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COMM domain-containing protein 1 (Protein Murr1)

 COMD1_CANLF             Reviewed;         188 AA.
Q8WMD0; O97832;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
15-FEB-2017, entry version 71.
RecName: Full=COMM domain-containing protein 1;
AltName: Full=Protein Murr1;
Name=COMMD1; Synonyms=MURR1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DISEASE.
STRAIN=Beagle; TISSUE=Liver;
PubMed=11809725; DOI=10.1093/hmg/11.2.165;
van De Sluis B.A.J., Rothuizen J., Pearson P.L., van Oost B.A.,
Wijmenga C.;
"Identification of a new copper metabolism gene by positional cloning
in a purebred dog population.";
Hum. Mol. Genet. 11:165-173(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-124.
PubMed=9949209; DOI=10.1093/hmg/8.3.501;
van de Sluis B.A.J., Breen M., Nanji M., van Wolferen M., de Jong P.,
Binns M.M., Pearson P.L., Kuipers J., Rothuizen J., Cox D.W.,
Wijmenga C., van Oost B.A.;
"Genetic mapping of the copper toxicosis locus in Bedlington terriers
to dog chromosome 10, in a region syntenic to human chromosome region
2p13-p16.";
Hum. Mol. Genet. 8:501-507(1999).
-!- FUNCTION: Proposed scaffold protein that is implicated in diverse
physiological processes and whose function may be in part linked
to its ability to regulate ubiquitination of specific cellular
proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase
(CRL) complexes by displacing CAND1; in vitro promotes CRL E3
activity and dissociates CAND1 from CUL1 and CUL2. Promotes
ubiquitination of NF-kappa-B subunit RELA and its subsequent
proteasomal degradation. Down-regulates NF-kappa-B activity.
Involved in the regulation of membrane expression and
ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial
cells by regulation of apical cell surface expression of
amiloride-sensitive sodium channel (ENaC) subunits and by
promoting their ubiquitination presumably involving NEDD4L.
Promotes the localization of SCNN1D to recycling endosomes.
Promotes CFTR cell surface expression through regulation of its
ubiquitination. Down-regulates SOD1 activity by interfering with
its homodimerization. Plays a role in copper ion homeostasis.
Involved in copper-dependent ATP7A trafficking between the trans-
Golgi network and vesicles in the cell periphery; the function is
proposed to depend on its association within the CCC complex and
cooperation with the WASH complex on early endosomes. Can bind one
copper ion per monomer. May function to facilitate biliary copper
excretion within hepatocytes. Binds to phosphatidylinositol 4,5-
bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-
mediated transcription; competes with ARNT/Hif-1-beta for binding
to HIF1A resulting in decreased DNA binding and impaired
transcriptional activation by HIF-1.
{ECO:0000250|UniProtKB:Q8N668}.
-!- SUBUNIT: Monomer, homodimer. Can form heterodimers with other COMM
domain-containing proteins but only certain combinations may exist
in vivo. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4,
COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain).
Identified in a complex with an E3 ubiquitin ligase complex
composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1; in the complex
interacts directly with SOCS1 and CUL2. Interacts directly with
ATP7B (via the N-terminal region). Interacts with CCS, CDKN2A,
RELA, REL, RELB, NFKB1/p105, NFKB2/p100, NFKBIB, SCNN1D, SCNN1B,
CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, CUL7,
HIF1A. Identified in a complex with NF-kappa-B. Interacts directly
with SLC12A2. Interacts with CCDC22, CCDC93 and C16orf62 homolog;
proposed to be a component of the CCC (COMMD/CCDC22/CCDC93)
complex which contains at least COMMD1 (and possibly other COMM
domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog.
Interacts with ATP7A (By similarity).
{ECO:0000250|UniProtKB:Q8N668}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N668}.
Cytoplasm {ECO:0000250|UniProtKB:Q8N668}. Endosome membrane
{ECO:0000250|UniProtKB:Q8N668}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:Q8N668}. Early endosome
{ECO:0000250|UniProtKB:Q8N668}. Recycling endosome
{ECO:0000250|UniProtKB:Q8N668}. Note=Shuttles between nucleus and
cytosol. Detected in perinuclear foci that may be aggresomes
containing misfolded, ubiquitinated proteins (By similarity).
{ECO:0000250|UniProtKB:Q8N668}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked
polyubiquitination. Ubiquitinated by XIAP, leading to its
proteasomal degradation (By similarity).
{ECO:0000250|UniProtKB:Q8N668}.
-!- DISEASE: Note=Defects in COMMD1 are the cause of copper toxicosis
(CT) in Bedlington terriers, a genetic disease occurring with a
high prevalence worldwide and is unique to this breed. In
Bedlington terriers the biliary excretion of copper is impaired.
{ECO:0000269|PubMed:11809725}.
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EMBL; AY047597; AAK98638.1; -; mRNA.
EMBL; AY047600; AAK98639.1; -; Genomic_DNA.
EMBL; AY047598; AAK98639.1; JOINED; Genomic_DNA.
EMBL; AY047599; AAK98639.1; JOINED; Genomic_DNA.
EMBL; AF113322; AAD04948.1; -; Genomic_DNA.
RefSeq; NP_001003055.1; NM_001003055.1.
UniGene; Cfa.3453; -.
ProteinModelPortal; Q8WMD0; -.
STRING; 9615.ENSCAFP00000004595; -.
PaxDb; Q8WMD0; -.
GeneID; 403590; -.
KEGG; cfa:403590; -.
CTD; 150684; -.
eggNOG; ENOG410IWFF; Eukaryota.
eggNOG; ENOG4111IWI; LUCA.
HOGENOM; HOG000236295; -.
HOVERGEN; HBG051067; -.
InParanoid; Q8WMD0; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0055070; P:copper ion homeostasis; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IBA:GO_Central.
GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; IBA:GO_Central.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR017920; COMM.
InterPro; IPR033776; COMMD1_N.
Pfam; PF07258; COMM_domain; 1.
Pfam; PF17221; COMMD1_N; 1.
PROSITE; PS51269; COMM; 1.
2: Evidence at transcript level;
Complete proteome; Copper; Cytoplasm; Cytoplasmic vesicle; Endosome;
Membrane; Metal-binding; Nucleus; Protein transport;
Reference proteome; Transcription; Transcription regulation;
Transport; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 188 COMM domain-containing protein 1.
/FTId=PRO_0000077383.
DOMAIN 117 185 COMM. {ECO:0000255|PROSITE-
ProRule:PRU00602}.
REGION 1 122 Sufficient for interaction with SLC12A2.
{ECO:0000250|UniProtKB:Q8N668}.
REGION 124 188 Required for binding to PtdIns(4,5)P2.
{ECO:0000250|UniProtKB:Q8N668}.
METAL 100 100 Copper. {ECO:0000255}.
METAL 109 109 Copper. {ECO:0000255}.
METAL 133 133 Copper. {ECO:0000255}.
SEQUENCE 188 AA; 20916 MW; AFEB81D050F8DD73 CRC64;
MAAELEGSKA LGGLLSGLAQ EAFHGHHGIT EELLRSQLYP EVSLEEFRPF LAKMRGILKS
IASADMDFNQ LEAFLTAQTK KQGGITSDQA AVISKFWKNH KTKIRESLMN QSRWDSGLRG
LSWRVDGKSQ SRHSAQIHTP VAIMELEIGK SGQESEFLCL EFDEVKVSQL LKKLSEVEES
ISTLMQPA


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