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CRLS1_MOUSE
ID   CRLS1_MOUSE             Reviewed;         303 AA.
AC   Q80ZM8; Q9D4U1;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Cardiolipin synthase (CMP-forming);
DE            Short=CLS;
DE            EC=2.7.8.41 {ECO:0000250|UniProtKB:Q9UJA2};
GN   Name=Crls1;
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 [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-303.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Liver, and Testis;
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: Catalyzes the synthesis of cardiolipin (CL)
CC       (diphosphatidylglycerol) by specifically transferring a phosphatidyl
CC       group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key
CC       phospholipid in mitochondrial membranes and plays important roles in
CC       maintaining the functional integrity and dynamics of mitochondria under
CC       both optimal and stress conditions. {ECO:0000250|UniProtKB:Q9UJA2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-
CC         diacyl-sn-glycerol = a cardiolipin + CMP + H(+);
CC         Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41;
CC         Evidence={ECO:0000250|UniProtKB:Q9UJA2};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC048702; AAH48702.1; -; mRNA.
DR   EMBL; AK016165; BAB30134.1; ALT_INIT; mRNA.
DR   CCDS; CCDS16779.1; -.
DR   RefSeq; NP_001019556.1; NM_001024385.1.
DR   RefSeq; NP_079922.2; NM_025646.3.
DR   AlphaFoldDB; Q80ZM8; -.
DR   SMR; Q80ZM8; -.
DR   BioGRID; 211572; 5.
DR   STRING; 10090.ENSMUSP00000028835; -.
DR   PhosphoSitePlus; Q80ZM8; -.
DR   MaxQB; Q80ZM8; -.
DR   PaxDb; Q80ZM8; -.
DR   PRIDE; Q80ZM8; -.
DR   ProteomicsDB; 278037; -.
DR   Antibodypedia; 23985; 143 antibodies from 27 providers.
DR   DNASU; 66586; -.
DR   Ensembl; ENSMUST00000028835; ENSMUSP00000028835; ENSMUSG00000027357.
DR   GeneID; 66586; -.
DR   KEGG; mmu:66586; -.
DR   UCSC; uc008mnk.1; mouse.
DR   CTD; 54675; -.
DR   MGI; MGI:1913836; Crls1.
DR   VEuPathDB; HostDB:ENSMUSG00000027357; -.
DR   eggNOG; KOG1617; Eukaryota.
DR   GeneTree; ENSGT00390000001607; -.
DR   HOGENOM; CLU_051314_0_1_1; -.
DR   InParanoid; Q80ZM8; -.
DR   OMA; KRFNMAS; -.
DR   OrthoDB; 1169813at2759; -.
DR   PhylomeDB; Q80ZM8; -.
DR   TreeFam; TF314169; -.
DR   BRENDA; 2.7.8.41; 3474.
DR   Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-MMU-1483076; Synthesis of CL.
DR   BioGRID-ORCS; 66586; 23 hits in 77 CRISPR screens.
DR   ChiTaRS; Crls1; mouse.
DR   PRO; PR:Q80ZM8; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q80ZM8; protein.
DR   Bgee; ENSMUSG00000027357; Expressed in spermatid and 228 other tissues.
DR   ExpressionAtlas; Q80ZM8; baseline and differential.
DR   Genevisible; Q80ZM8; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0008808; F:cardiolipin synthase activity; ISO:MGI.
DR   GO; GO:0043337; F:CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase activity; IEA:RHEA.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:1905711; P:response to phosphatidylethanolamine; ISO:MGI.
DR   GO; GO:0097068; P:response to thyroxine; ISO:MGI.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
PE   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..303
FT                   /note="Cardiolipin synthase (CMP-forming)"
FT                   /id="PRO_0000056817"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          69..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  32502 MW;  E8CA43F50E04A388 CRC64;
     MLAWRVARGA WGPLRVALRP PGARLGRGGS RRALLPPAAC CLGCLAERWR LRPAAFALRL
     PGAGPRTHCS GAGKAAPEPA AGGGGAAAQA PSARWVPASA ASSYENPWTI PNLLSMTRIG
     LAPVLGYLIL EEDFNVALGV FALAGLTDLL DGFIARNWAN QKSALGSALD PLADKVLISI
     LYISLTYADL IPVPLTYMII SRDVMLIAAV FYVRYRTLPT PRTLAKYFNP CYATARLKPT
     FISKVNTAVQ LILVAASLAA PVFNYADSIY LQILWCCTAF TTAASAYSYY HYGRKTVQVI
     KGK
 
 
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