ID MARH4_MOUSE Reviewed; 409 AA.
AC Q80TE3; Q4QQN4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF4;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 4;
DE AltName: Full=Membrane-associated RING-CH protein IV;
DE Short=MARCH-IV;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF4 {ECO:0000305};
DE Flags: Precursor;
GN Name=Marchf4; Synonyms=Kiaa1399, March4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 that may mediate ubiquitination
CC of MHC-I and CD4, and promote their subsequent endocytosis and sorting
CC to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept
CC ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC thioester and then directly transfer the ubiquitin to targeted
CC substrates. {ECO:0000250|UniProtKB:Q9P2E8}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; AK122502; BAC65784.1; -; mRNA.
DR EMBL; BC098191; AAH98191.1; -; mRNA.
DR CCDS; CCDS15034.1; -.
DR RefSeq; NP_001038998.1; NM_001045533.1.
DR AlphaFoldDB; Q80TE3; -.
DR STRING; 10090.ENSMUSP00000042803; -.
DR iPTMnet; Q80TE3; -.
DR PhosphoSitePlus; Q80TE3; -.
DR PaxDb; 10090-ENSMUSP00000042803; -.
DR Antibodypedia; 3020; 207 antibodies from 27 providers.
DR Ensembl; ENSMUST00000047786.6; ENSMUSP00000042803.6; ENSMUSG00000039372.6.
DR GeneID; 381270; -.
DR KEGG; mmu:381270; -.
DR UCSC; uc007bkn.1; mouse.
DR AGR; MGI:2683550; -.
DR MGI; MGI:2683550; Marchf4.
DR VEuPathDB; HostDB:ENSMUSG00000039372; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000158179; -.
DR HOGENOM; CLU_045217_0_1_1; -.
DR InParanoid; Q80TE3; -.
DR OMA; CCGLCTP; -.
DR OrthoDB; 1342875at2759; -.
DR PhylomeDB; Q80TE3; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 381270; 1 hit in 48 CRISPR screens.
DR ChiTaRS; March4; mouse.
DR PRO; PR:Q80TE3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80TE3; Protein.
DR Bgee; ENSMUSG00000039372; Expressed in embryonic brain and 46 other cell types or tissues.
DR Genevisible; Q80TE3; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16824; RING_CH-C4HC3_MARCH4; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046356; MARCHF4/9/11.
DR InterPro; IPR047905; MARCHF4_RING_CH-C4HC3.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR PANTHER; PTHR46053:SF3; E3 UBIQUITIN-PROTEIN LIGASE MARCHF4; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..409
FT /note="E3 ubiquitin-protein ligase MARCHF4"
FT /id="PRO_0000055931"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 154..214
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 92..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT CONFLICT 237..241
FT /note="IAAAI -> CSRH (in Ref. 1; AAH98191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 45201 MW; 2A99BA71434A81E0 CRC64;
MLMPLGGLLW WWCCCCGWYS CGLCTPAPQM LRHQGLLKCR CRMLFNDLKV FLLRRPPPAP
LPMHGDPQLP GVAANNNTLP ALGAGGWAGW RGPREAVGRE TPPLPPPPPL PPSGDDDWDG
PATGPPASLL SSASSDEFCK EKTEDCYSLG SSLDSGMRTP LCRICFQGPE QGELLSPCRC
DGSVKCTHQP CLIKWISERG CWSCELCYYK YHVIAISTKN PLQWQAISLT VIEKVQIAAA
ILGSLFLIAS ISWLIWSTFS PSAKWQRQDL LFQICYGMYG FMDVVCIGLI IHEGPSVYRI
FKRWQAVNQQ WKVLNYDKTK DLEDQKSGGR TNLQTSSSAQ ANLPSAEEEA ASPPAREEGP
TRAASHPSGP VSQHHCAYTI LHILSHLRPH DQRSTQGSGR ELVMRVTTV
//
