAFAFQ ASEGKVCSIC
     MERVYDKQSP SERRFGILSN CHHTYCLACI RQWRCARQFE NPVIKSCPEC RVISEFVIPS
     AYWVEDQSKK FELIEAFKQG MGKKACKYFD QGRGTCPFGG KCLYLHAYPD GTRAEPEKPR
     KQLGSEGTVR FLNSVRLWDF IEEREQRNLP DAEDEVAELG ELFMHLSGVG EEPPAASN
 
 
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