ID   PRLD1_MOUSE             Reviewed;         217 AA.
AC   Q8R107; Q3UCN0; Q4QQJ9; Q6PCZ5; Q78IE2; Q9D1F7;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=PRELI domain-containing protein 1, mitochondrial;
DE   AltName: Full=Px19-like protein;
DE   Flags: Precursor;
GN   Name=Prelid1; Synonyms=Preli;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14640972; DOI=10.1042/bj20031504;
RA   Fox E.J., Stubbs S.A., Kyaw Tun J., Leek J.P., Markham A.F., Wright S.C.;
RT   "PRELI (protein of relevant evolutionary and lymphoid interest) is located
RT   within an evolutionarily conserved gene cluster on chromosome 5q34-q35 and
RT   encodes a novel mitochondrial protein.";
RL   Biochem. J. 378:817-825(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Dendritic cell, Embryo, and
RC   Embryonic stomach;
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=C57BL/6J, Czech II, and FVB/N;
RC   TISSUE=Brain, Lung tumor, and 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   [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).
RN   [5]
RP   FUNCTION.
RX   PubMed=21364629; DOI=10.1038/cddis.2009.19;
RA   McKeller M.R., Herrera-Rodriguez S., Ma W., Ortiz-Quintero B., Rangel R.,
RA   Cande C., Sims-Mourtada J.C., Melnikova V., Kashi C., Phan L.M., Chen Z.,
RA   Huang P., Dunner K. Jr., Kroemer G., Singh K.K., Martinez-Valdez H.;
RT   "Vital function of PRELI and essential requirement of its LEA motif.";
RL   Cell Death Dis. 1:E21-E21(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. Regulates
CC       the mitochondrial apoptotic pathway in primary Th cells. Regulates Th
CC       cell differentiation by down-regulating STAT6 thereby reducing IL-4-
CC       induced Th2 cell number. May be important for the development of vital
CC       and immunocompetent organs (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y255, ECO:0000269|PubMed:21364629}.
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:Q9Y255};
CC   -!- SUBUNIT: Forms a complex with TRIAP1 in the mitochondrion intermembrane
CC       space. Interacts with OPA1 and AIFM1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y255, ECO:0000269|PubMed:21364629}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14640972}.
CC       Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9Y255}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in all tissues tested except
CC       testis with highest levels in thymus. {ECO:0000269|PubMed:14640972}.
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DR   EMBL; AK003629; BAB22898.2; -; mRNA.
DR   EMBL; AK146857; BAE27486.1; -; mRNA.
DR   EMBL; AK150465; BAE29582.1; -; mRNA.
DR   EMBL; AK151321; BAE30302.1; -; mRNA.
DR   EMBL; AK155042; BAE33009.1; -; mRNA.
DR   EMBL; BC024813; AAH24813.2; -; mRNA.
DR   EMBL; BC025859; AAH25859.1; -; mRNA.
DR   EMBL; BC098241; AAH98241.1; -; mRNA.
DR   CCDS; CCDS26542.1; -.
DR   RefSeq; NP_079872.4; NM_025596.5.
DR   AlphaFoldDB; Q8R107; -.
DR   SMR; Q8R107; -.
DR   STRING; 10090.ENSMUSP00000021942; -.
DR   PhosphoSitePlus; Q8R107; -.
DR   EPD; Q8R107; -.
DR   PaxDb; Q8R107; -.
DR   PeptideAtlas; Q8R107; -.
DR   PRIDE; Q8R107; -.
DR   ProteomicsDB; 291813; -.
DR   Antibodypedia; 1204; 160 antibodies from 23 providers.
DR   DNASU; 66494; -.
DR   Ensembl; ENSMUST00000021942; ENSMUSP00000021942; ENSMUSG00000021486.
DR   GeneID; 66494; -.
DR   KEGG; mmu:66494; -.
DR   UCSC; uc007qql.1; mouse.
DR   CTD; 27166; -.
DR   MGI; MGI:1913744; Prelid1.
DR   VEuPathDB; HostDB:ENSMUSG00000021486; -.
DR   eggNOG; KOG3337; Eukaryota.
DR   GeneTree; ENSGT00950000182810; -.
DR   HOGENOM; CLU_067902_3_0_1; -.
DR   InParanoid; Q8R107; -.
DR   OMA; LAFFNRY; -.
DR   OrthoDB; 1369397at2759; -.
DR   PhylomeDB; Q8R107; -.
DR   TreeFam; TF313119; -.
DR   Reactome; R-MMU-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR   BioGRID-ORCS; 66494; 28 hits in 72 CRISPR screens.
DR   ChiTaRS; Prelid1; mouse.
DR   PRO; PR:Q8R107; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8R107; protein.
DR   Bgee; ENSMUSG00000021486; Expressed in endothelial cell of lymphatic vessel and 251 other tissues.
DR   Genevisible; Q8R107; MM.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:1990050; F:phosphatidic acid transfer activity; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR   GO; GO:1901857; P:positive regulation of cellular respiration; ISS:UniProtKB.
DR   GO; GO:0010950; P:positive regulation of endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR   GO; GO:0070234; P:positive regulation of T cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0097035; P:regulation of membrane lipid distribution; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0045580; P:regulation of T cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR006797; PRELI/MSF1_dom.
DR   InterPro; IPR037365; Slowmo/Ups.
DR   PANTHER; PTHR11158; PTHR11158; 1.
DR   Pfam; PF04707; PRELI; 1.
DR   PROSITE; PS50904; PRELI_MSF1; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Lipid transport; Mitochondrion; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y255"
FT   CHAIN           ?..217
FT                   /note="PRELI domain-containing protein 1, mitochondrial"
FT                   /id="PRO_0000097120"
FT   DOMAIN          36..174
FT                   /note="PRELI/MSF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00158"
FT   CONFLICT        40
FT                   /note="V -> L (in Ref. 2; BAE29582)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   217 AA;  24960 MW;  8D909AB939B6D851 CRC64;
     MVKYFLGQSV LRSSWDQVFA AFWQRYPNPY SKHVLTEDIV HREVTPDQKL LSRRLLTKTN
     RMPRWAERLF PANVAHSVYI LEDSIVDPQN QTMTTFTWNI NHARLMVVEE RCVYCVNSDN
     SGWTEIRREA WVSSSLFGVS RAVQEFGLAR FKSNVTKTMK GFEYILAKLQ GEAPSKTLVE
     TAKEAKEKAK ETALAATEKA KDLANKAATK QQQRQLV