ACPM_NEUCR
ID ACPM_NEUCR Reviewed; 134 AA.
AC P11943; Q7RWC9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Acyl carrier protein, mitochondrial;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE Flags: Precursor;
GN Name=nuo-12; Synonyms=acp, nuo9.6; ORFNames=NCU05008;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 47-71.
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=1832379; DOI=10.1111/j.1432-1033.1991.tb16205.x;
RA Sackmann U., Zensen R., Roehlen D.-A., Jahnke U., Weiss H.;
RT "The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of
RT NADH:ubiquinone reductase (complex I).";
RL Eur. J. Biochem. 200:463-469(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8595652; DOI=10.1007/bf00313188;
RA Schneider R., Massow M., Lisowsky T.U., Weiss H.;
RT "Different respiratory-defective phenotypes of Neurospora crassa and
RT Saccharomyces cerevisiae after inactivation of the gene encoding the
RT mitochondrial acyl carrier protein.";
RL Curr. Genet. 29:10-17(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP PROTEIN SEQUENCE OF 47-105, AND PHOSPHOPANTETHEINYLATION AT SER-91.
RX PubMed=3360014; DOI=10.1111/j.1432-1033.1988.tb14005.x;
RA Brody S., Mikolajczyk S.;
RT "Neurospora mitochondria contain an acyl-carrier protein.";
RL Eur. J. Biochem. 173:353-359(1988).
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. Accessory and non-catalytic subunit of the
CC mitochondrial membrane respiratory chain NADH dehydrogenase (Complex
CC I), which functions in the transfer of electrons from NADH to the
CC respiratory chain (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Complex I is composed of about 30 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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}.
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DR EMBL; X59258; CAA41951.1; -; mRNA.
DR EMBL; X83578; CAA58561.1; -; Genomic_DNA.
DR EMBL; CM002241; EAA26699.1; -; Genomic_DNA.
DR PIR; S17647; S17647.
DR RefSeq; XP_955935.1; XM_950842.3.
DR AlphaFoldDB; P11943; -.
DR SMR; P11943; -.
DR STRING; 5141.EFNCRP00000001470; -.
DR TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblFungi; EAA26699; EAA26699; NCU05008.
DR GeneID; 3872082; -.
DR KEGG; ncr:NCU05008; -.
DR VEuPathDB; FungiDB:NCU05008; -.
DR HOGENOM; CLU_108696_0_0_1; -.
DR InParanoid; P11943; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0099128; C:mitochondrial iron-sulfur cluster assembly complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IDA:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR GO; GO:0009107; P:lipoate biosynthetic process; IDA:SGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1832379,
FT ECO:0000269|PubMed:3360014"
FT CHAIN 47..134
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000000564"
FT DOMAIN 55..131
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 91
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:3360014"
FT CONFLICT 63
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 14457 MW; B7A603F1F410D95A CRC64;
MFRTAALTAA RVARPAVASA VRAGVARPAF VQAVPKVAAF QAVRFYSAGG HLKKDEVFSR
IAQVLSGFDK VNDPKNITET AHFANDLGLD SLDTVEVVMA IEEEFSIEIP DKDADQIHSV
DKAVEYILSQ PDAN
