ID A0A2K6FWH5_PROCO Unreviewed; 572 AA.
AC A0A2K6FWH5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF8 {ECO:0000256|ARBA:ARBA00040153};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Membrane-associated RING finger protein 8 {ECO:0000256|ARBA:ARBA00043184};
DE AltName: Full=Membrane-associated RING-CH protein VIII {ECO:0000256|ARBA:ARBA00041425};
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF8 {ECO:0000256|ARBA:ARBA00043233};
GN Name=MARCHF8 {ECO:0000313|Ensembl:ENSPCOP00000018341.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000018341.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000018341.1}
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: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004439}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004520}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004337}. 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_012513863.1; XM_012658409.1.
DR RefSeq; XP_012513864.1; XM_012658410.1.
DR AlphaFoldDB; A0A2K6FWH5; -.
DR STRING; 379532.ENSPCOP00000018341; -.
DR Ensembl; ENSPCOT00000028982.1; ENSPCOP00000018341.1; ENSPCOG00000021062.1.
DR GeneID; 105821654; -.
DR KEGG; pcoq:105821654; -.
DR CTD; 220972; -.
DR GeneTree; ENSGT00940000158282; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR CDD; cd16807; RING_CH-C4HC3_MARCH8; 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; PTHR45981:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF8; 1.
DR PANTHER; PTHR45981; LD02310P; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 437..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..415
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 362..409
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63056 MW; 033B2892852EFD19 CRC64;
MNMPLHQISA IPSQDATSAR VYRSKTKEKE REEQHEKTLG HSMSHSSDIS KAGSPPSASA
PAPVSAFSRT SVTPSAQDIC SSSAVFSECC HHSPVQSAVV LKTPQCQSSL TQGLTVTVIC
KDTVQASKRN SFGSEWVQGF KPGKNTKARR TLKFSKSLND VGEKAQDTLE SFDYVERTCS
EGKLILPQDP RLRINRFHHQ EKRMLIRRPL GSSKHSCVSS LSASCSAASE VGAGKGGAHI
PLSDEKGDGE AVSRSRRLLR YLLSLSRGSS TSSLHRFHEL ESCAAHLRAA KSSSGPAGST
GFCSDEMGDD DVFEDSTSTK PKSRVLRAPL CSTEKDSDLD SSSPLSEKCP PMSPVSTSGD
ACRICHCEGD DESPLITPCR CTGSLHFVHR TCLQQWIKSS DTRCCELCKY EFVMETKLKP
LRKWEKLQMT ANERRKIMCS VTFHVIAITC VVWSLYVLID RTAEEIKQGQ ATGILEWPFW
TKLVVVAVGF TGGLLFMYVQ CKVYVQLWKR LKAYNRVIYV QNCPETSKKN IFEKSALTEP
NFENKDGRGV SHSDTNSCCT EPEDTGADII HV
//
