PKDRE_HUMAN
ID PKDRE_HUMAN Reviewed; 2253 AA.
AC Q9NTG1; B1AJY3; O95850;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Polycystin family receptor for egg jelly {ECO:0000312|HGNC:HGNC:9015};
DE AltName: Full=PKD and REJ homolog;
DE AltName: Full=Polycystic kidney disease and receptor for egg jelly-related protein;
DE Flags: Precursor;
GN Name=PKDREJ;
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].
RC TISSUE=Testis;
RX PubMed=9949214; DOI=10.1093/hmg/8.3.543;
RA Hughes J., Ward C.J., Aspinwall R., Butler R., Harris P.C.;
RT "Identification of a human homologue of the sea urchin receptor for egg
RT jelly: a polycystic kidney disease-like protein.";
RL Hum. Mol. Genet. 8:543-549(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1829-2253.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP REVIEW.
RX PubMed=11698076; DOI=10.1016/s0165-6147(00)01832-0;
RA Stayner C., Zhou J.;
RT "Polycystin channels and kidney disease.";
RL Trends Pharmacol. Sci. 22:543-546(2001).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-669 AND ILE-1875.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May have a central role in fertilization. May generate a
CC Ca(2+) transporting channel directly involved in initiating the
CC acrosome reaction of the sperm.
CC -!- SUBUNIT: May form homomultimers or heteromultimers in combination with
CC an as yet unidentified subunits.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in testis.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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DR EMBL; AF116458; AAD18021.1; -; mRNA.
DR EMBL; AL031034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73411.1; -; Genomic_DNA.
DR EMBL; AL137288; CAB70680.1; -; mRNA.
DR CCDS; CCDS14073.1; -.
DR PIR; T46355; T46355.
DR RefSeq; NP_006062.1; NM_006071.1.
DR AlphaFoldDB; Q9NTG1; -.
DR SMR; Q9NTG1; -.
DR BioGRID; 115625; 5.
DR IntAct; Q9NTG1; 3.
DR STRING; 9606.ENSP00000253255; -.
DR GlyGen; Q9NTG1; 17 sites.
DR iPTMnet; Q9NTG1; -.
DR PhosphoSitePlus; Q9NTG1; -.
DR BioMuta; PKDREJ; -.
DR DMDM; 23396800; -.
DR MassIVE; Q9NTG1; -.
DR PaxDb; Q9NTG1; -.
DR PeptideAtlas; Q9NTG1; -.
DR PRIDE; Q9NTG1; -.
DR ProteomicsDB; 82605; -.
DR Antibodypedia; 28028; 29 antibodies from 13 providers.
DR DNASU; 10343; -.
DR Ensembl; ENST00000253255.7; ENSP00000253255.5; ENSG00000130943.7.
DR GeneID; 10343; -.
DR KEGG; hsa:10343; -.
DR MANE-Select; ENST00000253255.7; ENSP00000253255.5; NM_006071.2; NP_006062.1.
DR UCSC; uc003bhh.4; human.
DR CTD; 10343; -.
DR DisGeNET; 10343; -.
DR GeneCards; PKDREJ; -.
DR HGNC; HGNC:9015; PKDREJ.
DR HPA; ENSG00000130943; Tissue enriched (testis).
DR MIM; 604670; gene.
DR neXtProt; NX_Q9NTG1; -.
DR OpenTargets; ENSG00000130943; -.
DR PharmGKB; PA33347; -.
DR VEuPathDB; HostDB:ENSG00000130943; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000162080; -.
DR HOGENOM; CLU_001765_0_0_1; -.
DR InParanoid; Q9NTG1; -.
DR OMA; GVYVFNF; -.
DR OrthoDB; 1276906at2759; -.
DR PhylomeDB; Q9NTG1; -.
DR TreeFam; TF316484; -.
DR PathwayCommons; Q9NTG1; -.
DR SignaLink; Q9NTG1; -.
DR BioGRID-ORCS; 10343; 6 hits in 1058 CRISPR screens.
DR GenomeRNAi; 10343; -.
DR Pharos; Q9NTG1; Tdark.
DR PRO; PR:Q9NTG1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NTG1; protein.
DR Bgee; ENSG00000130943; Expressed in adult organism and 49 other tissues.
DR Genevisible; Q9NTG1; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007340; P:acrosome reaction; TAS:ProtInc.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR CDD; cd01752; PLAT_polycystin; 1.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR014010; REJ_dom.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2253
FT /note="Polycystin family receptor for egg jelly"
FT /id="PRO_0000024299"
FT TOPO_DOM 20..1184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1185..1205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1206..1389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1390..1410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1411..1427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1428..1448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1449..1576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1577..1597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1598..1607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1608..1628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1629..1708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1709..1729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1730..1966
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1967..1987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1988..1996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1997..2017
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2018..2042
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2043..2063
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2064..2091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2092..2112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2113..2145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2146..2166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2167..2253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 215..913
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1230..1347
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 26
FT /note="V -> A (in dbSNP:rs7293071)"
FT /id="VAR_059550"
FT VARIANT 528
FT /note="R -> Q (in dbSNP:rs6008394)"
FT /id="VAR_050544"
FT VARIANT 669
FT /note="A -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036573"
FT VARIANT 914
FT /note="L -> P (in dbSNP:rs6519993)"
FT /id="VAR_050545"
FT VARIANT 992
FT /note="T -> P (in dbSNP:rs7291444)"
FT /id="VAR_050546"
FT VARIANT 993
FT /note="V -> A (in dbSNP:rs34798212)"
FT /id="VAR_050547"
FT VARIANT 1091
FT /note="N -> S (in dbSNP:rs6008384)"
FT /id="VAR_050548"
FT VARIANT 1147
FT /note="I -> M (in dbSNP:rs36125344)"
FT /id="VAR_034386"
FT VARIANT 1411
FT /note="N -> D (in dbSNP:rs35276226)"
FT /id="VAR_050549"
FT VARIANT 1528
FT /note="I -> M (in dbSNP:rs4823496)"
FT /id="VAR_050550"
FT VARIANT 1729
FT /note="V -> I (in dbSNP:rs9626829)"
FT /id="VAR_050551"
FT VARIANT 1875
FT /note="T -> I (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1203491707)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036574"
SQ SEQUENCE 2253 AA; 255449 MW; 0878D9FE9106AAE4 CRC64;
MRPGPALLLL GVGLSLSVGR LPLPPVPRGA QAAVSGAPGG LLRGAPGLGV RGGRALLSLR
PSAVRAGGAV LSGRGSLCFP HGGTGRRWYC LDLRVLLSAQ RLPWPAAPAL ALVDLQLSAR
GGRLSLTWSV RLPRSPGRLA WAFRLRLLGP GAARPASPAA RVSPRSAAPG PRPQQGFVAR
TECPTDGPAR VMLQAVNSSS HRAVESSVSC QINACVIQRV RINTDQKGAP VRLSMQAEAT
INASVQLDCP AARAIAQYWQ VFSVPAVGQA PDWTQPLDLP QLEIRNSPLF IHIPNNSLQW
GVYVFNFTVS ITTGNPKMPE VKDSDAVYVW IVRSSLQAVM LGDANITANF TEQLILDGST
SSDPDADSPL QGLQFFWYCT TDPRNYGGDR IILGSKEVCH PEQANLKWPW ASGPVLTLLP
ETLKGDHVYF FRMVIRKDSR TAFSDKRVHV LQGPKAIAHI TCIENCERNF IVSDRFSLFL
NCTNCASRDF YKWSILSSSG GEMLFDWMGE TVTGRNGAYL SIKAFAFRHF LEAEFSISLY
LACWSGVTSV FRHSFIINHG PQIGECKINP AKGIALITKF VVQCSNFRDK HVPLTYKIIV
SDLHSVGEIS SVKENTLGTI LYLGPQSTVP PSFLPVGMLA SQYGLKIYAQ VYDSLGAFSQ
VTLHATAQAP TDKNSSKTVL NQLLSFTVGP SSLLSTLIQK KDFLPAGYLL YIVASVLNNM
KTELPLRDDR VNLRKHLIDQ SFLLPVSTLV EIGQVVMTIT KLTQKPSEFT WDAQKRATMR
VWQANQALQE YQQKDKRFRS EQIEIVSTGI LMSLSNILKM TSPHQVVKDP FYVIESLSDT
ILANKVPGNK TTSMRTPNFN MYVKKVEKWG INQLFRNEKH CRNCFYPTLN VSSVPGLSAN
GPISTMFCDF TNDLFPWLND QENTSVEVSG FRMTGVADNG SVLEITPDVA EVYLVRKNLT
FAAFNLTVGP NSEVDGSLKK TTGGFSFQVD STVLREVLVH IVTEVMVLFT VLVYTGSQIT
PTALVATFLV PHDIPPFASQ SALFDPACTV KKARVVCLPV SLLQLIAQHS HSPHCTVSIV
LQAPRFVMKL NDKLVRISIF SVQCLDMYGI QSEWREGYCI LGEKTSWYEV HCICKNVVRA
RRQLGTIGLT GIHLHTHYVM AKVIVIPNPV DLRLNIIKSL HQNPVTLFTV LFIILLYVGL
AFWALYRDEM DQHLRGHVIV LPDNDPYDNL CYLVTIFTGS RWGSGTRANV FVQLRGTVST
SDVHCLSHPH FTTLYRGSIN TFLLTTKSDL GDIHSIRVWH NNEGRSPSWY LSRIKVENLF
SRHIWLFICQ KWLSVDTTLD RTFHVTHPDE RLTRKDFFFI DVSSNLRKNH MWFSIFASVV
AKTFNRLQRL SCCLAMLLSS LLCNIMFFNL NRQEQTESRE RKYMRSMMIG IESVLITIPV
QLLITFLFTC SQRKPQADLK EVSPQKHPLM SEASEHWEEY LRKWHAYETA KVHPREVAKP
ASKGKPRLPK ASPKATSKPK HRHRKAQIKT PETLGPNTNS NNNIEDDQDV HSEQHPSQKD
LQQLKKKPRI VLPWWCVYVA WFLVFATSSI SSFFIVFYGL TYGYDKSIEW LFASFCSFCQ
SVLLVQPSKI ILLSGFRTNK PKYCKNLSWS TKYKYTEIRL DGMRMHPEEM QRIHDQIVRI
RGTRMYQPLT EDEIRIFKRK KRIKRRALLF LSYILTHFIF LALLLILIVL LRHTDCFYYN
QFIRDRFSMD LATVTKLEDI YRWLNSVLLP LLHNDLNPTF LPESSSKILG LPLMRQVRAK
SSEKMCLPAE KFVQNSIRRE IHCHPKYGID PEDTKNYSGF WNEVDKQAID ESTNGFTYKP
QGTQWLYYSY GLLHTYGSGG YALYFFPEQQ RFNSTLRLKE LQESNWLDEK TWAVVLELTT
FNPDINLFCS ISVIFEVSQL GVVNTSISLH SFSLADFDRK ASAEIYLYVA ILIFFLAYVV
DEGCIIMQER ASYVRSVYNL LNFALKCIFT VLIVLFLRKH FLATGIIRFY LSNPEDFIPF
HAVSQVDHIM RIILGFLLFL TILKTLRYSR FFYDVRLAQR AIQAALPGIC HMAFVVSVYF
FVYMAFGYLV FGQHEWNYSN LIHSTQTVFS YCVSAFQNTE FSNNRILGVL FLSSFMLVMI
CVLINLFQAV ILSAYEEMKQ PVYEEPSDEV EAMTYLCRKL RTMFSFLTSQ SKAKDEPEFF
IDMLYGQPEK NSHRYLGLKT RNINGKKMVY LVV
