ID A0A2K5Y2T5_MANLE Unreviewed; 246 AA.
AC A0A2K5Y2T5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF2 {ECO:0000256|ARBA:ARBA00040156};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Membrane-associated RING finger protein 2 {ECO:0000256|ARBA:ARBA00043183};
DE AltName: Full=Membrane-associated RING-CH protein II {ECO:0000256|ARBA:ARBA00042437};
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF2 {ECO:0000256|ARBA:ARBA00043232};
GN Name=MARCHF2 {ECO:0000313|Ensembl:ENSMLEP00000009868.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000009868.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000009868.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_011821652.1; XM_011966262.1.
DR RefSeq; XP_011821653.1; XM_011966263.1.
DR RefSeq; XP_011821654.1; XM_011966264.1.
DR AlphaFoldDB; A0A2K5Y2T5; -.
DR SMR; A0A2K5Y2T5; -.
DR STRING; 9568.ENSMLEP00000009868; -.
DR Ensembl; ENSMLET00000033271.1; ENSMLEP00000009868.1; ENSMLEG00000029114.1.
DR GeneID; 105529177; -.
DR KEGG; mleu:105529177; -.
DR CTD; 51257; -.
DR GeneTree; ENSGT00940000158995; -.
DR OMA; ICHEGAS; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR CDD; cd16808; RING_CH-C4HC3_MARCH2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46065; E3 UBIQUITIN-PROTEIN LIGASE MARCH 2/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR46065:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF2; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 142..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..116
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 64..110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 220..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 26985 MW; 38D877D55211CB44 CRC64;
MTTGDCCHLP GSLCDCSGSP AFSKVVEATG LGPPQYVAQV TSRDGRLLST VIRALDTPSD
GPFCRICHEG ANGECLLSPC GCTGTLGAVH KSCLEKWLSS SNTSYCELCH TEFAVEKRPR
PLTEWLKDPG PRTEKRTLCC DMVCFLFITP LAAISGWLCL RGAQDHLRLH SQLEAVGLIA
LTIALFTIYV LWTLVSFRYH CQLYSEWRKT NQKVRLKIRE ADSSEGPQHS PLAAGLLKKV
AEETPV
//
