GA45G_MOUSE
ID GA45G_MOUSE Reviewed; 159 AA.
AC Q9Z111;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Growth arrest and DNA damage-inducible protein GADD45 gamma;
DE AltName: Full=Cytokine-responsive protein CR6;
GN Name=Gadd45g; Synonyms=Cr6;
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 [MRNA].
RX PubMed=10490824; DOI=10.1038/sj.onc.1202885;
RA Zhang W., Bae I., Krishnaraju K., Azam N., Fan W., Smith K., Hoffman B.,
RA Liebermann D.A.;
RT "CR6: a third member in the MyD118 and Gadd45 gene family which functions
RT in negative growth control.";
RL Oncogene 18:4899-4907(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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).
CC -!- FUNCTION: Involved in the regulation of growth and apoptosis. Mediates
CC activation of stress-responsive MTK1/MEKK4 MAPKKK.
CC -!- SUBUNIT: Undergoes concentration-dependent homodimerization, which is
CC required for growth inhibititory activity and enhances interaction with
CC PCNA. Interacts with GADD45GIP1. Interacts with PCNA (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Z111; P39689: Cdkn1a; NbExp=2; IntAct=EBI-1173616, EBI-1174103;
CC Q9Z111; Q9Z111: Gadd45g; NbExp=5; IntAct=EBI-1173616, EBI-1173616;
CC Q9Z111; P17918: Pcna; NbExp=2; IntAct=EBI-1173616, EBI-1173716;
CC Q9Z111; P12004: PCNA; Xeno; NbExp=9; IntAct=EBI-1173616, EBI-358311;
CC -!- DOMAIN: Two central helices mediate homodimerization through parallel
CC packing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GADD45 family. {ECO:0000305}.
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DR EMBL; AF055638; AAD15798.1; -; mRNA.
DR EMBL; AK002237; BAB21955.1; -; mRNA.
DR PDB; 3CG6; X-ray; 1.70 A; A/B=15-159.
DR PDBsum; 3CG6; -.
DR AlphaFoldDB; Q9Z111; -.
DR SMR; Q9Z111; -.
DR DIP; DIP-29978N; -.
DR IntAct; Q9Z111; 3.
DR STRING; 10090.ENSMUSP00000021903; -.
DR PaxDb; Q9Z111; -.
DR PRIDE; Q9Z111; -.
DR ProteomicsDB; 267414; -.
DR MGI; MGI:1346325; Gadd45g.
DR eggNOG; ENOG502RXKU; Eukaryota.
DR InParanoid; Q9Z111; -.
DR PhylomeDB; Q9Z111; -.
DR ChiTaRS; Gadd45g; mouse.
DR EvolutionaryTrace; Q9Z111; -.
DR PRO; PR:Q9Z111; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z111; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; TAS:MGI.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR024824; GADD45.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR PANTHER; PTHR10411; PTHR10411; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Developmental protein; Differentiation;
KW Reference proteome.
FT CHAIN 1..159
FT /note="Growth arrest and DNA damage-inducible protein
FT GADD45 gamma"
FT /id="PRO_0000148337"
FT REGION 43..86
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3CG6"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3CG6"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:3CG6"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:3CG6"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3CG6"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3CG6"
SQ SEQUENCE 159 AA; 17211 MW; 4B5996927C57988F CRC64;
MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAHGQGCLT AGVYESAKVL NVDPDNVTFC
VLAADEEDEG DIALQIHFTL IQAFCCENDI DIVRVGDVQR LAAIVGADEE GGAPGDLHCI
LISNPNEDTW KDPALEKLSL FCEESRSFND WVPSITLPE
