ID   MGRN1_DANRE             Reviewed;         529 AA.
AC   Q7ZUL9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase MGRN1;
DE            EC=2.3.2.27;
DE   AltName: Full=Mahogunin RING finger protein 1;
DE   AltName: Full=RING-type E3 ubiquitin transferase MGRN1 {ECO:0000305};
GN   Name=mgrn1;
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 MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. Acts also as a negative
CC       regulator of hedgehog signaling. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q9D074}.
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   -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC       {ECO:0000250}.
CC   -!- PTM: Autoubiquitinated in vitro. {ECO:0000250}.
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DR   EMBL; BC048069; AAH48069.1; -; mRNA.
DR   AlphaFoldDB; Q7ZUL9; -.
DR   STRING; 7955.ENSDARP00000068493; -.
DR   PaxDb; Q7ZUL9; -.
DR   ZFIN; ZDB-GENE-030131-6192; mgrn1a.
DR   eggNOG; KOG4265; Eukaryota.
DR   InParanoid; Q7ZUL9; -.
DR   PhylomeDB; Q7ZUL9; -.
DR   TreeFam; TF314969; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q7ZUL9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR   GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996; PTHR22996; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..529
FT                   /note="Probable E3 ubiquitin-protein ligase MGRN1"
FT                   /id="PRO_0000246690"
FT   ZN_FING         275..314
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          341..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  58146 MW;  6453F6BF5E55D8A1 CRC64;
     MGSILSRRIA GVEDIDIQAN SAYRYPPKSG NYFTSHFFMG GEKFDTPHPE GYLFGENMDL
     NFLGNRPVQF PYVTPAAHEP VKTLRSLVNI RKDSLRLVRY KDDSDSTPED TGDPRVLYSV
     EFCFDTDARV AITLYCQAFE EFANGMAIYS AKSPSMVSET VHYKRGINQQ FSLPSFKIDF
     TKWKPEELNF DLDKGVFPLV VQAIVDDGDD VTGHAHVLLA AFERHVDGSF SVKPLKQKQI
     VDRVSYLLQE IYGIENRNNQ ETKSTEDENS DNSSECVVCL SDLRDTLILP CRHLCLCNAC
     ADTLRYQANN CPICRLPFRA LLQIRAVRKK TAATLSPVSF SPVLSQSSDH TEHSNADNIP
     PGYEPISLLE ALNGVQPVSP SIPSAPLYEE IQFSGEMGDP LNLTGRQQNG DPGALKGKGS
     KSPDGSVRSP SSPIQEEEDE ERLSELSDAQ PQSVLPCSLS PSEDTVEGVT AKPGLPNSGS
     ESRSLGVSVS EILQDCHSER SSLSQSESDP SADLALPASE SWSTAVEEC