ID ACPM_SCHPO Reviewed; 112 AA.
AC Q10217;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Putative acyl carrier protein, mitochondrial;
DE Short=ACP;
DE Flags: Precursor;
GN ORFNames=SPAC4H3.09;
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: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis (By similarity). May be involved in the synthesis of very-
CC long-chain fatty acids. {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by acpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was previously considered as a subunit of the NADH
CC dehydrogenase of the mitochondrial respiratory chain complex I. Due to
CC lack of 38 of the other 40 subunits that are present in that complex in
CC mammals, this attribution is unlikely (PubMed:1518044). {ECO:0000305}.
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DR EMBL; CU329670; CAA93348.1; -; Genomic_DNA.
DR PIR; T38889; T38889.
DR RefSeq; NP_594345.1; NM_001019766.2.
DR AlphaFoldDB; Q10217; -.
DR SMR; Q10217; -.
DR BioGRID; 279978; 1.
DR STRING; 284812.Q10217; -.
DR iPTMnet; Q10217; -.
DR MaxQB; Q10217; -.
DR PaxDb; 4896-SPAC4H3-09-1; -.
DR EnsemblFungi; SPAC4H3.09.1; SPAC4H3.09.1:pep; SPAC4H3.09.
DR GeneID; 2543562; -.
DR KEGG; spo:SPAC4H3.09; -.
DR PomBase; SPAC4H3.09; -.
DR VEuPathDB; FungiDB:SPAC4H3.09; -.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_0_3_1; -.
DR InParanoid; Q10217; -.
DR OMA; VNMAVEE; -.
DR PhylomeDB; Q10217; -.
DR Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SPO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q10217; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISO:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:PomBase.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR003231; ACP.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR00517; acyl_carrier; 1.
DR PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR PANTHER; PTHR20863:SF28; ACYL CARRIER PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..112
FT /note="Putative acyl carrier protein, mitochondrial"
FT /id="PRO_0000000565"
FT DOMAIN 33..109
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 69
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 112 AA; 12519 MW; 969C777F3622FE0D CRC64;
MLSRFSSQLR FISAVRPVIP KFQPLRFYSV ARPDAEKRIL KVVSSFDKIQ DPKKVTPTST
FANDLGLDSL DAVEVVMAIE EEFSIQIPDK DADEITSVGD AISYITKNPE AK
//
