COMD3_HUMAN
ID COMD3_HUMAN Reviewed; 195 AA.
AC Q9UBI1; D3DRU7; Q5T8Y9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=COMM domain-containing protein 3;
DE AltName: Full=Protein Bup;
DE AltName: Full=Protein PIL;
GN Name=COMMD3; Synonyms=BUP, C10orf8;
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 [MRNA], FUNCTION, INTERACTION WITH COMMD1 AND NFKB1,
RP AND TISSUE SPECIFICITY.
RX PubMed=15799966; DOI=10.1074/jbc.m501928200;
RA Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A.,
RA Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.;
RT "COMMD proteins, a novel family of structural and functional homologs of
RT MURR1.";
RL J. Biol. Chem. 280:22222-22232(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Li Y., Li N., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, INTERACTION WITH CUL3; CUL4A; CUL4B AND CUL5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21778237; DOI=10.1074/jbc.m111.278408;
RA Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N.,
RA Burstein E.;
RT "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates
RT Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-
RT dissociated protein 1) binding.";
RL J. Biol. Chem. 286:32355-32365(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH SCNN1B.
RX PubMed=23637203; DOI=10.1152/ajprenal.00158.2013;
RA Liu Y.F., Swart M., Ke Y., Ly K., McDonald F.J.;
RT "Functional interaction of COMMD3 and COMMD9 with the epithelial sodium
RT channel.";
RL Am. J. Physiol. 305:F80-F89(2013).
RN [10]
RP INTERACTION WITH CCDC22.
RX PubMed=23563313; DOI=10.1172/jci66466;
RA Starokadomskyy P., Gluck N., Li H., Chen B., Wallis M., Maine G.N., Mao X.,
RA Zaidi I.W., Hein M.Y., McDonald F.J., Lenzner S., Zecha A., Ropers H.H.,
RA Kuss A.W., McGaughran J., Gecz J., Burstein E.;
RT "CCDC22 deficiency in humans blunts activation of proinflammatory NF-kappaB
RT signaling.";
RL J. Clin. Invest. 123:2244-2256(2013).
RN [11]
RP INTERACTION WITH CCDC93.
RX PubMed=25355947; DOI=10.1091/mbc.e14-06-1073;
RA Phillips-Krawczak C.A., Singla A., Starokadomskyy P., Deng Z.,
RA Osborne D.G., Li H., Dick C.J., Gomez T.S., Koenecke M., Zhang J.S.,
RA Dai H., Sifuentes-Dominguez L.F., Geng L.N., Kaufmann S.H., Hein M.Y.,
RA Wallis M., McGaughran J., Gecz J., van de Sluis B., Billadeau D.D.,
RA Burstein E.;
RT "COMMD1 is linked to the WASH complex and regulates endosomal trafficking
RT of the copper transporter ATP7A.";
RL Mol. Biol. Cell 26:91-103(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase
CC (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-
CC kappa-B (PubMed:15799966). Modulates Na(+) transport in epithelial
CC cells by regulation of apical cell surface expression of amiloride-
CC sensitive sodium channel (ENaC) subunits (PubMed:23637203).
CC {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:23637203,
CC ECO:0000305|PubMed:21778237}.
CC -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain).
CC Interacts with NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL3,
CC CUL4A, CUL4B, CUL5. {ECO:0000269|PubMed:15799966,
CC ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:23563313,
CC ECO:0000269|PubMed:23637203, ECO:0000269|PubMed:25355947}.
CC -!- INTERACTION:
CC Q9UBI1; O60826: CCDC22; NbExp=7; IntAct=EBI-714979, EBI-3943153;
CC Q9UBI1; Q567U6: CCDC93; NbExp=4; IntAct=EBI-714979, EBI-1104769;
CC Q9UBI1; Q8N668: COMMD1; NbExp=6; IntAct=EBI-714979, EBI-1550112;
CC Q9UBI1; Q86X83: COMMD2; NbExp=5; IntAct=EBI-714979, EBI-1550220;
CC Q9UBI1; Q9NX08: COMMD8; NbExp=3; IntAct=EBI-714979, EBI-725694;
CC Q9UBI1; Q8WWB5: PIH1D2; NbExp=5; IntAct=EBI-714979, EBI-10232538;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus
CC {ECO:0000269|PubMed:21778237}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in thymus.
CC {ECO:0000269|PubMed:15799966}.
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DR EMBL; AY542159; AAS22241.1; -; mRNA.
DR EMBL; AF201948; AAF17240.1; -; mRNA.
DR EMBL; AF078848; AAD44480.1; -; mRNA.
DR EMBL; AL158211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86149.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86155.1; -; Genomic_DNA.
DR EMBL; BC022898; AAH22898.1; -; mRNA.
DR CCDS; CCDS7137.1; -.
DR RefSeq; NP_036203.1; NM_012071.3.
DR AlphaFoldDB; Q9UBI1; -.
DR SMR; Q9UBI1; -.
DR BioGRID; 116984; 74.
DR CORUM; Q9UBI1; -.
DR IntAct; Q9UBI1; 50.
DR MINT; Q9UBI1; -.
DR STRING; 9606.ENSP00000366032; -.
DR GlyGen; Q9UBI1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBI1; -.
DR MetOSite; Q9UBI1; -.
DR PhosphoSitePlus; Q9UBI1; -.
DR BioMuta; COMMD3; -.
DR DMDM; 51316114; -.
DR EPD; Q9UBI1; -.
DR jPOST; Q9UBI1; -.
DR MassIVE; Q9UBI1; -.
DR MaxQB; Q9UBI1; -.
DR PaxDb; Q9UBI1; -.
DR PeptideAtlas; Q9UBI1; -.
DR PRIDE; Q9UBI1; -.
DR ProteomicsDB; 83972; -.
DR TopDownProteomics; Q9UBI1; -.
DR Antibodypedia; 25612; 89 antibodies from 17 providers.
DR DNASU; 23412; -.
DR Ensembl; ENST00000376836.8; ENSP00000366032.3; ENSG00000148444.16.
DR GeneID; 23412; -.
DR KEGG; hsa:23412; -.
DR MANE-Select; ENST00000376836.8; ENSP00000366032.3; NM_012071.4; NP_036203.1.
DR UCSC; uc001irf.4; human.
DR CTD; 23412; -.
DR DisGeNET; 23412; -.
DR GeneCards; COMMD3; -.
DR HGNC; HGNC:23332; COMMD3.
DR HPA; ENSG00000148444; Low tissue specificity.
DR MIM; 616700; gene.
DR neXtProt; NX_Q9UBI1; -.
DR OpenTargets; ENSG00000148444; -.
DR PharmGKB; PA134864927; -.
DR VEuPathDB; HostDB:ENSG00000148444; -.
DR eggNOG; ENOG502R79J; Eukaryota.
DR GeneTree; ENSGT00390000015971; -.
DR InParanoid; Q9UBI1; -.
DR OMA; HIVDIDW; -.
DR PhylomeDB; Q9UBI1; -.
DR TreeFam; TF329267; -.
DR PathwayCommons; Q9UBI1; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9UBI1; -.
DR BioGRID-ORCS; 23412; 113 hits in 1038 CRISPR screens.
DR GenomeRNAi; 23412; -.
DR Pharos; Q9UBI1; Tbio.
DR PRO; PR:Q9UBI1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UBI1; protein.
DR Bgee; ENSG00000148444; Expressed in diaphragm and 201 other tissues.
DR ExpressionAtlas; Q9UBI1; baseline and differential.
DR Genevisible; Q9UBI1; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR037355; COMMD3.
DR PANTHER; PTHR31159; PTHR31159; 1.
DR Pfam; PF07258; COMM_domain; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Ion transport; Nucleus; Reference proteome; Sodium;
KW Sodium transport; Transcription; Transcription regulation; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..195
FT /note="COMM domain-containing protein 3"
FT /id="PRO_0000077389"
FT DOMAIN 124..193
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT VARIANT 18
FT /note="R -> G (in dbSNP:rs11552445)"
FT /id="VAR_061121"
SQ SEQUENCE 195 AA; 22151 MW; AC757941FC17F757 CRC64;
MELSESVQKG FQMLADPRSF DSNAFTLLLR AAFQSLLDAQ ADEAVLDHPD LKHIDPVVLK
HCHAAAATYI LEAGKHRADK STLSTYLEDC KFDRERIELF CTEYQNNKNS LEILLGSIGR
SLPHITDVSW RLEYQIKTNQ LHRMYRPAYL VTLSVQNTDS PSYPEISFSC SMEQLQDLVG
KLKDASKSLE RATQL
