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E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain-interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP)

 MYLIP_MOUSE             Reviewed;         445 AA.
Q8BM54; Q3TX01; Q8BLY9; Q91Z47;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
05-DEC-2018, entry version 145.
RecName: Full=E3 ubiquitin-protein ligase MYLIP;
EC=2.3.2.27;
AltName: Full=Inducible degrader of the LDL-receptor;
Short=Idol;
AltName: Full=Myosin regulatory light chain-interacting protein;
Short=MIR;
AltName: Full=RING-type E3 ubiquitin transferase MYLIP {ECO:0000305};
Name=Mylip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Aorta, Embryo, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-387, AND
UBIQUITINATION.
PubMed=19520913; DOI=10.1126/science.1168974;
Zelcer N., Hong C., Boyadjian R., Tontonoz P.;
"LXR regulates cholesterol uptake through Idol-dependent
ubiquitination of the LDL receptor.";
Science 325:100-104(2009).
[5]
FUNCTION.
PubMed=20427281; DOI=10.1074/jbc.M110.123729;
Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D.,
Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.;
"The E3 ubiquitin ligase IDOL induces the degradation of the low
density lipoprotein receptor family members VLDLR and ApoER2.";
J. Biol. Chem. 285:19720-19726(2010).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
and subsequent proteasomal degradation of myosin regulatory light
chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes
of the UBE2D family. Proteasomal degradation of MRLC leads to
inhibit neurite outgrowth in presence of NGF by counteracting the
stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and
reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-
dependent inhibitor of cellular cholesterol uptake by mediating
ubiquitination and subsequent degradation of LDLR.
{ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281}.
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=2.3.2.27;
-!- ACTIVITY REGULATION: Can bind 1 iron ion per dimer. Iron binding
seems to decrease LDLR degradation activity.
{ECO:0000250|UniProtKB:Q8WY64}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with the E2 ubiquitin-conjugating
enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin
regulatory light chain (MRLC) and TMEM4.
{ECO:0000250|UniProtKB:Q8WY64}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane
{ECO:0000250|UniProtKB:Q8WY64}; Peripheral membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BM54-1; Sequence=Displayed;
Name=2;
IsoId=Q8BM54-2; Sequence=VSP_011830;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in liver, spleen, intestine and
adrenals. {ECO:0000269|PubMed:19520913}.
-!- DOMAIN: The RING domain mediates ubiquitination and the neurite
outgrowth inhibitory activity. {ECO:0000250}.
-!- DOMAIN: The FERM domain binds phospholipids and mediates
lipoprotein receptors recognition at the plasma membrane through
their cytoplasmic tails. {ECO:0000250}.
-!- DOMAIN: The RING-type zinc finger mediates the interaction with
UBE2D E2 enzymes. {ECO:0000250}.
-!- PTM: Autoubiquitinated. {ECO:0000305|PubMed:19520913}.
-----------------------------------------------------------------------
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EMBL; AY434449; AAQ98867.1; -; mRNA.
EMBL; AK034887; BAC28868.1; -; mRNA.
EMBL; AK040836; BAC30716.1; -; mRNA.
EMBL; AK159478; BAE35115.1; -; mRNA.
EMBL; BC010206; AAH10206.1; -; mRNA.
CCDS; CCDS36648.1; -. [Q8BM54-1]
RefSeq; NP_722484.2; NM_153789.3. [Q8BM54-1]
UniGene; Mm.212855; -.
UniGene; Mm.489954; -.
ProteinModelPortal; Q8BM54; -.
SMR; Q8BM54; -.
IntAct; Q8BM54; 1.
MINT; Q8BM54; -.
STRING; 10090.ENSMUSP00000047403; -.
PhosphoSitePlus; Q8BM54; -.
PaxDb; Q8BM54; -.
PRIDE; Q8BM54; -.
Ensembl; ENSMUST00000038275; ENSMUSP00000047403; ENSMUSG00000038175. [Q8BM54-1]
Ensembl; ENSMUST00000222178; ENSMUSP00000152597; ENSMUSG00000038175. [Q8BM54-2]
GeneID; 218203; -.
KEGG; mmu:218203; -.
UCSC; uc007qgz.1; mouse. [Q8BM54-1]
CTD; 29116; -.
MGI; MGI:2388271; Mylip.
eggNOG; ENOG410IG7I; Eukaryota.
eggNOG; ENOG410XRZN; LUCA.
GeneTree; ENSGT00940000156206; -.
HOGENOM; HOG000007353; -.
HOVERGEN; HBG052549; -.
InParanoid; Q8BM54; -.
KO; K10637; -.
OMA; LNIICEM; -.
OrthoDB; EOG091G0A4V; -.
PhylomeDB; Q8BM54; -.
TreeFam; TF351936; -.
Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Mylip; mouse.
PRO; PR:Q8BM54; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000038175; Expressed in 295 organ(s), highest expression level in lymph node.
CleanEx; MM_MYLIP; -.
Genevisible; Q8BM54; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IC:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0007399; P:nervous system development; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
GO; GO:0031648; P:protein destabilization; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0032803; P:regulation of low-density lipoprotein particle receptor catabolic process; IMP:BHF-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR000798; Ez/rad/moesin-like.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF09380; FERM_C; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
PRINTS; PR00935; BAND41.
PRINTS; PR00661; ERMFAMILY.
SMART; SM00295; B41; 1.
SMART; SM01196; FERM_C; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Iron; Membrane; Metal-binding; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 445 E3 ubiquitin-protein ligase MYLIP.
/FTId=PRO_0000055973.
DOMAIN 1 279 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
ZN_FING 387 422 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 431 433 Critical for homodimerization.
{ECO:0000250}.
METAL 360 360 Iron. {ECO:0000250}.
METAL 363 363 Iron. {ECO:0000250}.
METAL 368 368 Iron. {ECO:0000250}.
VAR_SEQ 1 65 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011830.
MUTAGEN 387 387 C->A: Loss of ubiquitin ligase activity.
{ECO:0000269|PubMed:19520913}.
CONFLICT 113 113 P -> A (in Ref. 3; AAH10206).
{ECO:0000305}.
SEQUENCE 445 AA; 49849 MW; 31C73572C95D0711 CRC64;
MLCYVTRPDA VLMEVEVEAK ANGEDCLNQV CRRLGIIEVD YFGLQFTGSK GESLWLNLRN
RISQQMDGLA PYRLKLRVKF FVEPHLILQE QTRHIFFLHI KESLLAGHLQ CSPEQAVELS
ALLAQTKFGD YNQNTAQYSY EDLCEKELSS STLNSIVAKH KELEGISQAS AEYQVLQIVS
AMENYGIEWH AVRDSEGQKL LIGVGPEGIS ICKEDFSPIN RIAYPVVQMA TQSGKNVYLT
VTKESGNSIV LLFKMISTRA ASGLYRAITE THAFYRCDTV TSAVMMQYSR DLKGHLASLF
LNENINLGKK YVFDIKRTSK EVYDHARRAL YNAGVVDLVS RSDQSPPSSP LKSSDSSMSC
SSCEGLSCQQ TRVLQEKLRK LKEAMLCMAC CEEEINSTFC PCGHTVCCES CAAQLQSCPV
CRSRVEHVQH VYLPTHTSLL NLTVI


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