ID   SO2A1_MOUSE             Reviewed;         643 AA.
AC   Q9EPT5;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Solute carrier organic anion transporter family member 2A1 {ECO:0000305};
DE            Short=SLCO2A1 {ECO:0000303|PubMed:26474801, ECO:0000303|PubMed:27169804, ECO:0000303|PubMed:29046334, ECO:0000303|PubMed:32442363};
DE   AltName: Full=OATP2A1 {ECO:0000303|PubMed:26474801};
DE   AltName: Full=PHOAR2;
DE   AltName: Full=Prostaglandin transporter {ECO:0000303|PubMed:10484490, ECO:0000303|PubMed:18579702};
DE            Short=PGT {ECO:0000303|PubMed:10484490, ECO:0000303|PubMed:18579702};
DE   AltName: Full=Solute carrier family 21 member 2;
DE            Short=SLC21A2;
GN   Name=Slco2a1 {ECO:0000312|MGI:MGI:1346021}; Synonyms=Oatp2a1, Slc21a2;
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] (ISOFORM 1), MUTAGENESIS OF VAL-610 AND ILE-611,
RP   TISSUE SPECIFICITY, FUNCTION, AND TRANSPORTER ACTIVITY.
RC   TISSUE=Lung;
RX   PubMed=10484490; DOI=10.1152/ajpregu.1999.277.3.r734;
RA   Pucci M.L., Bao Y., Chan B., Itoh S., Lu R., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Schuster V.L.;
RT   "Cloning of mouse prostaglandin transporter PGT cDNA: species-specific
RT   substrate affinities.";
RL   Am. J. Physiol. 277:R734-R741(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary cancer;
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   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18579702; DOI=10.1152/ajprenal.00564.2007;
RA   Chi Y., Pucci M.L., Schuster V.L.;
RT   "Dietary salt induces transcription of the prostaglandin transporter gene
RT   in renal collecting ducts.";
RL   Am. J. Physiol. 295:F765-F771(2008).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND TRANSPORTER
RP   ACTIVITY.
RX   PubMed=26474801; DOI=10.1016/j.bcp.2015.10.009;
RA   Shimada H., Nakamura Y., Nakanishi T., Tamai I.;
RT   "OATP2A1/SLCO2A1-mediated prostaglandin E2 loading into intracellular
RT   acidic compartments of macrophages contributes to exocytotic secretion.";
RL   Biochem. Pharmacol. 98:629-638(2015).
RN   [5]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=26692285; DOI=10.1016/j.prostaglandins.2015.12.003;
RA   Gose T., Nakanishi T., Kamo S., Shimada H., Otake K., Tamai I.;
RT   "Prostaglandin transporter (OATP2A1/SLCO2A1) contributes to local
RT   disposition of eicosapentaenoic acid-derived PGE3.";
RL   Prostaglandins Other Lipid Mediat. 122:10-17(2016).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=27169804; DOI=10.1126/scitranslmed.aad2709;
RA   Yerushalmi G.M., Markman S., Yung Y., Maman E., Aviel-Ronen S., Orvieto R.,
RA   Adashi E.Y., Hourvitz A.;
RT   "The prostaglandin transporter (PGT) as a potential mediator of
RT   ovulation.";
RL   Sci. Transl. Med. 8:338ra68-338ra68(2016).
RN   [7]
RP   FUNCTION.
RX   PubMed=29046334; DOI=10.15252/embj.201796685;
RA   Sabirov R.Z., Merzlyak P.G., Okada T., Islam M.R., Uramoto H., Mori T.,
RA   Makino Y., Matsuura H., Xie Y., Okada Y.;
RT   "The organic anion transporter SLCO2A1 constitutes the core component of
RT   the Maxi-Cl channel.";
RL   EMBO J. 36:3309-3324(2017).
RN   [8]
RP   FUNCTION.
RX   PubMed=32442363; DOI=10.33594/000000238;
RA   Islam M.R., Okada T., Merzlyak P.G., Toychiev A.H., Ando-Akatsuka Y.,
RA   Sabirov R.Z., Okada Y.;
RT   "Annexin A2-S100A10 Represents the Regulatory Component of Maxi-Cl Channel
RT   Dependent on Protein Tyrosine Dephosphorylation and Intracellular
RT   Calcium.";
RL   Cell. Physiol. Biochem. 54:538-555(2020).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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).
CC   -!- FUNCTION: Mediates the transport of prostaglandins (PGs, mainly PGE2,
CC       PGE1, PGE3, PGF2alpha, PGD2, PGH2) and thromboxanes (thromboxane B2)
CC       across the cell membrane (PubMed:10484490) (Probable). PGs and
CC       thromboxanes play fundamental roles in diverse functions such as
CC       intraocular pressure, gastric acid secretion, renal salt and water
CC       transport, vascular tone, and fever (By similarity). Plays a role in
CC       the clearance of PGs from the circulation through cellular uptake,
CC       which allows cytoplasmic oxidation and PG signal termination
CC       (PubMed:10484490) (Probable). PG uptake is dependent upon membrane
CC       potential and involves exchange of a monovalent anionic substrate (PGs
CC       exist physiologically as an anionic monovalent form) with a
CC       stoichiometry of 1:1 for divalent anions or of 1:2 for monovalent
CC       anions (By similarity). Uses lactate, generated by glycolysis, as a
CC       counter-substrate to mediate PG influx and efflux. Under nonglycolytic
CC       conditions, metabolites other than lactate might serve as counter-
CC       substrates. Although the mechanism is not clear, this transporter can
CC       function in bidirectional mode (By similarity). When apically expressed
CC       in epithelial cells, it facilitates transcellular transport (also
CC       called vectorial release), extracting PG from the apical medium and
CC       facilitating transport across the cell toward the basolateral side,
CC       whereupon the PG exits the cell by simple diffusion (PubMed:18579702).
CC       In the renal collecting duct, regulates renal Na+ balance by removing
CC       PGE2 from apical medium (PGE2 EP4 receptor is likely localized to the
CC       luminal/apical membrane and stimulates Na+ resorption) and transporting
CC       it toward the basolateral membrane (where PGE2 EP1 and EP3 receptors
CC       inhibit Na+ resorption) (PubMed:18579702). Plays a role in endometrium
CC       during decidualization, increasing uptake of PGs by decidual cells (By
CC       similarity). Involved in critical events for ovulation
CC       (PubMed:27169804). Regulates extracellular PGE2 concentration for
CC       follicular development in the ovaries (PubMed:27169804). When expressed
CC       intracellularly, such as in macrophages, contributes to vesicular
CC       uptake of newly synthesized intracellular PGs, thereby facilitating
CC       exocytotic secretion of PGs without being metabolized
CC       (PubMed:26474801). Essential core component of the major type of large-
CC       conductance anion channel, Maxi-Cl, which plays essential roles in
CC       inorganic anion transport, cell volume regulation and release of ATP
CC       and glutamate not only in physiological processes but also in
CC       pathological processes (PubMed:29046334, PubMed:32442363). May
CC       contribute to regulate the transport of organic compounds in testis
CC       across the blood-testis-barrier (By similarity).
CC       {ECO:0000250|UniProtKB:Q92959, ECO:0000269|PubMed:10484490,
CC       ECO:0000269|PubMed:18579702, ECO:0000269|PubMed:26474801,
CC       ECO:0000269|PubMed:27169804, ECO:0000269|PubMed:29046334,
CC       ECO:0000269|PubMed:32442363, ECO:0000305|PubMed:26692285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:26474801};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin E2(out) = 2 (S)-lactate(out)
CC         + prostaglandin E2(in); Xref=Rhea:RHEA:74383, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:10484490,
CC         ECO:0000305|PubMed:18579702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin E1(out) = 2 (S)-lactate(out)
CC         + prostaglandin E1(in); Xref=Rhea:RHEA:74395, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:57397; Evidence={ECO:0000250|UniProtKB:Q92959};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin F2alpha(out) = 2 (S)-
CC         lactate(out) + prostaglandin F2alpha(in); Xref=Rhea:RHEA:74399,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57404;
CC         Evidence={ECO:0000305|PubMed:10484490};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin D2(out) = 2 (S)-lactate(out)
CC         + prostaglandin D2(in); Xref=Rhea:RHEA:74403, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:57406; Evidence={ECO:0000305|PubMed:10484490};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + thromboxane B2(out) = 2 (S)-lactate(out) +
CC         thromboxane B2(in); Xref=Rhea:RHEA:74407, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:90696; Evidence={ECO:0000250|UniProtKB:Q92959};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin E3(out) = 2 (S)-lactate(out)
CC         + prostaglandin E3(in); Xref=Rhea:RHEA:74351, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:133132; Evidence={ECO:0000305|PubMed:26692285};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (S)-lactate(in) + prostaglandin H2(out) = 2 (S)-lactate(out)
CC         + prostaglandin H2(in); Xref=Rhea:RHEA:74379, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:57405; Evidence={ECO:0000250|UniProtKB:Q00910};
CC   -!- ACTIVITY REGULATION: Higher dietary salt intake stimulates
CC       transcription (PubMed:18579702). Chorionic gonadotropin stimulates
CC       expression in the ovaries (PubMed:27169804).
CC       {ECO:0000269|PubMed:18579702, ECO:0000269|PubMed:27169804}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92959};
CC       Multi-pass membrane protein {ECO:0000255}. Basal cell membrane
CC       {ECO:0000250|UniProtKB:Q92959}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:26474801}. Lysosome
CC       {ECO:0000269|PubMed:26474801}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPT5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPT5-2; Sequence=VSP_006128, VSP_006129;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and liver
CC       (PubMed:10484490). Expressed at lower levels in kidney and skeletal
CC       muscle (PubMed:10484490, PubMed:18579702). Expressed in the ovaries (at
CC       mRNA and protein levels) (PubMed:27169804). Expressed in peritoneal
CC       macrophages (at mRNA and protein levels) (PubMed:26474801).
CC       {ECO:0000269|PubMed:10484490, ECO:0000269|PubMed:18579702,
CC       ECO:0000269|PubMed:26474801, ECO:0000269|PubMed:27169804}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; AF323958; AAG40332.1; -; mRNA.
DR   EMBL; BC035200; AAH35200.1; -; mRNA.
DR   CCDS; CCDS23448.1; -. [Q9EPT5-1]
DR   RefSeq; NP_201571.2; NM_033314.3. [Q9EPT5-1]
DR   AlphaFoldDB; Q9EPT5; -.
DR   SMR; Q9EPT5; -.
DR   STRING; 10090.ENSMUSP00000035148; -.
DR   BindingDB; Q9EPT5; -.
DR   ChEMBL; CHEMBL2073699; -.
DR   GlyCosmos; Q9EPT5; 3 sites, No reported glycans.
DR   GlyGen; Q9EPT5; 3 sites.
DR   iPTMnet; Q9EPT5; -.
DR   PhosphoSitePlus; Q9EPT5; -.
DR   SwissPalm; Q9EPT5; -.
DR   MaxQB; Q9EPT5; -.
DR   PaxDb; 10090-ENSMUSP00000035148; -.
DR   PeptideAtlas; Q9EPT5; -.
DR   ProteomicsDB; 261103; -. [Q9EPT5-1]
DR   ProteomicsDB; 261104; -. [Q9EPT5-2]
DR   Pumba; Q9EPT5; -.
DR   Antibodypedia; 33384; 103 antibodies from 16 providers.
DR   DNASU; 24059; -.
DR   Ensembl; ENSMUST00000035148.13; ENSMUSP00000035148.7; ENSMUSG00000032548.15. [Q9EPT5-1]
DR   Ensembl; ENSMUST00000188664.2; ENSMUSP00000140533.2; ENSMUSG00000032548.15. [Q9EPT5-2]
DR   GeneID; 24059; -.
DR   KEGG; mmu:24059; -.
DR   UCSC; uc009rgd.1; mouse. [Q9EPT5-1]
DR   AGR; MGI:1346021; -.
DR   CTD; 6578; -.
DR   MGI; MGI:1346021; Slco2a1.
DR   VEuPathDB; HostDB:ENSMUSG00000032548; -.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01080000257336; -.
DR   HOGENOM; CLU_008954_4_1_1; -.
DR   InParanoid; Q9EPT5; -.
DR   OMA; MMVLRCV; -.
DR   OrthoDB; 2874223at2759; -.
DR   PhylomeDB; Q9EPT5; -.
DR   TreeFam; TF317540; -.
DR   Reactome; R-MMU-879518; Transport of organic anions.
DR   BioGRID-ORCS; 24059; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Slco2a1; mouse.
DR   PRO; PR:Q9EPT5; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9EPT5; Protein.
DR   Bgee; ENSMUSG00000032548; Expressed in placenta labyrinth and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9EPT5; baseline and differential.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IC:MGI.
DR   GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015732; P:prostaglandin transport; IDA:MGI.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   CDD; cd17461; MFS_SLCO2A_OATP2A; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF14; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 2A1; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q9EPT5; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Lipid transport; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..643
FT                   /note="Solute carrier organic anion transporter family
FT                   member 2A1"
FT                   /id="PRO_0000191059"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..52
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..71
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..196
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..279
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..342
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..386
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..414
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..517
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        518..540
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        541..549
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        550..575
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        576..609
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        610..628
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        629..643
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          437..495
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        477
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        443..473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        449..469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        458..493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   VAR_SEQ         368..414
FT                   /note="GAVNLPAAALGMLFGGILMKRFVFPLQTIPRVAATIMTISIILCAPL -> A
FT                   HQVLYIRSLPPAAGTACAQIPSSTLSAETMESSTSPPAMLAAAAST (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006128"
FT   VAR_SEQ         415..643
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006129"
FT   MUTAGEN         610
FT                   /note="V->M: No effect."
FT                   /evidence="ECO:0000269|PubMed:10484490"
FT   MUTAGEN         611
FT                   /note="I->G: No effect."
FT                   /evidence="ECO:0000269|PubMed:10484490"
FT   CONFLICT        3
FT                   /note="L -> F (in Ref. 1; AAG40332)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   643 AA;  70147 MW;  AC487386F847D9D8 CRC64;
     MGLLPKPGAR QGSGTSSVPA RRCSRSVFNN IKVFVLCHGL LQLCQLLYSA YFKSSLTTIE
     KRFGLSSSSS GLISSLNEIS NAILIIFVSY FGSRVNRPRM IGIGGLLLAA GAFVLTLPHF
     LSEPYQYAST TAGNSSHFQT DLCQKHLPGL LPSKCHSTVP DTQKETSSMW SLMVVAQLLA
     GVGTVPIQPF GISYVDDFAE PTNSPLYISI LFAIAVFGPA FGYLLGSVML RIFVDYGRVD
     TATVNLSPGD PRWIGAWWLG LLISSGFLIV TSLPFFFFPR AMSRGAERSV IAEETMKMEE
     DKSRGSLMDF IKRFPRIFLR LLMNPLFMLV VLSQCTFSSV IAGLSTFLNK FLEKQYDASA
     AYANLLIGAV NLPAAALGML FGGILMKRFV FPLQTIPRVA ATIMTISIIL CAPLFFMGCS
     TPAVAEVYPP STPSSIHPQP PACRRDCLCP DSVFHPVCGD NGVEYLSPCH AGCSSLNVSS
     AASKQPIYLN CSCVTGGSAS AKTGSCPTSC AQLLLPSIFL ISFVALIACV SHNPLYMMVL
     RVVNQDEKSF AIGVQFLLMR LLAWLPSPSL YGLLIDSSCI RWNYLCSGRR GACAYYDNDA
     LRNRYLGLQV IYKVLGTLLL FFISWRVKKN REYSLQENAS GLI
//