COMD5_MOUSE
ID COMD5_MOUSE Reviewed; 224 AA.
AC Q8R395; Q9D6R8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=COMM domain-containing protein 5;
GN Name=Commd5;
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=Tongue;
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 [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: May modulate activity of cullin-RING E3 ubiquitin ligase
CC (CRL) complexes. Negatively regulates cell proliferation. Negatively
CC regulates cell cycle G2/M phase transition probably by transactivating
CC p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved
CC in kidney proximal tubule morphogenesis. Down-regulates activation of
CC NF-kappa-B. {ECO:0000250|UniProtKB:Q9ERR2,
CC ECO:0000250|UniProtKB:Q9GZQ3}.
CC -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain).
CC Interacts with RELA, RELB, NFKB1/p105. Interacts with CCDC22, CCDC93,
CC SCNN1B, CUL2, CUL3, CUL4A, CUL4B, CUL7. {ECO:0000250|UniProtKB:Q9GZQ3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZQ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9GZQ3}.
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DR EMBL; AK010045; BAB26663.1; -; mRNA.
DR EMBL; BC025891; AAH25891.1; -; mRNA.
DR CCDS; CCDS27594.1; -.
DR RefSeq; NP_079812.1; NM_025536.2.
DR AlphaFoldDB; Q8R395; -.
DR SMR; Q8R395; -.
DR BioGRID; 211442; 5.
DR STRING; 10090.ENSMUSP00000069159; -.
DR iPTMnet; Q8R395; -.
DR PhosphoSitePlus; Q8R395; -.
DR EPD; Q8R395; -.
DR jPOST; Q8R395; -.
DR MaxQB; Q8R395; -.
DR PaxDb; Q8R395; -.
DR PeptideAtlas; Q8R395; -.
DR PRIDE; Q8R395; -.
DR ProteomicsDB; 283789; -.
DR DNASU; 66398; -.
DR GeneID; 66398; -.
DR KEGG; mmu:66398; -.
DR UCSC; uc007wms.1; mouse.
DR CTD; 28991; -.
DR MGI; MGI:1913648; Commd5.
DR eggNOG; ENOG502RCJ6; Eukaryota.
DR InParanoid; Q8R395; -.
DR OrthoDB; 1351388at2759; -.
DR PhylomeDB; Q8R395; -.
DR TreeFam; TF323880; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 66398; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Commd5; mouse.
DR PRO; PR:Q8R395; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R395; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:MGI.
DR GO; GO:0072158; P:proximal tubule morphogenesis; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR037357; COMMD5.
DR PANTHER; PTHR15666; PTHR15666; 1.
DR Pfam; PF07258; COMM_domain; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ3"
FT CHAIN 2..224
FT /note="COMM domain-containing protein 5"
FT /id="PRO_0000077396"
FT DOMAIN 151..215
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ3"
FT CONFLICT 7
FT /note="P -> A (in Ref. 1; BAB26663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24493 MW; 423091DFE266DE18 CRC64;
MSALGAPAPY LHHPTDSHSG RVSFLGSQPS AEVTAVAQLL KDLDRSTFRK LLKLVVGALH
GKDCREAVQH LGASANLSEE RLAVLLAGTH TLLQQALRLP PASLKPDAFQ DELQELGIPQ
DMIGDLASLA FGSQRPLLDS VAQQQGSSLP RVSNFRWRVD VAISTSAQSR SLQPSVLMQL
KLTDGSAHRF EVPIAKFQEL RYSVALVLKE MAELERKCER KLQD
