MARH3_RAT
ID MARH3_RAT Reviewed; 253 AA.
AC Q5XIE5; Q33E96;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF3;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 3;
DE AltName: Full=Membrane-associated RING-CH protein III;
DE Short=MARCH-III;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF3 {ECO:0000305};
GN Name=Marchf3; Synonyms=March3;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH MARCHF2 AND STX6.
RC TISSUE=Kidney;
RX PubMed=16428329; DOI=10.1093/jb/mvj012;
RA Fukuda H., Nakamura N., Hirose S.;
RT "MARCH-III is a novel component of endosomes with properties similar to
RT those of MARCH-II.";
RL J. Biochem. 139:137-145(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which may be involved in
CC endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2
CC ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfer the ubiquitin to targeted substrates.
CC {ECO:0000269|PubMed:16428329}.
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 MARCHF2 and STX6.
CC {ECO:0000269|PubMed:16428329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane
CC protein. Early endosome membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in lung, colon and spleen.
CC Present in liver (at protein level). {ECO:0000269|PubMed:16428329}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity.
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DR EMBL; AB048840; BAE47142.1; -; mRNA.
DR EMBL; BC083738; AAH83738.1; -; mRNA.
DR RefSeq; NP_001007760.1; NM_001007759.1.
DR RefSeq; XP_006254811.1; XM_006254749.3.
DR RefSeq; XP_008770381.1; XM_008772159.2.
DR RefSeq; XP_017456494.1; XM_017601005.1.
DR RefSeq; XP_017456495.1; XM_017601006.1.
DR AlphaFoldDB; Q5XIE5; -.
DR SMR; Q5XIE5; -.
DR BioGRID; 265017; 2.
DR STRING; 10116.ENSRNOP00000030051; -.
DR iPTMnet; Q5XIE5; -.
DR PhosphoSitePlus; Q5XIE5; -.
DR PaxDb; Q5XIE5; -.
DR Ensembl; ENSRNOT00000081020; ENSRNOP00000071176; ENSRNOG00000023013.
DR GeneID; 364878; -.
DR KEGG; rno:364878; -.
DR UCSC; RGD:1359308; rat.
DR CTD; 115123; -.
DR RGD; 1359308; March3.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000159206; -.
DR InParanoid; Q5XIE5; -.
DR OMA; TYCELCH; -.
DR OrthoDB; 1373244at2759; -.
DR PhylomeDB; Q5XIE5; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5XIE5; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000023013; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q5XIE5; RN.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endocytosis; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..253
FT /note="E3 ubiquitin-protein ligase MARCHF3"
FT /id="PRO_0000055929"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 63..123
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD3"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD3"
SQ SEQUENCE 253 AA; 28563 MW; C11A4D05CEBC9CE4 CRC64;
MTTSRCSHLP EVLPDCTSSA APVVKTVEDC GSLVNGQPQY VMQVSAKDGQ LLSTVVRTLA
TQSPFNDRPM CRICHEGSSQ EDLLSPCECT GTLGTIHRSC LEHWLSSSNT SYCELCHFRF
AVERKPRPLV EWLRNPGPQH EKRTLFGDMV CFLFITPLAT ISGWLCLRGA VDHLHFSSRL
EAVGLIALTV ALFTIYLFWT LVSFRYHCRL YNEWRRTNQR VILLIPKSVN IPSNQQSLLG
LHSVKRNSKE TIV
