MYLIA_DANRE
ID MYLIA_DANRE Reviewed; 472 AA.
AC Q6TEM9; Q1LUH7; Q6P0B8; Q6T628; Q7ZVI9;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=E3 ubiquitin-protein ligase MYLIP-A;
DE EC=2.3.2.27;
DE AltName: Full=Myosin regulatory light chain-interacting protein A;
DE Short=MIR-A;
DE AltName: Full=RING-type E3 ubiquitin transferase MYLIP-A {ECO:0000305};
GN Name=mylipa; Synonyms=mir, mylip; ORFNames=si:ch211-266j17.1;
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 [MRNA], FUNCTION, INTERACTION WITH ANXA5, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14651927; DOI=10.1016/j.ydbio.2003.09.001;
RA Knowlton M.N., Chan B.M.C., Kelly G.M.;
RT "The zebrafish band 4.1 member Mir is involved in cell movements associated
RT with gastrulation.";
RL Dev. Biol. 264:407-429(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=18248225; DOI=10.1089/zeb.2004.1.133;
RA Knowlton M.N., Kelly G.M.;
RT "Zebrafish Mir antagonizes Frizzled 7-induced gastrulation defects.";
RL Zebrafish 1:133-144(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of myosin regulatory light chain
CC (MRLC) (By similarity). Regulates cell movements during gastrulation by
CC acting downstream of fz7 to antagonize the frizzled-signaling pathway.
CC {ECO:0000250, ECO:0000269|PubMed:14651927,
CC ECO:0000269|PubMed:18248225}.
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 -!- SUBUNIT: Interacts with anxa5. {ECO:0000269|PubMed:14651927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14651927}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14651927}.
CC -!- DEVELOPMENTAL STAGE: Expression starts early during embryogenesis and
CC is maintained through late embryogenesis and in the adult.
CC {ECO:0000269|PubMed:14651927}.
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DR EMBL; AY434450; AAQ98868.1; -; mRNA.
DR EMBL; AY423020; AAQ97996.1; -; mRNA.
DR EMBL; BX936330; CAK04866.1; -; Genomic_DNA.
DR EMBL; BC065679; AAH65679.1; -; mRNA.
DR RefSeq; NP_956277.1; NM_199983.1.
DR AlphaFoldDB; Q6TEM9; -.
DR SMR; Q6TEM9; -.
DR STRING; 7955.ENSDARP00000012386; -.
DR PaxDb; Q6TEM9; -.
DR DNASU; 335888; -.
DR Ensembl; ENSDART00000013497; ENSDARP00000012386; ENSDARG00000008859.
DR GeneID; 335888; -.
DR KEGG; dre:335888; -.
DR CTD; 335888; -.
DR ZFIN; ZDB-GENE-030131-7831; mylipa.
DR eggNOG; ENOG502QV76; Eukaryota.
DR GeneTree; ENSGT00940000156206; -.
DR HOGENOM; CLU_031820_1_0_1; -.
DR InParanoid; Q6TEM9; -.
DR OMA; CRALNII; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q6TEM9; -.
DR TreeFam; TF351936; -.
DR Reactome; R-DRE-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6TEM9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000008859; Expressed in cleaving embryo and 30 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
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; IMP:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI: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 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Gastrulation; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..472
FT /note="E3 ubiquitin-protein ligase MYLIP-A"
FT /id="PRO_0000055974"
FT DOMAIN 1..279
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT ZN_FING 384..419
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 12
FT /note="V -> L (in Ref. 4; AAH65679)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> N (in Ref. 1; AAQ98868)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> P (in Ref. 1; AAQ98868)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> A (in Ref. 2; AAQ97996 and 4; AAH65679)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="E -> D (in Ref. 4; AAH65679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 53434 MW; AD7A5A1E7FC607AD CRC64;
MLCHVTRPDA VVMEIEVDAK ANGEDCLNKV CRKLGIIEVD YFGLQFSGSK GENLWLNLRN
RISQQMDNLT PCRLRLRVKF FVEPHLILQE QTRHLFFMHV KEDLHRGHLR MCSEQAQELS
ALLAQAEFGD YNQNTAKYWY TELCGSEPNQ TTINSIIAKH KALEGLSQAS VEYQALQLVS
SLEHYGVEWH WARDAEAQRL AIGVGPEGIA ICRDDFSLVN RISYPIIQIA TQSGKSVYLT
VTKESSDSVV LLFKLISNRA ASGLYRAITE THAFYRCDTV TNAVMMQYSR DFKGHLASLF
LNENINLGKK YVFDIRRTSK EVYDYARRAL YNAGIVDMMS RPGERTPSNR SPSREQEGAL
DCGGCQQSRL LQEKLQKLRE ALLCMLCCEE EIDAAFCPCG HMVCCQNCAA QLQSCPVCRS
EVEHVQHVYL PTCTSLLNLT IGENSPEPIH RGMAAHTCTT NDYSTSEKIY QN
