ID   MYLIB_DANRE             Reviewed;         464 AA.
AC   Q05AK5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=E3 ubiquitin-protein ligase MYLIP-B {ECO:0000250|UniProtKB:Q6TEM9};
DE            EC=2.3.2.27;
DE   AltName: Full=Myosin regulatory light chain-interacting protein B;
DE            Short=MIR-B;
DE   AltName: Full=RING-type E3 ubiquitin transferase MYLIP-B {ECO:0000305};
GN   Name=mylipb {ECO:0000312|ZFIN:ZDB-GENE-061027-67}; ORFNames=zgc:153767;
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] {ECO:0000312|EMBL:AAI24451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAI24451.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of myosin regulatory light chain
CC       (MRLC). Regulates cell movements during gastrulation by acting
CC       downstream of fz7 to antagonize the frizzled-signaling pathway (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with anxa5. {ECO:0000250|UniProtKB:Q6TEM9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q6TEM9}.
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; BC124450; AAI24451.1; -; mRNA.
DR   RefSeq; NP_001073491.1; NM_001080022.2.
DR   AlphaFoldDB; Q05AK5; -.
DR   SMR; Q05AK5; -.
DR   STRING; 7955.ENSDARP00000071903; -.
DR   PaxDb; Q05AK5; -.
DR   GeneID; 565911; -.
DR   KEGG; dre:565911; -.
DR   CTD; 565911; -.
DR   ZFIN; ZDB-GENE-061027-67; mylipb.
DR   eggNOG; ENOG502QV76; Eukaryota.
DR   InParanoid; Q05AK5; -.
DR   OrthoDB; 1340284at2759; -.
DR   PhylomeDB; Q05AK5; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q05AK5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13195; FERM_C_MYLIP_IDOL; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR041790; MYLIP_FERM_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Gastrulation; Metal-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..464
FT                   /note="E3 ubiquitin-protein ligase MYLIP-B"
FT                   /id="PRO_0000365452"
FT   DOMAIN          1..279
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   ZN_FING         381..416
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   464 AA;  52661 MW;  C9B99363E62D7C54 CRC64;
     MLCHITRPDS VVLEVEVDPK ANGEDILNKI CQKMGIIEVD YFGLQFTGTK GESLWMNLRN
     RICQEVDCVS PCRLRLRVKF FVEPHLILQE QTRHLFLMHV KEEIIKGSLR LDAEQAIELC
     ALLAQAEFGD YKQNTAKYCY SQIYGQDPSH DTINTISLKH KSLEGVSQAS AEYQALQLVS
     SLTYYGVEWH FARDSEGQQL LIGVGQEGLF VCKSDFTPIE RLMYPVIQMA TQSGRNVYVT
     ITKDNGDSVV LLFKFVSPSA ANGLYRAITE IHAFYRCDTV MSTVKMQYSR DFKGHLASLF
     LNESIDLGKR YIFDIQRTSK EVYDRTRRAL FNAGVSVNGR GISRSLLRQT KVDREERMCV
     DCRETHVLKE KLQRLQEALT CALCCEQEIS AAFCPCGHMF CCYNCASQLQ CCPVCRSEVD
     RVQHVYLPTC ASLLGLAEAK TTNSVLRRTG ISEDCANKEN ARQM