CLD1_SCHPO
ID CLD1_SCHPO Reviewed; 428 AA.
AC O14249;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Probable cardiolipin-specific deacylase 1, mitochondrial {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:P53264};
DE Flags: Precursor;
GN ORFNames=SPAC6G10.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Mitochondrial cardiolipin-specific phospholipase which
CC deacylates de novo synthesized cardiolipin (CL). Part of the remodeling
CC process of cardiolipin, which involves deacylation-reacylation of
CC premature cardiolipin. {ECO:0000250|UniProtKB:P53264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cardiolipin + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-
CC [1-acyl-sn-glycero-3-phospho]-glycerol + a fatty acid + H(+);
CC Xref=Rhea:RHEA:32935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000250|UniProtKB:P53264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32936;
CC Evidence={ECO:0000250|UniProtKB:P53264};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P53264}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53264}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53264}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P53264}; Matrix side
CC {ECO:0000250|UniProtKB:P53264}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:P53264}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11289.1; -; Genomic_DNA.
DR PIR; T39053; T39053.
DR RefSeq; NP_594100.1; NM_001019524.2.
DR AlphaFoldDB; O14249; -.
DR STRING; 4896.SPAC6G10.03c.1; -.
DR ESTHER; schpo-ye63; CGI-58_ABHD5_ABHD4.
DR MaxQB; O14249; -.
DR PaxDb; O14249; -.
DR EnsemblFungi; SPAC6G10.03c.1; SPAC6G10.03c.1:pep; SPAC6G10.03c.
DR GeneID; 2542281; -.
DR KEGG; spo:SPAC6G10.03c; -.
DR PomBase; SPAC6G10.03c; -.
DR VEuPathDB; FungiDB:SPAC6G10.03c; -.
DR eggNOG; KOG4409; Eukaryota.
DR HOGENOM; CLU_017361_3_1_1; -.
DR InParanoid; O14249; -.
DR OMA; DWMDPEG; -.
DR PhylomeDB; O14249; -.
DR Reactome; R-SPO-1482839; Acyl chain remodelling of PE.
DR PRO; PR:O14249; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:PomBase.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0007006; P:mitochondrial membrane organization; IC:PomBase.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..428
FT /note="Probable cardiolipin-specific deacylase 1,
FT mitochondrial"
FT /id="PRO_0000116702"
FT DOMAIN 93..217
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 178..182
FT /note="GXSXG lipase motif"
FT /evidence="ECO:0000250|UniProtKB:P53264"
FT MOTIF 398..403
FT /note="HXXXXD acyl transferase motif"
FT /evidence="ECO:0000250|UniProtKB:P53264"
FT MOTIF 398..403
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P53264"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P53264"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P53264"
FT ACT_SITE 398
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P53264"
SQ SEQUENCE 428 AA; 48720 MW; EDB60B76D0F6B4CF CRC64;
MSQVKVAVRS EEAANSYTQT FGMSWRQWRQ ACSEEYAKQC EREVLHTVDF IRENEKDPER
LVEVVDSKIY DNDGLVHEVC VSDKATGKAN KRSIVYMHGY GAGLGFYFRN MDGLTKGVTK
DFNSYFVDWL GMGNSSRPPF DIKGQTASEK VEETERFFTE SLETWRIGHG IEKMILVGHS
MGGYLSAVYA MQYPERVEKL LLVSPVAIPE NPFASNDDAE VYNSVASSAV HAVMDEPPLS
NVTNEVLQTQ EETTGLEPSR PSKPKNPLPR FITFLWEQNV TPFSLLRLSG PLGPKLMSFW
SSRRFSTLPP ETFRALHNYC YSIFRLKGSS EYALGNLLAP GAFARRCIMN RLRMLKCRTI
FMYGDKDWMD DVAGLEATNR LKEMNIEAEH HIISNAGHHC YLDNPEDFNE IVLKEIRMSL
RSFSSISE
