COMD9_HUMAN
ID COMD9_HUMAN Reviewed; 198 AA.
AC Q9P000; E9PAN2; Q96FI2; Q9H0R0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=COMM domain-containing protein 9;
GN Name=COMMD9; ORFNames=HSPC166;
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, INTERACTION WITH RELB AND
RP NFKB1, 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] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 CUL1, 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 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [12]
RP INTERACTION WITH CCDC22.
RX PubMed=28892079; DOI=10.1038/ncb3610;
RA McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D.,
RA Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A.,
RA Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I.,
RA Billadeau D.D., Burstein E., Cullen P.J.;
RT "Retriever is a multiprotein complex for retromer-independent endosomal
RT cargo recycling.";
RL Nat. Cell Biol. 19:1214-1225(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 1-116.
RA Hospenthal M., Celligoi D., McDonald F.J., Lott J.S.;
RT "The crystal structure of the N-terminal domain of COMMD9.";
RL Submitted (NOV-2013) to the PDB data bank.
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 with RELB and NFKB1/p105 (PubMed:15799966).
CC Interacts with CCDC22, CCDC93, SCNN1B, CUL1 (PubMed:21778237,
CC PubMed:23563313, PubMed:23637203, PubMed:25355947, PubMed:28892079).
CC {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:21778237,
CC ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:23637203,
CC ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:28892079}.
CC -!- INTERACTION:
CC Q9P000; O60826: CCDC22; NbExp=8; IntAct=EBI-1550510, EBI-3943153;
CC Q9P000; Q567U6: CCDC93; NbExp=2; IntAct=EBI-1550510, EBI-1104769;
CC Q9P000; Q7Z4G1: COMMD6; NbExp=4; IntAct=EBI-1550510, EBI-1550081;
CC Q9P000; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-1550510, EBI-10303987;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21778237}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:21778237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P000-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P000-2; Sequence=VSP_041499;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.
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DR EMBL; AY542164; AAS22246.1; -; mRNA.
DR EMBL; AF161515; AAF29130.1; -; mRNA.
DR EMBL; AL136688; CAB66623.1; -; mRNA.
DR EMBL; AC087277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010892; AAH10892.1; -; mRNA.
DR CCDS; CCDS44571.1; -. [Q9P000-2]
DR CCDS; CCDS7900.1; -. [Q9P000-1]
DR RefSeq; NP_001294866.1; NM_001307937.1.
DR RefSeq; NP_054905.2; NM_014186.3. [Q9P000-1]
DR PDB; 4NKN; X-ray; 2.79 A; A/B/C/D/E/F=1-116.
DR PDB; 4OE9; X-ray; 1.55 A; A/B=1-117.
DR PDB; 6BP6; X-ray; 2.17 A; A/B=115-198.
DR PDBsum; 4NKN; -.
DR PDBsum; 4OE9; -.
DR PDBsum; 6BP6; -.
DR AlphaFoldDB; Q9P000; -.
DR SMR; Q9P000; -.
DR BioGRID; 118867; 37.
DR CORUM; Q9P000; -.
DR IntAct; Q9P000; 21.
DR STRING; 9606.ENSP00000263401; -.
DR iPTMnet; Q9P000; -.
DR PhosphoSitePlus; Q9P000; -.
DR SwissPalm; Q9P000; -.
DR BioMuta; COMMD9; -.
DR DMDM; 124056492; -.
DR EPD; Q9P000; -.
DR jPOST; Q9P000; -.
DR MassIVE; Q9P000; -.
DR MaxQB; Q9P000; -.
DR PaxDb; Q9P000; -.
DR PeptideAtlas; Q9P000; -.
DR PRIDE; Q9P000; -.
DR ProteomicsDB; 83528; -. [Q9P000-1]
DR ProteomicsDB; 83529; -. [Q9P000-2]
DR Antibodypedia; 2123; 174 antibodies from 21 providers.
DR DNASU; 29099; -.
DR Ensembl; ENST00000263401.10; ENSP00000263401.5; ENSG00000110442.12. [Q9P000-1]
DR Ensembl; ENST00000452374.6; ENSP00000392510.2; ENSG00000110442.12. [Q9P000-2]
DR GeneID; 29099; -.
DR KEGG; hsa:29099; -.
DR MANE-Select; ENST00000263401.10; ENSP00000263401.5; NM_014186.4; NP_054905.2.
DR UCSC; uc001mwn.5; human. [Q9P000-1]
DR CTD; 29099; -.
DR DisGeNET; 29099; -.
DR GeneCards; COMMD9; -.
DR HGNC; HGNC:25014; COMMD9.
DR HPA; ENSG00000110442; Low tissue specificity.
DR MIM; 612299; gene.
DR neXtProt; NX_Q9P000; -.
DR OpenTargets; ENSG00000110442; -.
DR PharmGKB; PA134930445; -.
DR VEuPathDB; HostDB:ENSG00000110442; -.
DR eggNOG; ENOG502RHPY; Eukaryota.
DR GeneTree; ENSGT00390000006218; -.
DR HOGENOM; CLU_118635_0_0_1; -.
DR InParanoid; Q9P000; -.
DR OMA; CVQSHRG; -.
DR PhylomeDB; Q9P000; -.
DR TreeFam; TF323880; -.
DR PathwayCommons; Q9P000; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9P000; -.
DR BioGRID-ORCS; 29099; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; COMMD9; human.
DR GeneWiki; COMMD9; -.
DR GenomeRNAi; 29099; -.
DR Pharos; Q9P000; Tdark.
DR PRO; PR:Q9P000; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P000; protein.
DR Bgee; ENSG00000110442; Expressed in hindlimb stylopod muscle and 200 other tissues.
DR ExpressionAtlas; Q9P000; baseline and differential.
DR Genevisible; Q9P000; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR037360; COMMD9.
DR PANTHER; PTHR15663; PTHR15663; 1.
DR Pfam; PF07258; COMM_domain; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Ion transport; Nucleus; Reference proteome; Sodium; Sodium transport;
KW Transcription; Transcription regulation; Transport;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..198
FT /note="COMM domain-containing protein 9"
FT /id="PRO_0000077403"
FT DOMAIN 122..196
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VAR_SEQ 18..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041499"
FT CONFLICT 45
FT /note="V -> F (in Ref. 3; CAB66623)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="G -> R (in Ref. 1; AAS22246 and 2; AAF29130)"
FT /evidence="ECO:0000305"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:4OE9"
FT HELIX 92..114
FT /evidence="ECO:0007829|PDB:4OE9"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:6BP6"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:6BP6"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:6BP6"
FT HELIX 175..198
FT /evidence="ECO:0007829|PDB:6BP6"
SQ SEQUENCE 198 AA; 21819 MW; 54DA2FE525C3A24F CRC64;
MAALTAEHFA ALQSLLKASS KDVVRQLCQE SFSSSALGLK KLLDVTCSSL SVTQEEAEEL
LQALHRLTRL VAFRDLSSAE AILALFPENF HQNLKNLLTK IILEHVSTWR TEAQANQISL
PRLVDLDWRV DIKTSSDSIS RMAVPTCLLQ MKIQEDPSLC GDKPSISAVT VELSKETLDT
MLDGLGRIRD QLSAVASK
