ID   S22A5_MOUSE             Reviewed;         557 AA.
AC   Q9Z0E8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Organic cation/carnitine transporter 2;
DE   AltName: Full=High-affinity sodium-dependent carnitine cotransporter;
DE   AltName: Full=Solute carrier family 22 member 5;
GN   Name=Slc22a5 {ECO:0000312|MGI:MGI:1329012};
GN   Synonyms=Octn2 {ECO:0000303|PubMed:10454528,
GN   ECO:0000303|PubMed:9837751};
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 [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=9916797; DOI=10.1038/5030;
RA   Nezu J., Tamai I., Oku A., Ohashi R., Yabuuchi H., Hashimoto N.,
RA   Nikaido H., Sai Y., Koizumi A., Shoji Y., Takada G., Matsuishi T.,
RA   Yashino M., Kato H., Ohura T., Tsujimoto G., Hayakawa J., Shimane M.,
RA   Tsuji A.;
RT   "Primary systemic carnitine deficiency is caused by mutations in a gene
RT   encoding sodium ion-dependent carnitine transporter.";
RL   Nat. Genet. 21:91-94(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT JVS ARG-352.
RC   STRAIN=C3H/HeJ;
RX   PubMed=9837751; DOI=10.1006/bbrc.1998.9708;
RA   Lu K., Nishimori H., Nakamura Y., Shima K., Kuwajima M.;
RT   "A missense mutation of mouse OCTN2, a sodium-dependent carnitine
RT   cotransporter, in the juvenile visceral steatosis mouse.";
RL   Biochem. Biophys. Res. Commun. 252:590-594(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=10454528;
RA   Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H., Chen J.,
RA   Conway S.J., Ganapathy V.;
RT   "Functional characteristics and tissue distribution pattern of organic
RT   cation transporter 2 (OCTN2), an organic cation/carnitine transporter.";
RL   J. Pharmacol. Exp. Ther. 290:1482-1492(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11010964; DOI=10.1074/jbc.m005340200;
RA   Tamai I., Ohashi R., Nezu J., Sai Y., Kobayashi D., Oku A., Shimane M.,
RA   Tsuji A.;
RT   "Molecular and functional characterization of organic cation/carnitine
RT   transporter family in mice.";
RL   J. Biol. Chem. 275:40064-40072(2000).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PDZK1.
RX   PubMed=15523054; DOI=10.1124/mol.104.002212;
RA   Kato Y., Sai Y., Yoshida K., Watanabe C., Hirata T., Tsuji A.;
RT   "PDZK1 directly regulates the function of organic cation/carnitine
RT   transporter OCTN2.";
RL   Mol. Pharmacol. 67:734-743(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Kidney;
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   [9]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY CYTOKINES,
RP   AND TRANSPORTER ACTIVITY.
RX   PubMed=20722056; DOI=10.1002/ibd.21444;
RA   Fujiya M., Inaba Y., Musch M.W., Hu S., Kohgo Y., Chang E.B.;
RT   "Cytokine regulation of OCTN2 expression and activity in small and large
RT   intestine.";
RL   Inflamm. Bowel Dis. 17:907-916(2011).
CC   -!- FUNCTION: Sodium-ion dependent, high affinity carnitine transporter.
CC       Involved in the active cellular uptake of carnitine. Transports one
CC       sodium ion with one molecule of carnitine (PubMed:10454528,
CC       PubMed:20722056). Also transports organic cations such as
CC       tetraethylammonium (TEA) without the involvement of sodium. Also
CC       relative uptake activity ratio of carnitine to TEA is 11.3
CC       (PubMed:10454528). May also contribute to regulate the transport of
CC       organic compounds in testis across the blood-testis-barrier (By
CC       similarity). {ECO:0000250|UniProtKB:O70594,
CC       ECO:0000269|PubMed:10454528, ECO:0000269|PubMed:20722056}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine(out) + Na(+)(out) = (R)-carnitine(in) +
CC         Na(+)(in); Xref=Rhea:RHEA:72091, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10454528,
CC         ECO:0000269|PubMed:20722056};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine betaine(out) + Na(+)(out) = glycine betaine(in) +
CC         Na(+)(in); Xref=Rhea:RHEA:72115, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine(in) + glycine betaine(out) = (R)-carnitine(out)
CC         + glycine betaine(in); Xref=Rhea:RHEA:72119, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:17750; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(out) + O-butanoyl-(R)-carnitine(out) = Na(+)(in) + O-
CC         butanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72123, ChEBI:CHEBI:21949,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(out) + O-acetyl-(R)-carnitine(out) = Na(+)(in) + O-
CC         acetyl-(R)-carnitine(in); Xref=Rhea:RHEA:72099, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:57589; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(out) + O-propanoyl-(R)-carnitine(out) = Na(+)(in) + O-
CC         propanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72103, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:53210; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-carnitine(out) + Na(+)(out) = (S)-carnitine(in) +
CC         Na(+)(in); Xref=Rhea:RHEA:72095, ChEBI:CHEBI:11060,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(out) + O-acyl-(R)-carnitine(out) = Na(+)(in) + O-acyl-
CC         (R)-carnitine(in); Xref=Rhea:RHEA:72107, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:75659; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(out) +
CC         Na(+)(out) = L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(in)
CC         + Na(+)(in); Xref=Rhea:RHEA:72111, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:191852; Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N,N-dimethylglycine(out) + Na(+)(out) = N,N-
CC         dimethylglycine(in) + Na(+)(in); Xref=Rhea:RHEA:76591,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:58251;
CC         Evidence={ECO:0000250|UniProtKB:O76082};
CC   -!- ACTIVITY REGULATION: Inhibited by emetine, quinidine and verapamil. The
CC       IC(50) of emetine is 4.2 uM. Not inhibited by valproic acid. Transport
CC       of (R)-carnitine is stimulated by cholesterol in the plasma membrane.
CC       {ECO:0000250|UniProtKB:O76082}.
CC   -!- SUBUNIT: Interacts with PDZK1. {ECO:0000269|PubMed:15523054}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:20722056}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:15523054}. Basal cell membrane
CC       {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:O76082}. Note=Colocalizes with
CC       PDZK1 on apical membranes of kidney proximal tubules (PubMed:15523054).
CC       In intestinal cells, apical expression is induced by TNF
CC       (PubMed:20722056). {ECO:0000269|PubMed:15523054,
CC       ECO:0000269|PubMed:20722056}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in kidney, liver and
CC       testis (PubMed:11010964). Expressed at the brush border of the small,
CC       large intestine and colon (at protein level) (PubMed:11010964,
CC       PubMed:20722056). {ECO:0000269|PubMed:11010964,
CC       ECO:0000269|PubMed:20722056}.
CC   -!- INDUCTION: Intestinal expression is induced by IFNG.
CC       {ECO:0000269|PubMed:20722056}.
CC   -!- DISEASE: Note=Defects in Slc22a5 are the cause of the juvenile visceral
CC       steatosis (JVS) phenotype. JVS is an autosomal recessive animal model
CC       of systemic carnitine deficiency.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; AB015800; BAA36590.1; -; mRNA.
DR   EMBL; AF111425; AAC99787.1; -; mRNA.
DR   EMBL; AF110417; AAD54060.1; -; mRNA.
DR   EMBL; BC031118; AAH31118.1; -; mRNA.
DR   CCDS; CCDS24687.1; -.
DR   RefSeq; NP_035526.1; NM_011396.3.
DR   AlphaFoldDB; Q9Z0E8; -.
DR   SMR; Q9Z0E8; -.
DR   STRING; 10090.ENSMUSP00000019044; -.
DR   ChEMBL; CHEMBL2073665; -.
DR   GlyConnect; 2733; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q9Z0E8; 3 sites, 2 glycans.
DR   GlyGen; Q9Z0E8; 3 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q9Z0E8; -.
DR   PhosphoSitePlus; Q9Z0E8; -.
DR   jPOST; Q9Z0E8; -.
DR   MaxQB; Q9Z0E8; -.
DR   PaxDb; 10090-ENSMUSP00000019044; -.
DR   ProteomicsDB; 260885; -.
DR   DNASU; 20520; -.
DR   Ensembl; ENSMUST00000019044.8; ENSMUSP00000019044.8; ENSMUSG00000018900.8.
DR   GeneID; 20520; -.
DR   KEGG; mmu:20520; -.
DR   UCSC; uc007ixc.2; mouse.
DR   AGR; MGI:1329012; -.
DR   CTD; 6584; -.
DR   MGI; MGI:1329012; Slc22a5.
DR   VEuPathDB; HostDB:ENSMUSG00000018900; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000154155; -.
DR   HOGENOM; CLU_001265_33_4_1; -.
DR   InParanoid; Q9Z0E8; -.
DR   OMA; WRLVFVW; -.
DR   OrthoDB; 1448128at2759; -.
DR   PhylomeDB; Q9Z0E8; -.
DR   TreeFam; TF315847; -.
DR   Reactome; R-MMU-200425; Carnitine metabolism.
DR   Reactome; R-MMU-549127; Organic cation transport.
DR   BioGRID-ORCS; 20520; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Slc22a5; mouse.
DR   PRO; PR:Q9Z0E8; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9Z0E8; Protein.
DR   Bgee; ENSMUSG00000018900; Expressed in right kidney and 128 other cell types or tissues.
DR   ExpressionAtlas; Q9Z0E8; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0031526; C:brush border membrane; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IC:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:1902270; P:(R)-carnitine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1900749; P:(R)-carnitine transport; IDA:UniProtKB.
DR   GO; GO:0007512; P:adult heart development; IMP:MGI.
DR   GO; GO:0009437; P:carnitine metabolic process; IMP:MGI.
DR   GO; GO:0015879; P:carnitine transport; IDA:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0060731; P:positive regulation of intestinal epithelial structure maintenance; ISO:MGI.
DR   GO; GO:0015697; P:quaternary ammonium group transport; IDA:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0009609; P:response to symbiotic bacterium; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IDA:UniProtKB.
DR   GO; GO:0034341; P:response to type II interferon; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0070715; P:sodium-dependent organic cation transport; ISO:MGI.
DR   GO; GO:0150104; P:transport across blood-brain barrier; IMP:ARUK-UCL.
DR   CDD; cd17376; MFS_SLC22A4_5_OCTN1_2; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004749; Orgcat_transp/SVOP.
DR   InterPro; IPR045915; S22A4/5.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00898; 2A0119; 1.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   PANTHER; PTHR24064:SF283; SOLUTE CARRIER FAMILY 22 MEMBER 5; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   Genevisible; Q9Z0E8; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disease variant; Glycoprotein; Ion transport;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..557
FT                   /note="Organic cation/carnitine transporter 2"
FT                   /id="PRO_0000220501"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..142
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..373
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..406
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..430
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        484..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..557
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         486
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O76082"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         550
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         352
FT                   /note="L -> R (in JVS)"
FT                   /evidence="ECO:0000269|PubMed:9837751"
SQ   SEQUENCE   557 AA;  62780 MW;  6093F0EE9612B204 CRC64;
     MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFNGMSIV FLAGTPEHRC LVPHTVNLSS
     AWRNHSIPLE TKDGRQVPQK CRRYRLATIA NFSELGLEPG RDVDLEQLEQ ESCLDGWEYD
     KDVFLSTIVT EWDLVCKDDW KAPLTTSLFF VGVLMGSFIS GQLSDRFGRK NVLFLTMGMQ
     TGFSFLQVFS VNFEMFTVLF VLVGMGQISN YVAAFVLGTE ILSKSIRIIF ATLGVCIFYA
     FGFMVLPLFA YFIRDWRMLL LALTVPGVLC GALWWFIPES PRWLISQGRI KEAEVIIRKA
     AKINGIVAPS TIFDPSELQD LNSTKPQLHH IYDLIRTRNI RVITIMSIIL WLTISVGYFG
     LSLDTPNLHG DIYVNCFLLA AVEVPAYVLA WLLLQYLPRR YSISAALFLG GSVLLFMQLV
     PSELFYLSTA LVMVGKFGIT SAYSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF
     VYLGAYDRFL PYILMGSLTI LTAILTLFFP ESFGVPLPDT IDQMLRVKGI KQWQIQSQTR
     MQKDGEESPT VLKSTAF
//