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COMD1_MOUSE
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   03-AUG-2022, entry version 123.
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; Q8K4M5; -.
DR   PRIDE; Q8K4M5; -.
DR   ProteomicsDB; 283602; -.
DR   DNASU; 17846; -.
DR   Ensembl; ENSMUST00000159081; ENSMUSP00000124719; ENSMUSG00000051355.
DR   GeneID; 17846; -.
DR   KEGG; mmu:17846; -.
DR   UCSC; uc007iel.1; mouse.
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; SWRIDIK; -.
DR   OrthoDB; 1323631at2759; -.
DR   PhylomeDB; Q8K4M5; -.
DR   TreeFam; TF332823; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   BioGRID-ORCS; 17846; 2 hits in 72 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 272 other 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:0006878; P:cellular copper ion homeostasis; 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: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; PTHR21199; 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
 
 
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