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 27-MAR-2024, entry version 113.
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 DNASU; 448038; -.
DR Ensembl; ENSXETT00000115021; ENSXETP00000106466; ENSXETG00000043301.
DR GeneID; 448038; -.
DR KEGG; xtr:448038; -.
DR Xenbase; XB-GENE-5879487; mkrn2.
DR eggNOG; KOG1039; Eukaryota.
DR InParanoid; Q6GLD9; -.
DR OMA; MQGVCRE; -.
DR OrthoDB; 2906101at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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:0006351; P:DNA-templated transcription; ISS:UniProtKB.
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 non-canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd16731; RING-HC_MKRN2; 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; 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:SF17; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-2; 1.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF00642; zf-CCCH; 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; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
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
//
