FPR1_HUMAN
ID FPR1_HUMAN Reviewed; 350 AA.
AC P21462; Q14939; Q7Z6A4; Q86U52; Q9NS48;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=fMet-Leu-Phe receptor;
DE Short=fMLP receptor;
DE AltName: Full=N-formyl peptide receptor;
DE Short=FPR;
DE AltName: Full=N-formylpeptide chemoattractant receptor;
GN Name=FPR1;
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 [MRNA], FUNCTION, AND VARIANTS LEU-101 AND ALA-346.
RX PubMed=2161213; DOI=10.1016/0006-291x(90)91143-g;
RA Boulay F., Tardif M., Brouchon L., Vignais P.;
RT "Synthesis and use of a novel N-formyl peptide derivative to isolate a
RT human N-formyl peptide receptor cDNA.";
RL Biochem. Biophys. Res. Commun. 168:1103-1109(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS
RP LEU-101 AND ALA-346.
RX PubMed=2176894; DOI=10.1021/bi00502a016;
RA Boulay F., Tardif M., Brouchon L., Vignais P.;
RT "The human N-formylpeptide receptor. Characterization of two cDNA isolates
RT and evidence for a new subfamily of G-protein-coupled receptors.";
RL Biochemistry 29:11123-11133(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1712023; DOI=10.1016/s0021-9258(18)98935-0;
RA Murphy P.M., McDermott D.;
RT "Functional expression of the human formyl peptide receptor in Xenopus
RT oocytes requires a complementary human factor.";
RL J. Biol. Chem. 266:12560-12567(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-192.
RX PubMed=1612600; DOI=10.1016/0888-7543(92)90265-t;
RA Bao L., Gerard N.P., Eddy R.L. Jr., Shows T.B., Gerard C.;
RT "Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor
RT (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to
RT chromosome 19.";
RL Genomics 13:437-440(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-346.
RA Perez H.D.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8224916; DOI=10.1016/0378-1119(93)90653-k;
RA Murphy P.M., Tiffany H.L., McDermott D., Ahuja S.K.;
RT "Sequence and organization of the human N-formyl peptide receptor-encoding
RT gene.";
RL Gene 133:285-290(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-11 AND LYS-192.
RA Kopatz S.A., 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-5.
RC TISSUE=Bone marrow;
RX PubMed=1445895; DOI=10.1021/bi00161a044;
RA Perez H.D., Holmes R., Kelly E., McClary J., Chou Q., Andrews W.H.;
RT "Cloning of the gene coding for a human receptor for formyl peptides.
RT Characterization of a promoter region and evidence for polymorphic
RT expression.";
RL Biochemistry 31:11595-11599(1992).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-328; THR-329;
RP THR-331; SER-332; THR-334; THR-336; SER-338 AND THR-339.
RX PubMed=10514456; DOI=10.1074/jbc.274.42.29791;
RA Maestes D.C., Potter R.M., Prossnitz E.R.;
RT "Differential phosphorylation paradigms dictate desensitization and
RT internalization of the N-formyl peptide receptor.";
RL J. Biol. Chem. 274:29791-29795(1999).
RN [13]
RP FUNCTION, INTERACTION WITH CHIPS, AND SUBCELLULAR LOCATION.
RX PubMed=15153520; DOI=10.4049/jimmunol.172.11.6994;
RA Postma B., Poppelier M.J.J.G., van Galen J.C., Prossnitz E.R.,
RA van Strijp J.A.G., de Haas C.J.C., van Kessel K.P.M.;
RT "Chemotaxis inhibitory protein of Staphylococcus aureus binds specifically
RT to the C5a and formylated peptide receptor.";
RL J. Immunol. 172:6994-7001(2004).
RN [14]
RP FUNCTION.
RX PubMed=15210802; DOI=10.4049/jimmunol.173.1.428;
RA Sun R., Iribarren P., Zhang N., Zhou Y., Gong W., Cho E.H., Lockett S.,
RA Chertov O., Bednar F., Rogers T.J., Oppenheim J.J., Wang J.M.;
RT "Identification of neutrophil granule protein cathepsin G as a novel
RT chemotactic agonist for the G protein-coupled formyl peptide receptor.";
RL J. Immunol. 173:428-436(2004).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25109685; DOI=10.1038/cmi.2014.61;
RA Wang W., Li T., Wang X., Yuan W., Cheng Y., Zhang H., Xu E., Zhang Y.,
RA Shi S., Ma D., Han W.;
RT "FAM19A4 is a novel cytokine ligand of formyl peptide receptor 1 (FPR1) and
RT is able to promote the migration and phagocytosis of macrophages.";
RL Cell. Mol. Immunol. 12:615-624(2015).
CC -!- FUNCTION: High affinity receptor for N-formyl-methionyl peptides
CC (fMLP), which are powerful neutrophil chemotactic factors
CC (PubMed:2161213, PubMed:2176894, PubMed:10514456, PubMed:15153520).
CC Binding of fMLP to the receptor stimulates intracellular calcium
CC mobilization and superoxide anion release (PubMed:2161213,
CC PubMed:1712023, PubMed:15153520, PubMed:15210802). This response is
CC mediated via a G-protein that activates a phosphatidylinositol-calcium
CC second messenger system (PubMed:1712023, PubMed:10514456). Receptor for
CC TAFA4, mediates its effects on chemoattracting macrophages, promoting
CC phagocytosis and increasing ROS release (PubMed:25109685). Receptor for
CC cathepsin CTSG, leading to increased phagocyte chemotaxis
CC (PubMed:15210802). {ECO:0000269|PubMed:10514456,
CC ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:2161213,
CC ECO:0000269|PubMed:2176894, ECO:0000269|PubMed:25109685,
CC ECO:0000303|PubMed:10514456, ECO:0000303|PubMed:1712023,
CC ECO:0000303|PubMed:2161213, ECO:0000303|PubMed:2176894}.
CC -!- SUBUNIT: Interacts with S.aureus chemotaxis inhibitory protein (CHIPS);
CC the interaction blocks the receptor and may thus inhibit the immune
CC response. {ECO:0000269|PubMed:15153520}.
CC -!- INTERACTION:
CC P21462; P25098: GRK2; NbExp=3; IntAct=EBI-2869495, EBI-3904795;
CC P21462; O15264: MAPK13; NbExp=3; IntAct=EBI-2869495, EBI-2116951;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15153520,
CC ECO:0000269|PubMed:2176894, ECO:0000269|PubMed:25109685,
CC ECO:0000305|PubMed:10514456}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Internalizes in presence of its ligands, fMLP,
CC TAFA4 and CTSG. {ECO:0000269|PubMed:15210802,
CC ECO:0000269|PubMed:25109685}.
CC -!- TISSUE SPECIFICITY: Neutrophils.
CC -!- PTM: Phosphorylated; which is necessary for desensitization.
CC {ECO:0000269|PubMed:10514456}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FPR1ID44328ch19q13.html";
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DR EMBL; M37128; AAA36362.1; -; mRNA.
DR EMBL; M60626; AAA35846.1; -; mRNA.
DR EMBL; M60627; AAA35847.1; -; mRNA.
DR EMBL; L10820; AAA16863.1; -; Genomic_DNA.
DR EMBL; AY301273; AAP58403.1; -; Genomic_DNA.
DR EMBL; BT007429; AAP36097.1; -; mRNA.
DR EMBL; AC018755; AAF87842.1; -; Genomic_DNA.
DR EMBL; BC005315; AAH05315.1; -; mRNA.
DR EMBL; S49810; AAD14906.1; -; mRNA.
DR CCDS; CCDS12839.1; -.
DR PIR; JC2014; A42009.
DR RefSeq; NP_001180235.1; NM_001193306.1.
DR RefSeq; NP_002020.1; NM_002029.3.
DR PDB; 7T6T; EM; 3.20 A; R=1-333.
DR PDB; 7WVU; EM; 3.30 A; R=2-321.
DR PDBsum; 7T6T; -.
DR PDBsum; 7WVU; -.
DR AlphaFoldDB; P21462; -.
DR SMR; P21462; -.
DR BioGRID; 108640; 152.
DR IntAct; P21462; 4.
DR STRING; 9606.ENSP00000471493; -.
DR BindingDB; P21462; -.
DR ChEMBL; CHEMBL3359; -.
DR DrugBank; DB00716; Nedocromil.
DR DrugCentral; P21462; -.
DR GuidetoPHARMACOLOGY; 222; -.
DR GlyGen; P21462; 2 sites.
DR iPTMnet; P21462; -.
DR PhosphoSitePlus; P21462; -.
DR BioMuta; FPR1; -.
DR DMDM; 288558848; -.
DR EPD; P21462; -.
DR jPOST; P21462; -.
DR MassIVE; P21462; -.
DR PaxDb; P21462; -.
DR PeptideAtlas; P21462; -.
DR PRIDE; P21462; -.
DR ProteomicsDB; 53872; -.
DR ABCD; P21462; 8 sequenced antibodies.
DR Antibodypedia; 19049; 439 antibodies from 33 providers.
DR DNASU; 2357; -.
DR Ensembl; ENST00000304748.5; ENSP00000302707.3; ENSG00000171051.9.
DR Ensembl; ENST00000595042.5; ENSP00000471493.1; ENSG00000171051.9.
DR GeneID; 2357; -.
DR KEGG; hsa:2357; -.
DR MANE-Select; ENST00000304748.5; ENSP00000302707.3; NM_002029.4; NP_002020.1.
DR UCSC; uc002pxq.4; human.
DR CTD; 2357; -.
DR DisGeNET; 2357; -.
DR GeneCards; FPR1; -.
DR HGNC; HGNC:3826; FPR1.
DR HPA; ENSG00000171051; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; FPR1; -.
DR MIM; 136537; gene.
DR neXtProt; NX_P21462; -.
DR OpenTargets; ENSG00000171051; -.
DR Orphanet; 447740; Susceptibility to localized juvenile periodontitis.
DR PharmGKB; PA28244; -.
DR VEuPathDB; HostDB:ENSG00000171051; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR InParanoid; P21462; -.
DR OMA; GWFMCKF; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P21462; -.
DR TreeFam; TF330976; -.
DR BRENDA; 3.1.4.4; 2681.
DR PathwayCommons; P21462; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P21462; -.
DR SIGNOR; P21462; -.
DR BioGRID-ORCS; 2357; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; FPR1; human.
DR GeneWiki; Formyl_peptide_receptor_1; -.
DR GenomeRNAi; 2357; -.
DR Pharos; P21462; Tchem.
DR PRO; PR:P21462; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P21462; protein.
DR Bgee; ENSG00000171051; Expressed in blood and 142 other tissues.
DR ExpressionAtlas; P21462; baseline and differential.
DR Genevisible; P21462; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
DR GO; GO:0004982; F:N-formyl peptide receptor activity; IDA:MGI.
DR GO; GO:0050786; F:RAGE receptor binding; IEA:Ensembl.
DR GO; GO:0005124; F:scavenger receptor binding; IEA:Ensembl.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:ProtInc.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR027345; Formyl_pep_1/2_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF15; PTHR24225:SF15; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..350
FT /note="fMet-Leu-Phe receptor"
FT /id="PRO_0000069444"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 11
FT /note="I -> T (in dbSNP:rs5030878)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_055915"
FT VARIANT 101
FT /note="V -> L (in dbSNP:rs2070745)"
FT /evidence="ECO:0000269|PubMed:2161213,
FT ECO:0000269|PubMed:2176894"
FT /id="VAR_003476"
FT VARIANT 190
FT /note="R -> W (in dbSNP:rs5030880)"
FT /id="VAR_055916"
FT VARIANT 192
FT /note="N -> K (in dbSNP:rs1042229)"
FT /evidence="ECO:0000269|PubMed:1612600, ECO:0000269|Ref.7"
FT /id="VAR_003477"
FT VARIANT 346
FT /note="E -> A (in dbSNP:rs867228)"
FT /evidence="ECO:0000269|PubMed:2161213,
FT ECO:0000269|PubMed:2176894, ECO:0000269|Ref.5"
FT /id="VAR_003478"
FT CONFLICT 238
FT /note="R -> P (in Ref. 1; AAA36362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38446 MW; 06651DF820B1CBD1 CRC64;
METNSSLPTN ISGGTPAVSA GYLFLDIITY LVFAVTFVLG VLGNGLVIWV AGFRMTHTVT
TISYLNLAVA DFCFTSTLPF FMVRKAMGGH WPFGWFLCKF VFTIVDINLF GSVFLIALIA
LDRCVCVLHP VWTQNHRTVS LAKKVIIGPW VMALLLTLPV IIRVTTVPGK TGTVACTFNF
SPWTNDPKER INVAVAMLTV RGIIRFIIGF SAPMSIVAVS YGLIATKIHK QGLIKSSRPL
RVLSFVAAAF FLCWSPYQVV ALIATVRIRE LLQGMYKEIG IAVDVTSALA FFNSCLNPML
YVFMGQDFRE RLIHALPASL ERALTEDSTQ TSDTATNSTL PSAEVELQAK
