S27A3_MOUSE
ID S27A3_MOUSE Reviewed; 667 AA.
AC O88561; Q6PAU1; Q8BK70;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Long-chain fatty acid transport protein 3 {ECO:0000303|PubMed:9671728};
DE Short=FATP-3 {ECO:0000303|PubMed:15469937, ECO:0000303|PubMed:9671728};
DE Short=Fatty acid transport protein 3 {ECO:0000303|PubMed:9671728};
DE AltName: Full=Arachidonate--CoA ligase {ECO:0000303|PubMed:15699031};
DE EC=6.2.1.15 {ECO:0000269|PubMed:15699031};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
DE AltName: Full=Solute carrier family 27 member 3 {ECO:0000312|MGI:MGI:1347358};
DE AltName: Full=Very long-chain acyl-CoA synthetase homolog 3 {ECO:0000303|PubMed:15469937};
DE Short=VLCS-3 {ECO:0000303|PubMed:15469937};
DE EC=6.2.1.- {ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
GN Name=Slc27a3; Synonyms=Acsvl3, Fatp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-667 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-667 (ISOFORM 1).
RX PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
RA Hirsch D., Stahl A., Lodish H.F.;
RT "A family of fatty acid transporters conserved from mycobacterium to man.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND CATALYTIC ACTIVITY.
RX PubMed=15469937; DOI=10.1074/jbc.m410091200;
RA Pei Z., Fraisl P., Berger J., Jia Z., Forss-Petter S., Watkins P.A.;
RT "Mouse very long-chain acyl-CoA synthetase 3/fatty acid transport protein 3
RT catalyzes fatty acid activation but not fatty acid transport in MA-10
RT cells.";
RL J. Biol. Chem. 279:54454-54462(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRANSPORT ACTIVITY.
RX PubMed=15699031; DOI=10.1074/jbc.m409598200;
RA DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
RT "Comparative biochemical studies of the murine fatty acid transport
RT proteins (FATP) expressed in yeast.";
RL J. Biol. Chem. 280:16829-16837(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=23936004; DOI=10.1371/journal.pone.0069392;
RA Pei Z., Fraisl P., Shi X., Gabrielson E., Forss-Petter S., Berger J.,
RA Watkins P.A.;
RT "Very long-chain acyl-CoA synthetase 3: overexpression and growth
RT dependence in lung cancer.";
RL PLoS ONE 8:E69392-E69392(2013).
CC -!- FUNCTION: Mainly functions as an acyl-CoA ligase catalyzing the ATP-
CC dependent formation of fatty acyl-CoA using LCFA and very-long-chain
CC fatty acids (VLCFA) as substrates (PubMed:15469937, PubMed:15699031).
CC Can mediate the levels of long-chain fatty acids (LCFA) in the cell by
CC facilitating their transport across membranes (PubMed:15699031).
CC {ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15469937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:15469937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5K4L6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:Q5K4L6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5K4L6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000250|UniProtKB:Q5K4L6};
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:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:15469937}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88561-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88561-2; Sequence=VSP_016219, VSP_016220;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in adrenal gland, testis
CC and ovary. Expressed at lower levels in adult brain. Found in adrenal
CC cortical cells, spermatocytes and interstitial cells of the testis,
CC theca cells of the ovary, cerebral cortical neurons, and cerebellar
CC Purkinje cells (at protein level). {ECO:0000269|PubMed:15469937,
CC ECO:0000269|PubMed:23936004}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in embryonic brain
CC (embryonic days 12-14) than in newborn or adult.
CC {ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:23936004}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60052.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36120.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC060052; AAH60052.1; ALT_INIT; mRNA.
DR EMBL; AK076014; BAC36120.1; ALT_INIT; mRNA.
DR EMBL; AF072758; AAC40187.1; -; mRNA.
DR CCDS; CCDS17527.1; -. [O88561-1]
DR RefSeq; NP_001303617.1; NM_001316688.1.
DR RefSeq; NP_036118.2; NM_011988.3.
DR AlphaFoldDB; O88561; -.
DR SMR; O88561; -.
DR BioGRID; 205024; 2.
DR STRING; 10090.ENSMUSP00000029541; -.
DR SwissLipids; SLP:000001142; -.
DR iPTMnet; O88561; -.
DR PhosphoSitePlus; O88561; -.
DR MaxQB; O88561; -.
DR PaxDb; O88561; -.
DR PeptideAtlas; O88561; -.
DR PRIDE; O88561; -.
DR ProteomicsDB; 256873; -. [O88561-1]
DR ProteomicsDB; 256874; -. [O88561-2]
DR DNASU; 26568; -.
DR GeneID; 26568; -.
DR KEGG; mmu:26568; -.
DR CTD; 11000; -.
DR MGI; MGI:1347358; Slc27a3.
DR eggNOG; KOG1179; Eukaryota.
DR InParanoid; O88561; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; O88561; -.
DR BRENDA; 6.2.1.3; 3474.
DR BioGRID-ORCS; 26568; 1 hit in 73 CRISPR screens.
DR PRO; PR:O88561; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88561; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IMP:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IC:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
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; IPR030307; SLC27A3.
DR PANTHER; PTHR43107:SF12; PTHR43107:SF12; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Lipid transport; Membrane; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..667
FT /note="Long-chain fatty acid transport protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000193208"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 114..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT VAR_SEQ 437..528
FT /note="HIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGA
FT PELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRT -> VRDRVDRRTPGAEGG
FT MARAGAPGANDAVWLSLPAHLPLLLDSIRCHDRGAYSECPGALHDHISRFVLGGVQSWQ
FT TRLNLAPEVGAEPRGSGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016219"
FT VAR_SEQ 529..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016220"
FT CONFLICT 302
FT /note="Missing (in Ref. 1; AAH60052)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="C -> F (in Ref. 3; AAC40187)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="I -> F (in Ref. 2; BAC36120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 72965 MW; 0F343D14952075E7 CRC64;
MAALLLLLPL LLLLPLLLKL DVWPQLRWLP ADLAFTVRAL RCKRALRARA LAAAAADPES
SESGCSLAWR LAYLAREQPT HTFLIHGAQR FSYAEAERES NRIARAFLRA RGWTGGRRGS
GRGSTEEGAR VAPPAGDAAA RGTTAPPLAP GATVALLLPA GPDFLWIWFG LAKAGLRTAF
VPTALRRGPL LHCLRSCGAS ALVLATEFLE SLEPDLPALR AMGLHLWATG PETNVAGISN
LLSEAADQVD EPVPGYLSAP QNIMDTCLYI FTSGTTGLPK AARISHLKVL QCQGFYHLCG
VHQEDVIYLA LPLYHMSGSL LGIVGCLGIG ATVVLKPKFS ASQFWDDCQK HRVTVFQYIG
ELCRYLVNQP PSKAECDHKV RLAVGSGLRP DTWERFLRRF GPLQILETYG MTEGNVATFN
YTGRQGAVGR ASWLYKHIFP FSLIRYDVMT GEPIRNAQGH CMTTSPGEPG LLVAPVSQQS
PFLGYAGAPE LAKDKLLKDV FWSGDVFFNT GDLLVCDEQG FLHFHDRTGD TIRWKGENVA
TTEVAEVLET LDFLQEVNIY GVTVPGHEGR AGMAALALRP PQALNLVQLY SHVSENLPPY
ARPRFLRLQE SLATTETFKQ QKVRMANEGF DPSVLSDPLY VLDQDIGAYL PLTPARYSAL
LSGDLRI
