MGRN1_RAT
ID MGRN1_RAT Reviewed; 533 AA.
AC Q5XIQ4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Mediates TSG101
CC monoubiquitination at multiple sites. Plays a role in the regulation of
CC endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by
CC competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP
CC production. Does not inhibit ADRB2-signaling. Does not promote MC1R
CC ubiquitination. Acts also as a negative regulator of hedgehog signaling
CC (By similarity). {ECO:0000250, 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 -!- SUBUNIT: Interacts with MC1R and MC4R. Interacts with TSG101. Interacts
CC with mislocalized cytosolically exposed PRNP; this interaction alters
CC MGRN1 subcellular location and causes lysosomal enlargement (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5XIQ4; O81775: GDU1; Xeno; NbExp=3; IntAct=EBI-920669, EBI-6290661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Early endosome {ECO:0000250}. Note=The endosomal
CC localization is dependent on the interaction with TSG101.
CC {ECO:0000250}.
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; BC083621; AAH83621.1; -; mRNA.
DR RefSeq; NP_001013986.1; NM_001013964.1.
DR AlphaFoldDB; Q5XIQ4; -.
DR BioGRID; 257343; 5.
DR IntAct; Q5XIQ4; 8.
DR MINT; Q5XIQ4; -.
DR STRING; 10116.ENSRNOP00000004416; -.
DR iPTMnet; Q5XIQ4; -.
DR PhosphoSitePlus; Q5XIQ4; -.
DR PaxDb; Q5XIQ4; -.
DR PRIDE; Q5XIQ4; -.
DR GeneID; 302938; -.
DR KEGG; rno:302938; -.
DR UCSC; RGD:1311862; rat.
DR CTD; 23295; -.
DR RGD; 1311862; Mgrn1.
DR VEuPathDB; HostDB:ENSRNOG00000003234; -.
DR eggNOG; KOG4265; Eukaryota.
DR InParanoid; Q5XIQ4; -.
DR OrthoDB; 883624at2759; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5XIQ4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003234; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; Q5XIQ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endosome; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60291"
FT CHAIN 2..533
FT /note="E3 ubiquitin-protein ligase MGRN1"
FT /id="PRO_0000246689"
FT ZN_FING 278..317
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 421..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 385..388
FT /note="Required for TSG101-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 421..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 390
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D074"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D074"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D074"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60291"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 533 AA; 58603 MW; DC013B16F73D1D1F CRC64;
MGSILSRRIA GVEDIDIQAN SAYRYPPKSA GNYFASHFFM GGEKFDTPHP EGYLFGENMD
LNFLGSRPVQ FPYVTPAPHE PVKTLRSLVN IRKDSLRLVR YKDDTDSPTE DGEKPRVLYS
LEFTFDADAR VAITIYCQAV EEFVNGMTVY SCKNPSLQSE TVHYKRGVSQ QFSLPSFKID
FSEWKDDELN FDLDRGVFPV VIQAVVDEGD VVEVTGHAHV LLAAFEKHVD GSFSVKPLKQ
KQIVDRVSYL LQEIYGIENK NNQETKPSDD ENSDNSSECV VCLSDLRDTL ILPCRHLCLC
TSCADTLRYQ ANNCPICRLP FRALLQIRAV RKKPGALSPI SFSPVLAQSV DHDEHSNSDS
VPPGYEPISL LEALNGLRAV SPAIPSAPLY EEITYSGISD GLSQASCPLA GLDRIIENGI
QKGKTQSKSP DSTLRSPSSP IHEEDEEKLS EDPEAPLPPS GVELVLQESS SPESFGTEEV
GEPSLKQGSR VPSIDDVLQD GSPQHHGCSQ PVPPADIYLP ALGPESCSVG IEE
