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ACPM_SCHPO
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   03-AUG-2022, entry version 146.
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; 4896.SPAC4H3.09.1; -.
DR   iPTMnet; Q10217; -.
DR   MaxQB; Q10217; -.
DR   PaxDb; Q10217; -.
DR   PRIDE; Q10217; -.
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; VEMIMAF; -.
DR   PhylomeDB; Q10217; -.
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; -; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR00517; acyl_carrier; 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
 
 
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