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P32463 (ACPM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl carrier protein, mitochondrial
Short name=ACP
Alternative name(s):
NADH-ubiquinone oxidoreductase 9.6 kDa subunit
Gene names
Name:ACP1
Ordered Locus Names:YKL192C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carrier of the growing fatty acid chain in fatty acid biosynthesis By similarity. May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Complex I is composed of about 30 different subunits.

Subcellular location

Mitochondrion.

Post-translational modification

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group By similarity.

Miscellaneous

Present with 60500 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 12589Acyl carrier protein, mitochondrial
PRO_0000000566

Amino acid modifications

Modified residue821O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
P32463 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A0C64C5B796A5DDF

FASTA12513,943
        10         20         30         40         50         60 
MFRSVCRISS RVAPSAYRTI MGRSVMSNTI LAQRFYSANL SKDQVSQRVI DVIKAFDKNS 

        70         80         90        100        110        120 
PNIANKQISS DTQFHKDLGL DSLDTVELLV AIEEEFDIEI PDKVADELRS VGETVDYIAS 


NPDAN

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence analysis of the YCN2 region of chromosome XI in Saccharomyces cerevisiae."
Cheret G., Mattheakis L.C., Sor F.
Yeast 9:661-667(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / GRF88.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X69765 Genomic DNA. Translation: CAA49419.1.
Z28192 Genomic DNA. Translation: CAA82036.1.
AY558392 Genomic DNA. Translation: AAS56718.1.
BK006944 Genomic DNA. Translation: DAA08974.1.
PIRS33960.
RefSeqNP_012729.1. NM_001179758.1.

3D structure databases

ProteinModelPortalP32463.
SMRP32463. Positions 67-118.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3990N.
IntActP32463. 2 interactions.
MINTMINT-494746.
STRING4932.YKL192C.

Proteomic databases

PaxDbP32463.
PeptideAtlasP32463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL192C; YKL192C; YKL192C.
GeneID853642.
KEGGsce:YKL192C.

Organism-specific databases

CYGDYKL192c.
SGDS000001675. ACP1.

Phylogenomic databases

eggNOGCOG0236.
GeneTreeENSGT00390000002127.
HOGENOMHOG000178184.
KOK03955.
OMAWMSSEDA.
OrthoDBEOG4CRQ8W.

Enzyme and pathway databases

UniPathwayUPA00094.

Gene expression databases

GenevestigatorP32463.
GermOnlineYKL192C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
InterProIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. PPantetheine_attach_site.
[Graphical view]
PfamPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47336. ACP_like. 1 hit.
TIGRFAMsTIGR00517. acyl_carrier. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974537.

Entry information

Entry nameACPM_YEAST
AccessionPrimary (citable) accession number: P32463
Secondary accession number(s): D6VX08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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