TRIA1_MOUSE
ID TRIA1_MOUSE Reviewed; 76 AA.
AC Q9D8Z2; Q6LCG5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=TP53-regulated inhibitor of apoptosis 1;
DE AltName: Full=Protein 15E1.1;
DE AltName: Full=WF-1;
DE AltName: Full=p53-inducible cell-survival factor;
DE Short=p53CSV;
GN Name=Triap1; Synonyms=15e1.1;
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].
RC STRAIN=RS-4; TISSUE=Fibroblast;
RA Sugihara T.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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, and Kidney;
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: Involved in the modulation of the mitochondrial apoptotic
CC pathway by ensuring the accumulation of cardiolipin (CL) in
CC mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates
CC the transfer of phosphatidic acid (PA) between liposomes and probably
CC functions as a PA transporter across the mitochondrion intermembrane
CC space to provide PA for CL synthesis in the inner membrane. Likewise,
CC the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid
CC (PA) between liposomes (in vitro) and probably functions as a PA
CC transporter across the mitochondrion intermembrane space (in vivo).
CC Mediates cell survival by inhibiting activation of caspase-9 which
CC prevents induction of apoptosis. {ECO:0000250|UniProtKB:O43715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000250|UniProtKB:O43715};
CC -!- SUBUNIT: Monomer. Interacts with APAF1 and HSP70. Forms a complex with
CC PRELID1 in the mitochondrion intermembrane space. Interacts with
CC PRELID3A. {ECO:0000250|UniProtKB:O43715}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O43715}.
CC Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}.
CC -!- SIMILARITY: Belongs to the TRIAP1/MDM35 family. {ECO:0000305}.
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DR EMBL; U61156; AAR00569.1; -; mRNA.
DR EMBL; AK007514; BAB25082.1; -; mRNA.
DR EMBL; BC030325; AAH30325.1; -; mRNA.
DR CCDS; CCDS39228.1; -.
DR RefSeq; NP_081209.1; NM_026933.2.
DR AlphaFoldDB; Q9D8Z2; -.
DR SMR; Q9D8Z2; -.
DR BioGRID; 213214; 2.
DR STRING; 10090.ENSMUSP00000031508; -.
DR iPTMnet; Q9D8Z2; -.
DR PhosphoSitePlus; Q9D8Z2; -.
DR EPD; Q9D8Z2; -.
DR MaxQB; Q9D8Z2; -.
DR PaxDb; Q9D8Z2; -.
DR PeptideAtlas; Q9D8Z2; -.
DR PRIDE; Q9D8Z2; -.
DR ProteomicsDB; 298224; -.
DR Antibodypedia; 53934; 48 antibodies from 17 providers.
DR DNASU; 69076; -.
DR Ensembl; ENSMUST00000031508; ENSMUSP00000031508; ENSMUSG00000029535.
DR GeneID; 69076; -.
DR KEGG; mmu:69076; -.
DR UCSC; uc008zds.1; mouse.
DR CTD; 51499; -.
DR MGI; MGI:1916326; Triap1.
DR VEuPathDB; HostDB:ENSMUSG00000029535; -.
DR eggNOG; KOG3481; Eukaryota.
DR GeneTree; ENSGT00940000162087; -.
DR HOGENOM; CLU_101473_4_0_1; -.
DR InParanoid; Q9D8Z2; -.
DR OMA; KQWYAYT; -.
DR OrthoDB; 1552088at2759; -.
DR PhylomeDB; Q9D8Z2; -.
DR TreeFam; TF326640; -.
DR Reactome; R-MMU-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR BioGRID-ORCS; 69076; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Triap1; mouse.
DR PRO; PR:Q9D8Z2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D8Z2; protein.
DR Bgee; ENSMUSG00000029535; Expressed in morula and 246 other tissues.
DR Genevisible; Q9D8Z2; MM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:HGNC.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:HGNC.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; ISS:UniProtKB.
DR InterPro; IPR007918; MDM35_apoptosis.
DR PANTHER; PTHR46403; PTHR46403; 1.
DR Pfam; PF05254; UPF0203; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Coiled coil; Disulfide bond; Lipid transport;
KW Mitochondrion; Reference proteome; Transport.
FT CHAIN 1..76
FT /note="TP53-regulated inhibitor of apoptosis 1"
FT /id="PRO_0000220524"
FT DOMAIN 5..55
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COILED 1..52
FT /evidence="ECO:0000250|UniProtKB:O43715"
FT MOTIF 8..18
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 37..47
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT SITE 27
FT /note="Important for interaction with PRELID3A"
FT /evidence="ECO:0000250|UniProtKB:O43715"
FT SITE 41
FT /note="Important for interaction with PRELID3A"
FT /evidence="ECO:0000250|UniProtKB:O43715"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43715"
FT DISULFID 8..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 18..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT CONFLICT 42
FT /note="K -> I (in Ref. 1; AAR00569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8756 MW; 00B41AC389862094 CRC64;
MNSVGEACTD MKREYDQCFN RWFAEKFLKG DGSGDPCTDL FKRYQQCVQK AIKEKEIPIE
GLEFMGHGKE KPENSS
