CGRE1_RAT
ID CGRE1_RAT Reviewed; 281 AA.
AC P97586;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cell growth regulator with EF hand domain protein 1 {ECO:0000305};
DE AltName: Full=Cell growth regulatory gene 11 protein;
DE AltName: Full=Hydrophobestin;
DE Flags: Precursor;
GN Name=Cgref1 {ECO:0000312|RGD:620801}; Synonyms=Cgr11;
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].
RC STRAIN=Fischer; TISSUE=Fibroblast;
RX PubMed=8968090;
RA Madden S.L., Galella E.A., Riley D., Bertelsen A.H., Beaudry G.A.;
RT "Induction of cell growth regulatory genes by p53.";
RL Cancer Res. 56:5384-5390(1996).
RN [2]
RP FUNCTION, CALCIUM-BINDING, SUBCELLULAR LOCATION, PTM, AND TISSUE
RP SPECIFICITY.
RX PubMed=19473726; DOI=10.1016/j.ejcb.2009.04.003;
RA Devnath S., Kataoka T., Miura K., Kusuda M., Kitamura K., Kumada Y.,
RA Mochiduki A., Kaneko K., Adachi A., Inoue K.;
RT "Cgr11 encodes a secretory protein involved in cell adhesion.";
RL Eur. J. Cell Biol. 88:521-529(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217 AND SER-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates cell-cell adhesion in a calcium-dependent manner.
CC Able to inhibit growth in several cell lines.
CC {ECO:0000269|PubMed:19473726}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19473726}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in whole brain and kidney,
CC with limited expression in heart, lung, liver, and skeletal muscle and
CC no expression in spleen and testis. Also expressed in pituitary gland,
CC adrenal gland, digestive tract, and reproductive organs.
CC {ECO:0000269|PubMed:19473726}.
CC -!- INDUCTION: By p53.
CC -!- DOMAIN: Both EF-hands are required for function.
CC -!- PTM: Probably digested extracellularly by an unknown serine protease
CC generating extremely hydrophobic bioactive peptides.
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DR EMBL; U66470; AAC52950.1; -; mRNA.
DR RefSeq; NP_620787.2; NM_139087.2.
DR AlphaFoldDB; P97586; -.
DR SMR; P97586; -.
DR STRING; 10116.ENSRNOP00000010586; -.
DR iPTMnet; P97586; -.
DR PhosphoSitePlus; P97586; -.
DR jPOST; P97586; -.
DR PaxDb; P97586; -.
DR GeneID; 245918; -.
DR KEGG; rno:245918; -.
DR CTD; 10669; -.
DR RGD; 620801; Cgref1.
DR eggNOG; ENOG502S2TZ; Eukaryota.
DR InParanoid; P97586; -.
DR OrthoDB; 1308168at2759; -.
DR PhylomeDB; P97586; -.
DR TreeFam; TF315801; -.
DR PRO; PR:P97586; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
DR InterPro; IPR040139; CGREF1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23104:SF11; PTHR23104:SF11; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell cycle; Growth arrest; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..281
FT /note="Cell growth regulator with EF hand domain protein 1"
FT /id="PRO_0000073876"
FT DOMAIN 71..106
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 115..150
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 146..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 281 AA; 30835 MW; C8195BED34BB1549 CRC64;
MSRWLMQMLM LPLLLLPLGQ AAPKDGVARL DPEAQQQLTT NPFQPGPEQL RRLRDYLKGL
EKMEEDPEQM NREQVLLYLF ALHDFDQNGQ LDGLELLSML TAALAPGAAH FPINPVILVV
DMVLETQDLD GDGLMTPAEL INFPGEAPKR AESLPPALQE PQPAGSQPLL ANSPLQSETQ
QSLGTKEEIT SQVEAKRALE PEQEAGHHIE TKVDALSPEG EARGQAESEG DAPGPREDAE
RQVESKDNEG EAKDLPAETL ETQNTPNVVE AHSIQLENDE I
