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E3 ubiquitin-protein ligase MYLIP-A (EC 2.3.2.27) (Myosin regulatory light chain-interacting protein A) (MIR-A) (RING-type E3 ubiquitin transferase MYLIP-A)

 MYLIA_DANRE             Reviewed;         472 AA.
Q6TEM9; Q1LUH7; Q6P0B8; Q6T628; Q7ZVI9;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 2.
30-AUG-2017, entry version 108.
RecName: Full=E3 ubiquitin-protein ligase MYLIP-A;
EC=2.3.2.27;
AltName: Full=Myosin regulatory light chain-interacting protein A;
Short=MIR-A;
AltName: Full=RING-type E3 ubiquitin transferase MYLIP-A {ECO:0000305};
Name=mylipa; Synonyms=mir, mylip; ORFNames=si:ch211-266j17.1;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ANXA5,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=14651927; DOI=10.1016/j.ydbio.2003.09.001;
Knowlton M.N., Chan B.M.C., Kelly G.M.;
"The zebrafish band 4.1 member Mir is involved in cell movements
associated with gastrulation.";
Dev. Biol. 264:407-429(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney marrow;
PubMed=15520368; DOI=10.1073/pnas.0407241101;
Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y.,
Sheng Y., Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I.,
Kanki J.P., Liu T.X., Look A.T., Chen Z.;
"Hematopoietic gene expression profile in zebrafish kidney marrow.";
Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=18248225; DOI=10.1089/zeb.2004.1.133;
Knowlton M.N., Kelly G.M.;
"Zebrafish Mir antagonizes Frizzled 7-induced gastrulation defects.";
Zebrafish 1:133-144(2004).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
and subsequent proteasomal degradation of myosin regulatory light
chain (MRLC) (By similarity). Regulates cell movements during
gastrulation by acting downstream of fz7 to antagonize the
frizzled-signaling pathway. {ECO:0000250,
ECO:0000269|PubMed:14651927, ECO:0000269|PubMed:18248225}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with anxa5. {ECO:0000269|PubMed:14651927}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:14651927}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14651927}.
-!- DEVELOPMENTAL STAGE: Expression starts early during embryogenesis
and is maintained through late embryogenesis and in the adult.
{ECO:0000269|PubMed:14651927}.
-----------------------------------------------------------------------
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EMBL; AY434450; AAQ98868.1; -; mRNA.
EMBL; AY423020; AAQ97996.1; -; mRNA.
EMBL; BX936330; CAK04866.1; -; Genomic_DNA.
EMBL; BC065679; AAH65679.1; -; mRNA.
RefSeq; NP_956277.1; NM_199983.1.
UniGene; Dr.75665; -.
ProteinModelPortal; Q6TEM9; -.
SMR; Q6TEM9; -.
STRING; 7955.ENSDARP00000012386; -.
PaxDb; Q6TEM9; -.
DNASU; 335888; -.
Ensembl; ENSDART00000013497; ENSDARP00000012386; ENSDARG00000008859.
GeneID; 335888; -.
KEGG; dre:335888; -.
CTD; 335888; -.
ZFIN; ZDB-GENE-030131-7831; mylipa.
eggNOG; ENOG410IG7I; Eukaryota.
eggNOG; ENOG410XRZN; LUCA.
GeneTree; ENSGT00890000139341; -.
HOGENOM; HOG000007353; -.
HOVERGEN; HBG052549; -.
InParanoid; Q6TEM9; -.
KO; K10637; -.
OMA; NCRVKIT; -.
OrthoDB; EOG091G0A4V; -.
PhylomeDB; Q6TEM9; -.
TreeFam; TF351936; -.
Reactome; R-DRE-8866427; VLDLR internalisation and degradation.
Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q6TEM9; -.
Proteomes; UP000000437; Chromosome 19.
Bgee; ENSDARG00000008859; -.
GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR001841; Znf_RING.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
PRINTS; PR00935; BAND41.
SMART; SM00295; B41; 1.
SMART; SM01196; FERM_C; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Developmental protein; Gastrulation;
Metal-binding; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 472 E3 ubiquitin-protein ligase MYLIP-A.
/FTId=PRO_0000055974.
DOMAIN 1 279 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
ZN_FING 384 419 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
CONFLICT 12 12 V -> L (in Ref. 4; AAH65679).
{ECO:0000305}.
CONFLICT 120 120 S -> N (in Ref. 1; AAQ98868).
{ECO:0000305}.
CONFLICT 326 326 A -> P (in Ref. 1; AAQ98868).
{ECO:0000305}.
CONFLICT 340 340 S -> A (in Ref. 2; AAQ97996 and 4;
AAH65679). {ECO:0000305}.
CONFLICT 443 443 E -> D (in Ref. 4; AAH65679).
{ECO:0000305}.
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


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