MARH3_HUMAN
ID MARH3_HUMAN Reviewed; 253 AA.
AC Q86UD3; A8K264; B9EJE7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 finger protein 173;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF3 {ECO:0000305};
GN Name=MARCHF3 {ECO:0000312|HGNC:HGNC:28728}; Synonyms=MARCH3, RNF173;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-68.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC 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).
RN [5]
RP SUBCELLULAR LOCATION.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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:0000250|UniProtKB:Q5XIE5}.
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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q86UD3; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-2341065, EBI-4290634;
CC Q86UD3; Q969F0: FATE1; NbExp=3; IntAct=EBI-2341065, EBI-743099;
CC Q86UD3; P61086: UBE2K; NbExp=3; IntAct=EBI-2341065, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16428329}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16428329}. Early endosome membrane
CC {ECO:0000269|PubMed:16428329}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16428329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UD3-2; Sequence=VSP_055451, VSP_055452;
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; AK290129; BAF82818.1; -; mRNA.
DR EMBL; AC004507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62412.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62413.1; -; Genomic_DNA.
DR EMBL; BC047569; AAH47569.1; -; mRNA.
DR EMBL; BC146948; AAI46949.1; -; mRNA.
DR EMBL; BC146964; AAI46965.1; -; mRNA.
DR CCDS; CCDS4141.1; -. [Q86UD3-1]
DR RefSeq; NP_848545.1; NM_178450.4. [Q86UD3-1]
DR AlphaFoldDB; Q86UD3; -.
DR SMR; Q86UD3; -.
DR BioGRID; 125416; 41.
DR IntAct; Q86UD3; 11.
DR MINT; Q86UD3; -.
DR STRING; 9606.ENSP00000309141; -.
DR TCDB; 8.A.159.1.9; the march ubiquitin ligase (march) family.
DR iPTMnet; Q86UD3; -.
DR PhosphoSitePlus; Q86UD3; -.
DR BioMuta; MARCH3; -.
DR DMDM; 59798460; -.
DR MassIVE; Q86UD3; -.
DR PaxDb; Q86UD3; -.
DR PeptideAtlas; Q86UD3; -.
DR PRIDE; Q86UD3; -.
DR ProteomicsDB; 69801; -. [Q86UD3-1]
DR ProteomicsDB; 7532; -.
DR Antibodypedia; 25757; 171 antibodies from 27 providers.
DR DNASU; 115123; -.
DR Ensembl; ENST00000308660.6; ENSP00000309141.5; ENSG00000173926.6. [Q86UD3-1]
DR Ensembl; ENST00000515241.1; ENSP00000421979.1; ENSG00000173926.6. [Q86UD3-2]
DR GeneID; 115123; -.
DR KEGG; hsa:115123; -.
DR MANE-Select; ENST00000308660.6; ENSP00000309141.5; NM_178450.5; NP_848545.1.
DR UCSC; uc003kuf.4; human. [Q86UD3-1]
DR CTD; 115123; -.
DR DisGeNET; 115123; -.
DR GeneCards; MARCHF3; -.
DR HGNC; HGNC:28728; MARCHF3.
DR HPA; ENSG00000173926; Low tissue specificity.
DR MIM; 613333; gene.
DR neXtProt; NX_Q86UD3; -.
DR OpenTargets; ENSG00000173926; -.
DR VEuPathDB; HostDB:ENSG00000173926; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000159206; -.
DR HOGENOM; CLU_096532_0_0_1; -.
DR InParanoid; Q86UD3; -.
DR OMA; TYCELCH; -.
DR OrthoDB; 1373244at2759; -.
DR PhylomeDB; Q86UD3; -.
DR TreeFam; TF319557; -.
DR PathwayCommons; Q86UD3; -.
DR SignaLink; Q86UD3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 115123; 29 hits in 1049 CRISPR screens.
DR ChiTaRS; MARCH3; human.
DR GenomeRNAi; 115123; -.
DR Pharos; Q86UD3; Tbio.
DR PRO; PR:Q86UD3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86UD3; protein.
DR Bgee; ENSG00000173926; Expressed in pancreatic ductal cell and 145 other tissues.
DR Genevisible; Q86UD3; HS.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IDA: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 Alternative splicing; Cytoplasmic vesicle; Endocytosis; Endosome; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..253
FT /note="E3 ubiquitin-protein ligase MARCHF3"
FT /id="PRO_0000055927"
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:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 132..138
FT /note="WLRNPGP -> VSKWGTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055451"
FT VAR_SEQ 139..253
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055452"
FT VARIANT 68
FT /note="R -> Q (in dbSNP:rs34821177)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_053639"
SQ SEQUENCE 253 AA; 28504 MW; 6E090675CEBC8A88 CRC64;
MTTSRCSHLP EVLPDCTSSA APVVKTVEDC GSLVNGQPQY VMQVSAKDGQ LLSTVVRTLA
TQSPFNDRPM CRICHEGSSQ EDLLSPCECT GTLGTIHRSC LEHWLSSSNT SYCELCHFRF
AVERKPRPLV EWLRNPGPQH EKRTLFGDMV CFLFITPLAT ISGWLCLRGA VDHLHFSSRL
EAVGLIALTV ALFTIYLFWT LVSFRYHCRL YNEWRRTNQR VILLIPKSVN VPSNQPSLLG
LHSVKRNSKE TVV
