ID   FAS_RABIT               Reviewed;          64 AA.
AC   P07855;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85;
DE   Flags: Fragment;
GN   Name=FASN;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, AND PHOSPHOPANTETHEINYLATION AT SER-38.
RX   PubMed=6357793; DOI=10.1111/j.1432-1033.1983.tb07769.x;
RA   McCarthy A.D., Aitken A., Hardie D.G.;
RT   "The multifunctional polypeptide chain of rabbit mammary fatty acid
RT   synthase contains a domain homologous with the acyl carrier protein of
RT   Escherichia coli.";
RL   Eur. J. Biochem. 136:501-508(1983).
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   -!- 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; S07221; S07221.
DR   AlphaFoldDB; P07855; -.
DR   SMR; P07855; -.
DR   InParanoid; P07855; -.
DR   Proteomes; UP000001811; Unplaced.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Multifunctional enzyme; NAD; NADP; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           <1..>64
FT                   /note="Fatty acid synthase"
FT                   /id="PRO_0000180278"
FT   DOMAIN          1..64
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         38
FT                   /note="O-(pantetheine 4'-phosphoryl)serine; alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:6357793"
FT   MOD_RES         38
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P12785"
FT   NON_TER         1
FT   NON_TER         64
SQ   SEQUENCE   64 AA;  7037 MW;  7CECE99D8A76B42D CRC64;
     AEGEGQRDLL KAVAHILGIR DLAGINLDSS LADLGLDSLM GVEVRQTLER EHDLVLSMRE
     VRQL