ID   PD2R2_HUMAN             Reviewed;         395 AA.
AC   Q9Y5Y4; O94765; Q4QRI6;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Prostaglandin D2 receptor 2;
DE   AltName: Full=Chemoattractant receptor-homologous molecule expressed on Th2 cells;
DE   AltName: Full=G-protein coupled receptor 44;
DE   AltName: CD_antigen=CD294;
GN   Name=PTGDR2; Synonyms=CRTH2, DL1R, GPR44;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-204.
RX   PubMed=10036181; DOI=10.1006/geno.1998.5655;
RA   Marchese A., Sawzdargo M., Nguyen T., Cheng R., Heng H.H.Q., Nowak T.,
RA   Im D.-S., Lynch K.R., George S.R., O'Dowd B.F.;
RT   "Discovery of three novel orphan G-protein-coupled receptors.";
RL   Genomics 56:12-21(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ALA-204.
RC   TISSUE=Blood;
RX   PubMed=9973380;
RA   Nagata K., Tanaka K., Ogawa K., Kemmotsu K., Imai T., Yoshie O., Abe H.,
RA   Tada K., Nakamura M., Sugamura K., Takano S.;
RT   "Selective expression of a novel surface molecule by human Th2 cells in
RT   vivo.";
RL   J. Immunol. 162:1278-1286(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-204.
RC   TISSUE=Placenta;
RA   Methner A., Schroeder S.;
RT   "Tissue expression and chromosomal organization of a novel G protein-
RT   coupled receptor.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-204.
RC   TISSUE=Placenta;
RA   King M.M., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-204.
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   [7]
RP   FUNCTION AS RECEPTOR FOR PGD2.
RX   PubMed=11535533; DOI=10.1182/blood.v98.6.1942;
RA   Monneret G., Gravel S., Diamond M., Rokach J., Powell W.S.;
RT   "Prostaglandin D2 is a potent chemoattractant for human eosinophils that
RT   acts via a novel DP receptor.";
RL   Blood 98:1942-1948(2001).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=11168006; DOI=10.1046/j.1365-2249.2001.01422.x;
RA   Tsuda H., Michimata T., Sakai M., Nagata K., Nakamura M., Saito S.;
RT   "A novel surface molecule of Th2- and Tc2-type cells, CRTH2 expression on
RT   human peripheral and decidual CD4+ and CD8+ T cells during the early stage
RT   of pregnancy.";
RL   Clin. Exp. Immunol. 123:105-111(2001).
RN   [9]
RP   FUNCTION AS RECEPTOR FOR PGD2, AND TISSUE SPECIFICITY.
RX   PubMed=11208866; DOI=10.1084/jem.193.2.255;
RA   Hirai H., Tanaka K., Yoshie O., Ogawa K., Kenmotsu K., Takamori Y.,
RA   Ichimasa M., Sugamura K., Nakamura M., Takano S., Nagata K.;
RT   "Prostaglandin D2 selectively induces chemotaxis in T helper type 2 cells,
RT   eosinophils, and basophils via seven-transmembrane receptor CRTH2.";
RL   J. Exp. Med. 193:255-261(2001).
RN   [10]
RP   TISSUE SPECIFICITY, AND CHARACTERIZATION.
RX   PubMed=12466225; DOI=10.1038/sj.bjp.0704973;
RA   Sawyer N., Cauchon E., Chateauneuf A., Cruz R.P., Nicholson D.W.,
RA   Metters K.M., O'Neill G.P., Gervais F.G.;
RT   "Molecular pharmacology of the human prostaglandin D2 receptor, CRTH2.";
RL   Br. J. Pharmacol. 137:1163-1172(2002).
RN   [11]
RP   FUNCTION AS PGD2 RECEPTOR, AND FUNCTION IN PI3K SIGNALING.
RX   PubMed=17196174; DOI=10.1016/j.bcp.2006.11.021;
RA   Xue L., Gyles S.L., Barrow A., Pettipher R.;
RT   "Inhibition of PI3K and calcineurin suppresses chemoattractant receptor-
RT   homologous molecule expressed on Th2 cells (CRTH2)-dependent responses of
RT   Th2 lymphocytes to prostaglandin D(2).";
RL   Biochem. Pharmacol. 73:843-853(2007).
RN   [12]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=17207480; DOI=10.1016/j.ejphar.2006.11.058;
RA   Gallant M.A., Slipetz D., Hamelin E., Rochdi M.D., Talbot S.,
RA   de Brum-Fernandes A.J., Parent J.L.;
RT   "Differential regulation of the signaling and trafficking of the two
RT   prostaglandin D2 receptors, prostanoid DP receptor and CRTH2.";
RL   Eur. J. Pharmacol. 557:115-123(2007).
RN   [13]
RP   MUTAGENESIS OF ASP-330; SER-331; GLU-332; LEU-333 AND THR-347, AND
RP   IDENTIFICATION OF A RECYCLING MOTIF.
RX   PubMed=20035740; DOI=10.1016/j.ejphar.2009.12.022;
RA   Roy S.J., Parent A., Gallant M.A., de Brum-Fernandes A.J., Stankova J.,
RA   Parent J.L.;
RT   "Characterization of C-terminal tail determinants involved in CRTH2
RT   receptor trafficking: identification of a recycling motif.";
RL   Eur. J. Pharmacol. 630:10-18(2010).
CC   -!- FUNCTION: Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-
CC       protein. Receptor activation may result in pertussis toxin-sensitive
CC       decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is
CC       also implicated in mediating PTGDR2 effects. PGD2 induced receptor
CC       internalization. CRTH2 internalization can be regulated by diverse
CC       kinases such as, PKC, PKA, GRK2, GPRK5/GRK5 and GRK6. Receptor
CC       activation is responsible, at least in part, in immune regulation and
CC       allergic/inflammation responses. {ECO:0000269|PubMed:11208866,
CC       ECO:0000269|PubMed:11535533, ECO:0000269|PubMed:17196174}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Internalized receptors colocalized with
CC       RAB11A. {ECO:0000269|PubMed:17207480}.
CC   -!- TISSUE SPECIFICITY: Widespread expression. High expression in stomach,
CC       small intestine, heart and thymus. Intermediate expression in colon,
CC       spinal cord and peripheral blood and low expression in brain, skeletal
CC       muscle and spleen. Expressed also on Th2- and Tc2- type cells,
CC       eosinophils and basophils. {ECO:0000269|PubMed:11168006,
CC       ECO:0000269|PubMed:11208866, ECO:0000269|PubMed:12466225,
CC       ECO:0000269|PubMed:9973380}.
CC   -!- DOMAIN: The 330-DSEL-333 motif is involved in the recycling of PTGDR2
CC       to the cell surface after agonist-induced internalization. This motif
CC       seems to be required for GRK2 and GPRK5/GRK5 to promote agonist-induced
CC       internalization. Thr-347 is a major site for PKC-induced
CC       internalization of the receptor.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:17207480}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD21055.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAD21055.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF118265; AAD21055.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB008535; BAA74518.1; -; mRNA.
DR   EMBL; AF144308; AAD34539.1; -; mRNA.
DR   EMBL; AY507142; AAR92484.1; -; mRNA.
DR   EMBL; AP000777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096841; AAH96841.1; -; mRNA.
DR   CCDS; CCDS7994.1; -.
DR   RefSeq; NP_004769.2; NM_004778.2.
DR   PDB; 6D26; X-ray; 2.80 A; A=1-339.
DR   PDB; 6D27; X-ray; 2.74 A; A=1-339.
DR   PDB; 7M8W; X-ray; 2.61 A; A=1-339.
DR   PDBsum; 6D26; -.
DR   PDBsum; 6D27; -.
DR   PDBsum; 7M8W; -.
DR   AlphaFoldDB; Q9Y5Y4; -.
DR   SMR; Q9Y5Y4; -.
DR   BioGRID; 116412; 5.
DR   STRING; 9606.ENSP00000332812; -.
DR   BindingDB; Q9Y5Y4; -.
DR   ChEMBL; CHEMBL5071; -.
DR   DrugBank; DB00770; Alprostadil.
DR   DrugBank; DB12789; Dinoprost.
DR   DrugBank; DB00917; Dinoprostone.
DR   DrugBank; DB01088; Iloprost.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB02056; Prostaglandin D2.
DR   DrugBank; DB13036; Ramatroban.
DR   DrugBank; DB00605; Sulindac.
DR   DrugBank; DB04828; Zomepirac.
DR   DrugCentral; Q9Y5Y4; -.
DR   GuidetoPHARMACOLOGY; 339; -.
DR   SwissLipids; SLP:000001575; -.
DR   GlyCosmos; Q9Y5Y4; 2 sites, No reported glycans.
DR   GlyGen; Q9Y5Y4; 2 sites.
DR   iPTMnet; Q9Y5Y4; -.
DR   PhosphoSitePlus; Q9Y5Y4; -.
DR   BioMuta; PTGDR2; -.
DR   DMDM; 296439334; -.
DR   MassIVE; Q9Y5Y4; -.
DR   PaxDb; 9606-ENSP00000332812; -.
DR   PeptideAtlas; Q9Y5Y4; -.
DR   ProteomicsDB; 86540; -.
DR   Antibodypedia; 2960; 691 antibodies from 39 providers.
DR   DNASU; 11251; -.
DR   Ensembl; ENST00000332539.5; ENSP00000332812.4; ENSG00000183134.5.
DR   GeneID; 11251; -.
DR   KEGG; hsa:11251; -.
DR   MANE-Select; ENST00000332539.5; ENSP00000332812.4; NM_004778.3; NP_004769.2.
DR   UCSC; uc001nqc.3; human.
DR   AGR; HGNC:4502; -.
DR   CTD; 11251; -.
DR   DisGeNET; 11251; -.
DR   GeneCards; PTGDR2; -.
DR   HGNC; HGNC:4502; PTGDR2.
DR   HPA; ENSG00000183134; Tissue enhanced (intestine, skeletal muscle, stomach).
DR   MIM; 604837; gene.
DR   neXtProt; NX_Q9Y5Y4; -.
DR   OpenTargets; ENSG00000183134; -.
DR   PharmGKB; PA28891; -.
DR   VEuPathDB; HostDB:ENSG00000183134; -.
DR   eggNOG; ENOG502QTYS; Eukaryota.
DR   GeneTree; ENSGT00940000162009; -.
DR   HOGENOM; CLU_009579_8_0_1; -.
DR   InParanoid; Q9Y5Y4; -.
DR   OMA; CPDLCRK; -.
DR   OrthoDB; 5311208at2759; -.
DR   PhylomeDB; Q9Y5Y4; -.
DR   TreeFam; TF330976; -.
DR   PathwayCommons; Q9Y5Y4; -.
DR   Reactome; R-HSA-391908; Prostanoid ligand receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q9Y5Y4; -.
DR   BioGRID-ORCS; 11251; 11 hits in 1154 CRISPR screens.
DR   GeneWiki; GPR44; -.
DR   GenomeRNAi; 11251; -.
DR   Pharos; Q9Y5Y4; Tchem.
DR   PRO; PR:Q9Y5Y4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9Y5Y4; Protein.
DR   Bgee; ENSG00000183134; Expressed in mucosa of transverse colon and 82 other cell types or tissues.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR   GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR   GO; GO:0004956; F:prostaglandin D receptor activity; IDA:UniProtKB.
DR   GO; GO:0004958; F:prostaglandin F receptor activity; IEA:Ensembl.
DR   GO; GO:0001785; F:prostaglandin J receptor activity; IEA:Ensembl.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd15118; 7tmA_PD2R2_CRTH2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000826; Formyl_rcpt-rel.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1.
DR   PANTHER; PTHR24225:SF55; PROSTAGLANDIN D2 RECEPTOR 2-LIKE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00526; FMETLEUPHER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q9Y5Y4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Prostaglandin D2 receptor 2"
FT                   /id="PRO_0000069572"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..210
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..247
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..269
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..308
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          333..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           330..333
FT                   /note="Involved in the recycling of CRTH2"
FT   COMPBIAS        338..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XKD3"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2J6"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         204
FT                   /note="V -> A (in dbSNP:rs2467642)"
FT                   /evidence="ECO:0000269|PubMed:10036181,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9973380,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT                   /id="VAR_063131"
FT   MUTAGEN         330
FT                   /note="D->A: 45% increases internalization of PTGDR2."
FT                   /evidence="ECO:0000269|PubMed:20035740"
FT   MUTAGEN         331
FT                   /note="S->A: 45% increases internalization of PTGDR2."
FT                   /evidence="ECO:0000269|PubMed:20035740"
FT   MUTAGEN         332
FT                   /note="E->A: 45% increases internalization of PTGDR2."
FT                   /evidence="ECO:0000269|PubMed:20035740"
FT   MUTAGEN         333
FT                   /note="L->A: 45% increase in internalization of PTGDR2."
FT                   /evidence="ECO:0000269|PubMed:20035740"
FT   MUTAGEN         347
FT                   /note="T->A: Decreases in PKC-induced internalization of
FT                   PTGDR2."
FT                   /evidence="ECO:0000269|PubMed:20035740"
FT   HELIX           12..19
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           33..59
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           65..92
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           102..134
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           145..162
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           164..168
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:6D27"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           195..213
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           216..236
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           245..272
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           278..306
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   HELIX           309..324
FT                   /evidence="ECO:0007829|PDB:7M8W"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:7M8W"
SQ   SEQUENCE   395 AA;  43268 MW;  99A63CBDA418DEC9 CRC64;
     MSANATLKPL CPILEQMSRL QSHSNTSIRY IDHAAVLLHG LASLLGLVEN GVILFVVGCR
     MRQTVVTTWV LHLALSDLLA SASLPFFTYF LAVGHSWELG TTFCKLHSSI FFLNMFASGF
     LLSAISLDRC LQVVRPVWAQ NHRTVAAAHK VCLVLWALAV LNTVPYFVFR DTISRLDGRI
     MCYYNVLLLN PGPDRDATCN SRQVALAVSK FLLAFLVPLA IIASSHAAVS LRLQHRGRRR
     PGRFVRLVAA VVAAFALCWG PYHVFSLLEA RAHANPGLRP LVWRGLPFVT SLAFFNSVAN
     PVLYVLTCPD MLRKLRRSLR TVLESVLVDD SELGGAGSSR RRRTSSTARS ASPLALCSRP
     EEPRGPARLL GWLLGSCAAS PQTGPLNRAL SSTSS
//