ID S27A1_BOVIN Reviewed; 646 AA.
AC Q3ZKN0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 31-OCT-2012, entry version 51.
DE RecName: Full=Long-chain fatty acid transport protein 1;
DE Short=FATP-1;
DE Short=Fatty acid transport protein 1;
DE EC=6.2.1.-;
DE AltName: Full=Solute carrier family 27 member 1;
GN Name=SLC27A1; Synonyms=FATP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ordovas L., Zaragoza P., Rodellar C.;
RT "Bovine solute carrier family 27 member 1 (SLC27A1) gene: structural
RT and functional analysis.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in translocation of long-chain fatty acids
CC (LFCA) across the plasma membrane. The LFCA import appears to be
CC hormone-regulated in a tissue-specific manner. In adipocytes, but
CC not myocytes, insulin induces a rapid translocation of FATP1 from
CC intracellular compartments to the plasma membrane, paralleled by
CC increased LFCA uptake. May act directly as a bona fide
CC transporter, or alternatively, in a cytoplasmic or membrane-
CC associated multimeric protein complex to trap and draw fatty acids
CC towards accumulation. Plays a pivotal role in regulating available
CC LFCA substrates from exogenous sources in tissues undergoing high
CC levels of beta-oxidation or triglyceride synthesis. May be
CC involved in regulation of cholesterol metabolism. Has acyl-CoA
CC ligase activity for long-chain and very-long-chain fatty acids (By
CC similarity).
CC -!- SUBUNIT: Self-associates. May function as a homodimer (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Endomembrane system; Single-pass membrane protein. Cytoplasm (By
CC similarity). Note=Plasma membrane and intracellular membranes, at
CC least in adipocytes. Predominantly cytoplasmic in myocytes (By
CC similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
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DR EMBL; AY738459; AAW68434.1; -; mRNA.
DR IPI; IPI00847102; -.
DR UniGene; Bt.45842; -.
DR ProteinModelPortal; Q3ZKN0; -.
DR PRIDE; Q3ZKN0; -.
DR eggNOG; COG0318; -.
DR HOGENOM; HOG000044189; -.
DR HOVERGEN; HBG005642; -.
DR OrthoDB; EOG473PQW; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Lipid transport; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 646 Long-chain fatty acid transport protein
FT 1.
FT /FTId=PRO_0000193200.
FT TOPO_DOM 1 13 Extracellular (Potential).
FT TRANSMEM 14 34 Helical; (Potential).
FT TOPO_DOM 35 646 Cytoplasmic (Potential).
FT NP_BIND 246 257 AMP (By similarity).
FT REGION 191 475 Sufficient for oligomerization (By
FT similarity).
SQ SEQUENCE 646 AA; 71123 MW; 59BA7D8CF6B05684 CRC64;
MRAPGAGSAS VASLVLLWLL GLPWTWSTAA ALGVYVGGGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HQRARHTIPQ IFQAVVQRQP ERLALVDAGS GACWTFAQLD AYSNAVANLF
RRLGFAPGDV VAIFMEGRPE FVGLWLGLAK AGVEAALLNV NLRREPLAFC LGTSGAKALV
FGGELAAAVA EMSGELGKSL VKFCSGDVGP DGVFPDTQLL DPLLKETSTA PLAQPPGKGM
DDRLFYIYTS GTTGLPKAAI IVHSRYYRIA AFGHYSYSMQ AADVLYDCLP LYHSAGNIMG
VGQCLIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLKQPVR EAEGRHRVRL
AVGNGLRPSI WEEFTERFGV RQIGEFYGAT ECNCSIANMD GKVGSRGFNS RILPHVYPIR
LVKVNEDTME LLRDAQGLCI PCQTGEPGLL VGQINQQDPL RRFDGYISES ATSKKIAHSV
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEGVLSR LLGQTDVAVY
GVAVPGVEGK ACMAAIADPH GRLSPNALYE ELQKVLAPYA RPIFLRLLPQ VDTTGTFKIQ
KTRLQHEGFD PRQTSDRLFF LDLKQGHYLP LDQGVYTRIC SGAFAL
//
