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   08-NOV-2023, entry version 141.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 10090-ENSMUSP00000029541; -.
DR   PeptideAtlas; O88561; -.
DR   ProteomicsDB; 256873; -. [O88561-1]
DR   ProteomicsDB; 256874; -. [O88561-2]
DR   DNASU; 26568; -.
DR   GeneID; 26568; -.
DR   KEGG; mmu:26568; -.
DR   AGR; MGI:1347358; -.
DR   CTD; 11000; -.
DR   MGI; MGI:1347358; Slc27a3.
DR   eggNOG; KOG1179; Eukaryota.
DR   InParanoid; O88561; -.
DR   OrthoDB; 1650656at2759; -.
DR   PhylomeDB; O88561; -.
DR   BRENDA; 6.2.1.3; 3474.
DR   BioGRID-ORCS; 26568; 1 hit in 78 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: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   CDD; cd05938; hsFATP2a_ACSVL_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR43107:SF12; SOLUTE CARRIER FAMILY 27 MEMBER 3; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//