ID   FAS_CAPHI               Reviewed;          35 AA.
AC   P08757;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85;
DE   Flags: Fragment;
GN   Name=FASN; Synonyms=FAS;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3922356; DOI=10.1042/bj2270021;
RA   Mikkelsen J., Hoejrup P., Rasmussen M.M., Roepstorff P., Knudsen J.;
RT   "Amino acid sequence around the active-site serine residue in the
RT   acyltransferase domain of goat mammary fatty acid synthetase.";
RL   Biochem. J. 227:21-27(1985).
CC   -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC       fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This
CC       multifunctional protein has 7 catalytic activities as an acyl carrier
CC       protein.
CC   -!- FUNCTION: This fragment is from the acyltransferase domain of the fatty
CC       acid synthetase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC         fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85;
CC   -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion (By
CC       similarity). Interacts with CEACAM1; this interaction is insulin and
CC       phosphorylation-dependent; reduces fatty-acid synthase activity (By
CC       similarity). {ECO:0000250|UniProtKB:P12785,
CC       ECO:0000250|UniProtKB:P49327}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}.
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DR   PIR; S07131; S07131.
DR   AlphaFoldDB; P08757; -.
DR   SMR; P08757; -.
DR   STRING; 9925.ENSCHIP00000019407; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   Proteomes; UP000694566; Unplaced.
DR   Proteomes; UP000694900; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW   Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme; NAD; NADP;
KW   Reference proteome; Transferase.
FT   CHAIN           <1..>35
FT                   /note="Fatty acid synthase"
FT                   /id="PRO_0000180275"
FT   ACT_SITE        12
FT   NON_TER         1
FT   NON_TER         35
SQ   SEQUENCE   35 AA;  3808 MW;  401BEF8B4ABE562D CRC64;
     MGLRPDGIIG HSLGEVARAY YNGRISQEEA ILSAY
//