ID   COMD5_RAT               Reviewed;         224 AA.
AC   Q9ERR2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=COMM domain-containing protein 5;
DE   AltName: Full=Hypertension-related calcium-regulated gene protein;
DE            Short=HCaRG;
GN   Name=Commd5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=SHR; TISSUE=Parathyroid;
RX   PubMed=10918053; DOI=10.1074/jbc.m001352200;
RA   Solban N., Jia H.-P., Richard S., Tremblay S., Devlin A.M., Peng J.,
RA   Gossard F., Guo D.-F., Morel G., Hamet P., Lewanczuk R., Tremblay J.;
RT   "HCaRG, a novel calcium-regulated gene coding for a nuclear protein, is
RT   potentially involved in the regulation of cell proliferation.";
RL   J. Biol. Chem. 275:32234-32243(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=12620924; DOI=10.1152/ajprenal.00252.2002;
RA   Devlin A.M., Solban N., Tremblay S., Gutkowska J., Schurch W., Orlov S.N.,
RA   Lewanczuk R., Hamet P., Tremblay J.;
RT   "HCaRG is a novel regulator of renal epithelial cell growth and
RT   differentiation causing G2M arrest.";
RL   Am. J. Physiol. 284:F753-F762(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=24515317; DOI=10.1007/s40620-014-0054-3;
RA   Matsuda H., Hamet P., Tremblay J.;
RT   "Hypertension-related, calcium-regulated gene (HCaRG/COMMD5) and kidney
RT   diseases: HCaRG accelerates tubular repair.";
RL   J. Nephrol. 27:351-360(2014).
CC   -!- FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase
CC       (CRL) complexes (By similarity). Negatively regulates cell
CC       proliferation. Negatively regulates cell cycle G2/M phase transition
CC       probably by transactivating p21/CDKN1A through the p53/TP53-independent
CC       signaling pathway (PubMed:12620924). Involved in kidney proximal tubule
CC       morphogenesis (PubMed:24515317). Down-regulates activation of NF-kappa-
CC       B (By similarity). {ECO:0000250, ECO:0000269|PubMed:12620924,
CC       ECO:0000269|PubMed:24515317}.
CC   -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10918053}.
CC   -!- TISSUE SPECIFICITY: Expressed in the zona fasciculata and medulla of
CC       the adrenal gland; expressed in kidney proximal tubules. Basal
CC       expression is higher in hypertensive than in normotensive animals.
CC       {ECO:0000269|PubMed:10918053}.
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DR   EMBL; AF290194; AAG09914.1; -; mRNA.
DR   RefSeq; NP_620808.1; NM_139108.2.
DR   AlphaFoldDB; Q9ERR2; -.
DR   SMR; Q9ERR2; -.
DR   IntAct; Q9ERR2; 1.
DR   STRING; 10116.ENSRNOP00000005925; -.
DR   jPOST; Q9ERR2; -.
DR   PaxDb; Q9ERR2; -.
DR   PRIDE; Q9ERR2; -.
DR   GeneID; 245974; -.
DR   KEGG; rno:245974; -.
DR   UCSC; RGD:621468; rat.
DR   CTD; 28991; -.
DR   RGD; 621468; Commd5.
DR   eggNOG; ENOG502RCJ6; Eukaryota.
DR   InParanoid; Q9ERR2; -.
DR   OrthoDB; 1351388at2759; -.
DR   PhylomeDB; Q9ERR2; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   PRO; PR:Q9ERR2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:RGD.
DR   GO; GO:0072158; P:proximal tubule morphogenesis; IDA:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:RGD.
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   2: Evidence at transcript level;
KW   Acetylation; 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_0000077397"
FT   DOMAIN          151..215
FT                   /note="COMM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZQ3"
SQ   SEQUENCE   224 AA;  24453 MW;  AFE908DA9477FC0B CRC64;
     MSALGAAAPY LHHPADSHSG RVSFLGSQPS PEVTAVAQLL KDLDRSTFRK LLKLVVGALH
     GKDCREAVEQ LGASANLSEE RLAVLLAGTH TLLQQALRLP PASLKPDAFQ EELQELGIPQ
     DLIGDLASLA FGSQRPLLDS VAQQQGSSLP HVSYFRWRVD VAISTSAQSR SLQPSVLMQL
     KLTDGSAHRF EVPIAKFQEL RYSVALVLKE MAELEKKCER KLQD