FAT1_COCHE
ID FAT1_COCHE Reviewed; 643 AA.
AC O42633;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Very long-chain fatty acid transport protein;
DE EC=6.2.1.- {ECO:0000250|UniProtKB:P38225};
DE AltName: Full=Very-long-chain acyl-CoA synthetase;
DE Short=VLCS;
GN Name=FAT1;
OS Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris
OS maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5016;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 48329 / C2;
RX PubMed=9742699; DOI=10.1111/j.1574-6968.1998.tb13157.x;
RA Oeser B.;
RT "PKC1, encoding a protein kinase C, and FAT1, encoding a fatty acid
RT transporter protein, are neighbors in Cochliobolus heterostrophus.";
RL FEMS Microbiol. Lett. 165:273-280(1998).
CC -!- FUNCTION: Acyl-CoA synthetase required for both the import of long
CC chain fatty acids (LCFAs) (C14-C18) and the activation very long chain
CC fatty acids (VLCFAs) (C20-C26) by esterification of the fatty acids
CC into metabolically active CoA-thioesters for subsequent degradation or
CC incorporation into phospholipids. The transport and fatty acyl-CoA
CC synthetase activities are genetically separable and are thus
CC independent activities. Esterifies VLCFAs in the peroxisome matrix. The
CC VLCFAs are actively transported into peroxisomes by a PXA1-PXA2
CC heterodimeric transporter in the peroxisomal membrane.
CC {ECO:0000250|UniProtKB:P38225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain
CC fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P38225};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P38225}.
CC Cell membrane {ECO:0000250|UniProtKB:P38225}; Multi-pass membrane
CC protein {ECO:0000255}. Peroxisome membrane
CC {ECO:0000250|UniProtKB:P38225}; Multi-pass membrane protein
CC {ECO:0000255}. Peroxisome {ECO:0000250|UniProtKB:P38225}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; Y15839; CAA75802.1; -; Genomic_DNA.
DR PIR; T43052; T43052.
DR AlphaFoldDB; O42633; -.
DR SMR; O42633; -.
DR PRIDE; O42633; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:InterPro.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR030310; FadD17/FadD6-like.
DR PANTHER; PTHR43107:SF15; PTHR43107:SF15; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Ligase; Lipid droplet; Lipid transport;
KW Membrane; Nucleotide-binding; Peroxisome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..643
FT /note="Very long-chain fatty acid transport protein"
FT /id="PRO_0000193180"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38225"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..138
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38225"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38225"
FT INTRAMEM 250..318
FT /evidence="ECO:0000250|UniProtKB:P38225"
FT TOPO_DOM 319..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38225"
FT MOTIF 477..525
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT BINDING 235..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
SQ SEQUENCE 643 AA; 72311 MW; 0CAF3129C0D7B43C CRC64;
MACMHQAQLY NDLEELLTGP SVPIVAGAAG AAALTAYINA KYHIAHDLKT LGGGLTQSSE
AIDFINRRVA QKRVLTHHIF QEQVQKQSNH PFLIFEGKTW SYKEFSEAYT RVANWLIDEL
DVQVGEMVAI DGGNSAEHLM LWLALDAIGA ATSFLNWNLT GAGLIHCIKL CECRFVIADI
DIKANIEPCR GELEETGINI HYYDPSFISS LPNNTPIPDS RTENIELDSV RGLIYTSGTT
GLPKGVFIST GRELRTDWSI SKYLNLKPTD RMYTCMPLYH AAAHSLCTAS VIHGGGTVVL
SRKFSHKKFW PEVVASEANI IQYVGELGRY LLNGPKSPYD RAHKVQMAWG NGMRPDVWEA
FRERFNIPII HELYAATDGL GSMTNRNAGP FTANCIALRG LIWHWKFRNQ EVLVKMDLDT
DEIMRDRNGF AIRCAVNEPG QMLFRLTPET LAGAPSYYNN ETATQSRRIT DVFQKGDLWF
KSGDMLRQDA EGRVYFVDRL GDTFRWKSEN VSTNEVADVM GTFPQIAETN VYGVLVPGND
GRVRSLNCHG RRRDRVDIRF AALAKHARDR LPGYAVPLFL RVTPALEYTG TLKIQKGRLK
QEGIDPDKIS GEDKLYWLPP GSDIYLPFGK MEWQGIVDKR IRL
