ID M3YU56_MUSPF Unreviewed; 553 AA.
AC M3YU56;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
GN Name=MGRN1 {ECO:0000313|Ensembl:ENSMPUP00000014866.1,
GN ECO:0000313|RefSeq:XP_004750513.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000014866.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000014866.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004750513.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004750513.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU369081};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR EMBL; AEYP01027722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01027727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004750513.1; XM_004750456.3.
DR STRING; 9669.ENSMPUP00000014866; -.
DR Ensembl; ENSMPUT00000015102.1; ENSMPUP00000014866.1; ENSMPUG00000014976.1.
DR GeneID; 101686632; -.
DR CTD; 23295; -.
DR eggNOG; KOG4265; Eukaryota.
DR GeneTree; ENSGT00390000009925; -.
DR HOGENOM; CLU_016631_1_1_1; -.
DR OMA; CAQSGPP; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996:SF2; E3 UBIQUITIN-PROTEIN LIGASE MGRN1; 1.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369081};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transferase {ECO:0000256|RuleBase:RU369081};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369081};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 278..317
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 355..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60634 MW; 4541AFF74A3030E8 CRC64;
MGSILSRRIA GVEDIDIQAN SAYRYPPKSG NYFASHFFMG GEKFDTPHPE GYLFGENMDL
NFLGNRPVQF PYVTPAPHEP VKTLRSLVNI RKDSLRLVRY KDGADSPSED SEKPRVLYSL
EFTFDADARV AITIYCQAVE EFLNGMAVYS PKSPALQSET AHYKRGVSQQ FSLPSFKIDF
SEWKDDELNF DLDRGVFPVV IQAVVDEGDV VEVTGHAHVL LAAFEKHVDG SFSVKPLKQK
QIVDRVSYLL QEIYGIENKN NQETKPSDEE NSDNSNECVV CLSDLRDTLI LPCRHLCLCN
SCADTLRYQA SNCPICRLPF RALLQIRAVR KKPGALSPVS FSPVLAQSMD HDEHSCPFKK
SKAHPASLAS KKPKRETSSD SIPPGYEPIS LLEALNGLRA ISPAIPSAPL YEEITYSGVS
DGLSQASCPL AGMDRILESS HQKGKPRSKS PDSTLRSPSS PIHEEDEEKL SQDSDAPPPL
SGAGLALSSS PESFVTEEAD EAAALKQGSR VPSFENVLQD GSPEACSHGQ PRLPADVYLP
ALGPDSCSVG IEE
//
