ID A0A452DJW0_BOVIN Unreviewed; 312 AA.
AC A0A452DJW0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:ENSBTAP00000028017.3,
GN ECO:0000313|VGNC:VGNC:31238};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000028017.3, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000028017.3, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028017.3,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000028017.3}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028017.3};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A452DJW0; -.
DR Ensembl; ENSBTAT00000028017.3; ENSBTAP00000028017.3; ENSBTAG00000021036.3.
DR VEuPathDB; HostDB:ENSBTAG00000021036; -.
DR VGNC; VGNC:31238; MARCHF2.
DR GeneTree; ENSGT00940000158995; -.
DR OMA; ICHEGAS; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000021036; Expressed in temporal cortex and 106 other cell types or tissues.
DR ExpressionAtlas; A0A452DJW0; baseline and differential.
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:UP000009136};
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 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..183
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 131..177
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 312 AA; 34123 MW; 707219C1F3B39BB2 CRC64;
MAQSSRPEPG PLKDGQARTV GLSLPSKETH KPCWLVLGWK RSLPRVPADR LLGPWALGPE
DTGRPVAMTT GDCCHLPGSL CDCSDSPAFS KVVEATGLGP PQYVAQVTSR DGRLLSTVIR
ALETPSDGPF CRICHEGANG ESLLSPCGCS GTLGAVHKSC LERWLSSSNT SYCELCHTEF
AVEKRSRSLT EWLKDPGPRT EKRTLCCDVV CFLFITPLAA ISGWLCLRGA QDHLRLHSHL
EALGLIALTI ALFTIYVLWT LVSFRYHCQL YSEWRRTNQK VRLKMQADGS EGSQHSPLAA
GLLKKVAEET PV
//
