ID COMD1_MOUSE Reviewed; 188 AA.
AC Q8K4M5; Q3V012; Q80WG2; Q80Z41; Q8BNL9; Q8K2S9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=COMM domain-containing protein 1;
DE AltName: Full=Protein Murr1;
GN Name=Commd1; Synonyms=Murr1;
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 STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-23.
RC STRAIN=C57BL/6J;
RX PubMed=14673161; DOI=10.1128/mcb.24.1.270-279.2004;
RA Wang Y., Joh K., Masuko S., Yatsuki H., Soejima H., Nabetani A.,
RA Beechey C.V., Okinami S., Mukai T.;
RT "The mouse Murr1 gene is imprinted in the adult brain, presumably due to
RT transcriptional interference by the antisense-oriented U2af1-rs1 gene.";
RL Mol. Cell. Biol. 24:270-279(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-188.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Proposed scaffold protein that is implicated in diverse
CC physiological processes and whose function may be in part linked to its
CC ability to regulate ubiquitination of specific cellular proteins. Can
CC modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by
CC displacing CAND1; in vitro promotes CRL E3 activity and dissociates
CC CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit
CC RELA and its subsequent proteasomal degradation. Down-regulates NF-
CC kappa-B activity. Involved in the regulation of membrane expression and
CC ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial
CC cells by regulation of apical cell surface expression of amiloride-
CC sensitive sodium channel (ENaC) subunits and by promoting their
CC ubiquitination presumably involving NEDD4L. Promotes the localization
CC of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression
CC through regulation of its ubiquitination. Down-regulates SOD1 activity
CC by interfering with its homodimerization. Plays a role in copper ion
CC homeostasis. Involved in copper-dependent ATP7A trafficking between the
CC trans-Golgi network and vesicles in the cell periphery; the function is
CC proposed to depend on its association within the CCC complex and
CC cooperation with the WASH complex on early endosomes. Can bind one
CC copper ion per monomer. May function to facilitate biliary copper
CC excretion within hepatocytes. Binds to phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-
CC mediated transcription; competes with ARNT/Hif-1-beta for binding to
CC HIF1A resulting in decreased DNA binding and impaired transcriptional
CC activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell
CC cycle progression and cell proliferation by stimulating ubiquitination
CC of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and
CC actin-dependent manner. {ECO:0000250|UniProtKB:Q8N668}.
CC -!- SUBUNIT: Monomer, homodimer. Can form heterodimers with other COMM
CC domain-containing proteins but only certain combinations may exist in
CC vivo. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4, COMMD5,
CC COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain). Identified in a
CC complex with an E3 ubiquitin ligase complex composed of TCEB1/elongin
CC C, CUL2, SOCS1 and RBX1; in the complex interacts directly with SOCS1
CC and CUL2. Interacts directly with ATP7B (via the N-terminal region).
CC Interacts with CCS, CDKN2A, RELA, REL, RELB, NFKB1/p105, NFKB2/p100,
CC NFKBIB, SCNN1D, SCNN1B, CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A,
CC CUL4B, CUL5, CUL7, HIF1A. Identified in a complex with NF-kappa-B.
CC Interacts directly with SLC12A2. Interacts with CCDC22 and CCDC93;
CC proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex
CC which contains at least COMMD1 (and possibly other COMM domain-
CC containing proteins), CCDC22, CCDC93. Interacts with VPS35L; the
CC interaction associates CCC complex with retriever complex. Interacts
CC with ATP7A. Interacts with FAM107A; this interaction stabilizes COMMD1
CC in the nucleus. {ECO:0000250|UniProtKB:Q8N668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N668}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8N668}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8N668}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q8N668}. Early endosome
CC {ECO:0000250|UniProtKB:Q8N668}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q8N668}. Note=Shuttles between nucleus and
CC cytosol. Detected in perinuclear foci that may be aggresomes containing
CC misfolded, ubiquitinated proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q8N668}.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked
CC polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q8N668}.
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DR EMBL; AK133507; BAE21693.1; -; mRNA.
DR EMBL; AB089806; BAC07535.1; -; Genomic_DNA.
DR EMBL; AB104816; BAC57942.1; -; mRNA.
DR EMBL; BC030052; AAH30052.1; -; mRNA.
DR EMBL; BC051210; AAH51210.1; -; mRNA.
DR CCDS; CCDS24472.1; -.
DR RefSeq; NP_653097.2; NM_144514.2.
DR AlphaFoldDB; Q8K4M5; -.
DR SMR; Q8K4M5; -.
DR BioGRID; 201620; 1.
DR IntAct; Q8K4M5; 3.
DR MINT; Q8K4M5; -.
DR STRING; 10090.ENSMUSP00000124719; -.
DR iPTMnet; Q8K4M5; -.
DR PhosphoSitePlus; Q8K4M5; -.
DR EPD; Q8K4M5; -.
DR MaxQB; Q8K4M5; -.
DR PaxDb; 10090-ENSMUSP00000124719; -.
DR ProteomicsDB; 283602; -.
DR Pumba; Q8K4M5; -.
DR DNASU; 17846; -.
DR Ensembl; ENSMUST00000159081.8; ENSMUSP00000124719.2; ENSMUSG00000051355.19.
DR GeneID; 17846; -.
DR KEGG; mmu:17846; -.
DR UCSC; uc007iel.1; mouse.
DR AGR; MGI:109474; -.
DR CTD; 150684; -.
DR MGI; MGI:109474; Commd1.
DR VEuPathDB; HostDB:ENSMUSG00000051355; -.
DR eggNOG; ENOG502RXN6; Eukaryota.
DR GeneTree; ENSGT00390000012029; -.
DR HOGENOM; CLU_126878_0_0_1; -.
DR InParanoid; Q8K4M5; -.
DR OMA; MAFTHSC; -.
DR OrthoDB; 6795at2759; -.
DR PhylomeDB; Q8K4M5; -.
DR TreeFam; TF332823; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 17846; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Commd1; mouse.
DR PRO; PR:Q8K4M5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K4M5; Protein.
DR Bgee; ENSMUSG00000051355; Expressed in floor plate of midbrain and 274 other cell types or tissues.
DR ExpressionAtlas; Q8K4M5; baseline and differential.
DR Genevisible; Q8K4M5; MM.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019871; F:sodium channel inhibitor activity; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0055070; P:copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:MGI.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; ISO:MGI.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:MGI.
DR GO; GO:1902072; P:negative regulation of hypoxia-inducible factor-1alpha signaling pathway; IMP:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR GO; GO:1904109; P:positive regulation of cholesterol import; IMP:MGI.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; IMP:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IMP:MGI.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd04749; Commd1_MURR1; 1.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR033776; COMMD1_N.
DR InterPro; IPR037351; Murr1.
DR PANTHER; PTHR21199; COMM DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR21199:SF1; COMM DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF07258; COMM_domain; 1.
DR Pfam; PF17221; COMMD1_N; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; Cytoplasmic vesicle; Endosome; Membrane; Metal-binding;
KW Nucleus; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..188
FT /note="COMM domain-containing protein 1"
FT /id="PRO_0000077385"
FT DOMAIN 117..185
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT REGION 1..122
FT /note="Sufficient for interaction with SLC12A2"
FT /evidence="ECO:0000250|UniProtKB:Q8N668"
FT REGION 124..188
FT /note="Required for binding to PtdIns(4,5)P2"
FT /evidence="ECO:0000250|UniProtKB:Q8N668"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 133
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="L -> H (in Ref. 3; AAH51210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 20996 MW; EEEC6489BC59B483 CRC64;
MAGDLEGGKS LSGLLSGLAQ NAFHGHSGVT EELLHSQLYP EVPPEEFRPF LAKMRGLLKS
IASADMDFNQ LEAFLTAQTK KQGGITSEQA AVISKFWKSH KIKIRESLMK QSRWDNGLRG
LSWRVDGKSQ SRHSTQIHSP VAIIELEFGK NGQESEFLCL EFDEVKVKQI LKKLSEVEES
INRLMQAA
//
