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CLS_ORYSJ
ID   CLS_ORYSJ               Reviewed;         329 AA.
AC   Q8H8U0; A0A0P0VW69;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cardiolipin synthase (CMP-forming), mitochondrial;
DE            Short=CLS;
DE            EC=2.7.8.41;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os03g0283600, LOC_Os03g17520;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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:Q93YW7}.
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:Q93YW7};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q93YW7};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
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DR   EMBL; AC084405; AAN64500.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF95333.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11670.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83595.1; -; Genomic_DNA.
DR   EMBL; AK070093; BAG91767.1; -; mRNA.
DR   AlphaFoldDB; Q8H8U0; -.
DR   SMR; Q8H8U0; -.
DR   STRING; 4530.OS03T0283600-01; -.
DR   PaxDb; Q8H8U0; -.
DR   PRIDE; Q8H8U0; -.
DR   EnsemblPlants; Os03t0283600-01; Os03t0283600-01; Os03g0283600.
DR   Gramene; Os03t0283600-01; Os03t0283600-01; Os03g0283600.
DR   eggNOG; KOG1617; Eukaryota.
DR   HOGENOM; CLU_051314_5_0_1; -.
DR   InParanoid; Q8H8U0; -.
DR   OMA; YTARMAS; -.
DR   PlantReactome; R-OSA-1119260; Cardiolipin biosynthesis.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q8H8U0; baseline and differential.
DR   Genevisible; Q8H8U0; OS.
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:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0043337; F:CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase activity; IEA:RHEA.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   TIGRFAMs; TIGR00560; pgsA; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..329
FT                   /note="Cardiolipin synthase (CMP-forming), mitochondrial"
FT                   /id="PRO_0000429139"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          27..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  34364 MW;  A6DA4DDFD45F3BFC CRC64;
     MPPSVATHAS LLLKAAAAAA HLHPKPFFSP RAAPPRIPSA PAPPAAGGSR YRPTTTTTAA
     ATATSATAAC RWFRWPPPAQ APVRGLCSLP HSGGGGGGGE GMGSEGVGRR RRVVAPAVNG
     VAKDGAPQPP PPKLLTLPTV LTIGRVAAVP LLISTFYMEG PWAATATTGI FLAAAVTDWL
     DGYIARKMQL GTPFGAFLDP VADKLMVAAT LVLLCTKPLE ISLLRDGPWL LTVPAIAIIG
     REITMSAVRE WAASQNTKVL EAVAVNNLGK WKTATQMTAL TILLASRDKS LPAQDALVTS
     GIALLYVSAG LAIWSLVVYM RKIWRILLK
 
 
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