ACPM_YEAST
ID ACPM_YEAST Reviewed; 125 AA.
AC P32463; D6VX08;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
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=ACP1; OrderedLocusNames=YKL192C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8394042; DOI=10.1002/yea.320090612;
RA Cheret G., Mattheakis L.C., Sor F.;
RT "DNA sequence analysis of the YCN2 region of chromosome XI in Saccharomyces
RT cerevisiae.";
RL Yeast 9:661-667(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- MISCELLANEOUS: Present with 60500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
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; X69765; CAA49419.1; -; Genomic_DNA.
DR EMBL; Z28192; CAA82036.1; -; Genomic_DNA.
DR EMBL; AY558392; AAS56718.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08974.1; -; Genomic_DNA.
DR PIR; S33960; S33960.
DR RefSeq; NP_012729.1; NM_001179758.1.
DR AlphaFoldDB; P32463; -.
DR SMR; P32463; -.
DR BioGRID; 33929; 40.
DR ComplexPortal; CPX-392; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR DIP; DIP-3990N; -.
DR IntAct; P32463; 2.
DR MINT; P32463; -.
DR STRING; 4932.YKL192C; -.
DR MaxQB; P32463; -.
DR PaxDb; P32463; -.
DR PRIDE; P32463; -.
DR EnsemblFungi; YKL192C_mRNA; YKL192C; YKL192C.
DR GeneID; 853642; -.
DR KEGG; sce:YKL192C; -.
DR SGD; S000001675; ACP1.
DR VEuPathDB; FungiDB:YKL192C; -.
DR eggNOG; KOG1748; Eukaryota.
DR GeneTree; ENSGT00390000002127; -.
DR HOGENOM; CLU_108696_0_2_1; -.
DR InParanoid; P32463; -.
DR OMA; NIKPTAH; -.
DR BioCyc; YEAST:G3O-31954-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P32463; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32463; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0099128; C:mitochondrial iron-sulfur cluster assembly complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; ISS:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
DR GO; GO:0009107; P:lipoate biosynthetic process; IMP: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 Electron transport; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide;
KW Transport.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..125
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000000566"
FT DOMAIN 43..122
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 82
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 125 AA; 13943 MW; A0C64C5B796A5DDF CRC64;
MFRSVCRISS RVAPSAYRTI MGRSVMSNTI LAQRFYSANL SKDQVSQRVI DVIKAFDKNS
PNIANKQISS DTQFHKDLGL DSLDTVELLV AIEEEFDIEI PDKVADELRS VGETVDYIAS
NPDAN
