COMD7_HUMAN
ID COMD7_HUMAN Reviewed; 200 AA.
AC Q86VX2; A2BHJ2; B3KTZ2; Q5JYB0; Q96SI7; Q9BW53;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=COMM domain-containing protein 7;
GN Name=COMMD7; Synonyms=C20orf92;
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP 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] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-110 (ISOFORM 2).
RC TISSUE=Brain, and Eye;
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH CUL7, AND SUBCELLULAR 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 [8]
RP 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 [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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). Associates with the NF-kappa-B
CC complex and suppresses its transcriptional activity (PubMed:15799966).
CC {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.
CC -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain).
CC Interacts with RELA. Interacts with CCDC22, CCDC93, SCNN1B, CUL7.
CC {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:23563313,
CC ECO:0000269|PubMed:23637203, ECO:0000269|PubMed:25355947}.
CC -!- INTERACTION:
CC Q86VX2; O60826: CCDC22; NbExp=3; IntAct=EBI-1550280, EBI-3943153;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21778237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86VX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VX2-2; Sequence=VSP_038372;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in lung.
CC {ECO:0000269|PubMed:15799966}.
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DR EMBL; AY542162; AAS22244.1; -; mRNA.
DR EMBL; AK027893; BAB55436.1; -; mRNA.
DR EMBL; AK096307; BAG53254.1; -; mRNA.
DR EMBL; AL035071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76360.1; -; Genomic_DNA.
DR EMBL; BC000628; AAH00628.3; -; mRNA.
DR EMBL; BC047440; AAH47440.1; -; mRNA.
DR EMBL; BI821799; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS42864.1; -. [Q86VX2-1]
DR CCDS; CCDS46587.1; -. [Q86VX2-2]
DR RefSeq; NP_001092809.1; NM_001099339.1. [Q86VX2-2]
DR RefSeq; NP_444269.2; NM_053041.2. [Q86VX2-1]
DR AlphaFoldDB; Q86VX2; -.
DR SMR; Q86VX2; -.
DR BioGRID; 127250; 26.
DR CORUM; Q86VX2; -.
DR IntAct; Q86VX2; 16.
DR MINT; Q86VX2; -.
DR STRING; 9606.ENSP00000278980; -.
DR iPTMnet; Q86VX2; -.
DR PhosphoSitePlus; Q86VX2; -.
DR BioMuta; COMMD7; -.
DR DMDM; 108935829; -.
DR EPD; Q86VX2; -.
DR jPOST; Q86VX2; -.
DR MassIVE; Q86VX2; -.
DR MaxQB; Q86VX2; -.
DR PaxDb; Q86VX2; -.
DR PeptideAtlas; Q86VX2; -.
DR PRIDE; Q86VX2; -.
DR ProteomicsDB; 70084; -. [Q86VX2-1]
DR ProteomicsDB; 70085; -. [Q86VX2-2]
DR TopDownProteomics; Q86VX2-1; -. [Q86VX2-1]
DR TopDownProteomics; Q86VX2-2; -. [Q86VX2-2]
DR Antibodypedia; 25401; 105 antibodies from 24 providers.
DR DNASU; 149951; -.
DR Ensembl; ENST00000278980.11; ENSP00000278980.6; ENSG00000149600.12. [Q86VX2-1]
DR Ensembl; ENST00000446419.6; ENSP00000395339.1; ENSG00000149600.12. [Q86VX2-2]
DR GeneID; 149951; -.
DR KEGG; hsa:149951; -.
DR MANE-Select; ENST00000278980.11; ENSP00000278980.6; NM_053041.3; NP_444269.2.
DR UCSC; uc002wya.5; human. [Q86VX2-1]
DR CTD; 149951; -.
DR DisGeNET; 149951; -.
DR GeneCards; COMMD7; -.
DR HGNC; HGNC:16223; COMMD7.
DR HPA; ENSG00000149600; Low tissue specificity.
DR MIM; 616703; gene.
DR neXtProt; NX_Q86VX2; -.
DR OpenTargets; ENSG00000149600; -.
DR PharmGKB; PA25799; -.
DR VEuPathDB; HostDB:ENSG00000149600; -.
DR eggNOG; ENOG502QQ17; Eukaryota.
DR GeneTree; ENSGT00390000012419; -.
DR HOGENOM; CLU_118172_0_0_1; -.
DR InParanoid; Q86VX2; -.
DR OMA; SQMENVY; -.
DR OrthoDB; 1553822at2759; -.
DR PhylomeDB; Q86VX2; -.
DR TreeFam; TF329046; -.
DR PathwayCommons; Q86VX2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q86VX2; -.
DR BioGRID-ORCS; 149951; 19 hits in 1077 CRISPR screens.
DR ChiTaRS; COMMD7; human.
DR GenomeRNAi; 149951; -.
DR Pharos; Q86VX2; Tbio.
DR PRO; PR:Q86VX2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q86VX2; protein.
DR Bgee; ENSG00000149600; Expressed in kidney epithelium and 185 other tissues.
DR ExpressionAtlas; Q86VX2; baseline and differential.
DR Genevisible; Q86VX2; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR CDD; cd04755; Commd7; 1.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR037358; COMMD7.
DR Pfam; PF07258; COMM_domain; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..200
FT /note="COMM domain-containing protein 7"
FT /id="PRO_0000077399"
FT DOMAIN 133..200
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT VAR_SEQ 29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038372"
FT CONFLICT 44
FT /note="P -> Q (in Ref. 1; AAS22244 and 5; AAH47440)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> T (in Ref. 1; AAS22244 and 5; AAH47440)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> K (in Ref. 1; AAS22244 and 5; AAH47440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22540 MW; 41D483117729B495 CRC64;
MGRLHCTEDP VPEAVGGDMQ QLNQLGAQQF SALTEVLFHF LTEPKEVERF LAQLSEFATT
NQISLGSLRS IVKSLLLVPN GALKKSLTAK QVQADFITLG LSEEKATYFS EKWKQNAPTL
ARWAIGQTLM INQLIDMEWK FGVTSGSSEL EKVGSIFLQL KLVVKKGNQT ENVYIELTLP
QFYSFLHEME RVRTSMECFC
