PK1L1_HUMAN
ID PK1L1_HUMAN Reviewed; 2849 AA.
AC Q8TDX9; Q6UWK1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Polycystic kidney disease protein 1-like 1;
DE AltName: Full=PC1-like 1 protein;
DE AltName: Full=Polycystin-1L1;
GN Name=PKD1L1; ORFNames=UNQ5785/PRO19563;
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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11863367; DOI=10.1006/geno.2002.6719;
RA Yuasa T., Venugopal B., Weremowicz S., Morton C.C., Guo L., Zhou J.;
RT "The sequence, expression, and chromosomal localization of a novel
RT polycystic kidney disease 1-like gene, PKD1L1, in human.";
RL Genomics 79:376-386(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2247-2573 (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP FUNCTION, INTERACTION WITH PKD2L1, AND SUBCELLULAR LOCATION.
RX PubMed=24336289; DOI=10.1038/nature12832;
RA DeCaen P.G., Delling M., Vien T.N., Clapham D.E.;
RT "Direct recording and molecular identification of the calcium channel of
RT primary cilia.";
RL Nature 504:315-318(2013).
RN [4]
RP INVOLVEMENT IN HTX8, AND VARIANT HTX8 SER-1691.
RX PubMed=27616478; DOI=10.1016/j.ajhg.2016.07.011;
RA Vetrini F., D'Alessandro L.C., Akdemir Z.C., Braxton A., Azamian M.S.,
RA Eldomery M.K., Miller K., Kois C., Sack V., Shur N., Rijhsinghani A.,
RA Chandarana J., Ding Y., Holtzman J., Jhangiani S.N., Muzny D.M.,
RA Gibbs R.A., Eng C.M., Hanchard N.A., Harel T., Rosenfeld J.A.,
RA Belmont J.W., Lupski J.R., Yang Y.;
RT "Bi-allelic mutations in PKD1L1 are associated with laterality defects in
RT humans.";
RL Am. J. Hum. Genet. 99:886-893(2016).
RN [5]
RP VARIANT ILE-906.
RX PubMed=20869035; DOI=10.1016/j.ajhg.2010.08.015;
RA Funari V.A., Krakow D., Nevarez L., Chen Z., Funari T.L., Vatanavicharn N.,
RA Wilcox W.R., Rimoin D.L., Nelson S.F., Cohn D.H.;
RT "BMPER mutation in diaphanospondylodysostosis identified by ancestral
RT autozygosity mapping and targeted high-throughput sequencing.";
RL Am. J. Hum. Genet. 87:532-537(2010).
CC -!- FUNCTION: Component of a ciliary calcium channel that controls calcium
CC concentration within primary cilia without affecting cytoplasmic
CC calcium concentration. Forms a heterodimer with PKD2L1 in primary cilia
CC and forms a calcium-permeant ciliary channel that regulates sonic
CC hedgehog/SHH signaling and GLI2 transcription. Does not constitute the
CC pore-forming subunit. Also involved in left/right axis specification
CC downstream of nodal flow: forms a complex with PKD2 in cilia to
CC facilitate flow detection in left/right patterning.
CC {ECO:0000269|PubMed:24336289}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PKD2 proteins to form a
CC calcium channel. Interacts with PKD2L1; to form ciliary calcium
CC channel. Interacts with PKD2. {ECO:0000269|PubMed:24336289}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:24336289}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24336289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TDX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDX9-2; Sequence=VSP_013215, VSP_013216;
CC -!- TISSUE SPECIFICITY: Detected in testis and in fetal and adult heart.
CC -!- DISEASE: Heterotaxy, visceral, 8, autosomal (HTX8) [MIM:617205]: A form
CC of visceral heterotaxy, a complex disorder due to disruption of the
CC normal left-right asymmetry of the thoracoabdominal organs. Visceral
CC heterotaxy or situs ambiguus results in randomization of the placement
CC of visceral organs, including the heart, lungs, liver, spleen, and
CC stomach. The organs are oriented randomly with respect to the left-
CC right axis and with respect to one another. It can be associated with a
CC variety of congenital defects including cardiac malformations. HTX8
CC inheritance is autosomal recessive. {ECO:0000269|PubMed:27616478}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB061683; BAB85807.1; -; mRNA.
DR EMBL; AY358757; AAQ89117.1; ALT_INIT; mRNA.
DR CCDS; CCDS34633.1; -. [Q8TDX9-1]
DR RefSeq; NP_612152.1; NM_138295.4. [Q8TDX9-1]
DR BioGRID; 127967; 5.
DR IntAct; Q8TDX9; 1.
DR STRING; 9606.ENSP00000289672; -.
DR TCDB; 1.A.5.1.3; the polycystin cation channel (pcc) family.
DR GlyGen; Q8TDX9; 20 sites.
DR iPTMnet; Q8TDX9; -.
DR PhosphoSitePlus; Q8TDX9; -.
DR BioMuta; PKD1L1; -.
DR DMDM; 23821932; -.
DR EPD; Q8TDX9; -.
DR MassIVE; Q8TDX9; -.
DR PaxDb; Q8TDX9; -.
DR PeptideAtlas; Q8TDX9; -.
DR PRIDE; Q8TDX9; -.
DR ProteomicsDB; 74366; -. [Q8TDX9-1]
DR Antibodypedia; 13627; 62 antibodies from 13 providers.
DR DNASU; 168507; -.
DR Ensembl; ENST00000289672.7; ENSP00000289672.2; ENSG00000158683.10. [Q8TDX9-1]
DR GeneID; 168507; -.
DR KEGG; hsa:168507; -.
DR MANE-Select; ENST00000289672.7; ENSP00000289672.2; NM_138295.5; NP_612152.1.
DR UCSC; uc003tny.3; human. [Q8TDX9-1]
DR CTD; 168507; -.
DR DisGeNET; 168507; -.
DR GeneCards; PKD1L1; -.
DR HGNC; HGNC:18053; PKD1L1.
DR HPA; ENSG00000158683; Tissue enhanced (tongue).
DR MalaCards; PKD1L1; -.
DR MIM; 609721; gene.
DR MIM; 617205; phenotype.
DR neXtProt; NX_Q8TDX9; -.
DR OpenTargets; ENSG00000158683; -.
DR Orphanet; 157769; Situs ambiguus.
DR Orphanet; 101063; Situs inversus totalis.
DR PharmGKB; PA38282; -.
DR VEuPathDB; HostDB:ENSG00000158683; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000162104; -.
DR HOGENOM; CLU_000971_0_0_1; -.
DR InParanoid; Q8TDX9; -.
DR OMA; FDQFQFT; -.
DR OrthoDB; 1276906at2759; -.
DR PhylomeDB; Q8TDX9; -.
DR TreeFam; TF316484; -.
DR PathwayCommons; Q8TDX9; -.
DR SignaLink; Q8TDX9; -.
DR BioGRID-ORCS; 168507; 13 hits in 1062 CRISPR screens.
DR ChiTaRS; PKD1L1; human.
DR GenomeRNAi; 168507; -.
DR Pharos; Q8TDX9; Tbio.
DR PRO; PR:Q8TDX9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8TDX9; protein.
DR Bgee; ENSG00000158683; Expressed in apex of heart and 87 other tissues.
DR ExpressionAtlas; Q8TDX9; baseline and differential.
DR Genevisible; Q8TDX9; HS.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0003127; P:detection of nodal flow; ISS:BHF-UCL.
DR GO; GO:0070986; P:left/right axis specification; ISS:BHF-UCL.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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; PF00801; PKD; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR SMART; SM00308; LH2; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49299; SSF49299; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Cell projection; Cilium; Glycoprotein; Heterotaxy;
KW Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2849
FT /note="Polycystic kidney disease protein 1-like 1"
FT /id="PRO_0000164358"
FT TOPO_DOM 1..1748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1749..1769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1770..1956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1957..1977
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1978..1992
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1993..2013
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2014..2135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2136..2156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2157..2174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2175..2195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2196..2281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2282..2302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2303..2522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2523..2543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2544..2562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2563..2583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2584..2616
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2617..2637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2638..2646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2647..2667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2668..2711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2712..2732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2733..2849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 508..590
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 592..673
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 674..1571
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1688..1734
FT /note="GPS"
FT DOMAIN 1796..1913
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 970..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
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 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2563..2573
FT /note="LSVVGVSLTYY -> VASLVSFSFEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013215"
FT VAR_SEQ 2574..2849
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013216"
FT VARIANT 312
FT /note="V -> F (in dbSNP:rs2686817)"
FT /id="VAR_024566"
FT VARIANT 812
FT /note="D -> N (in dbSNP:rs17131915)"
FT /id="VAR_050552"
FT VARIANT 879
FT /note="T -> A (in dbSNP:rs11972142)"
FT /id="VAR_050553"
FT VARIANT 894
FT /note="V -> I (in dbSNP:rs56100904)"
FT /id="VAR_061522"
FT VARIANT 906
FT /note="V -> I (in dbSNP:rs141681038)"
FT /evidence="ECO:0000269|PubMed:20869035"
FT /id="VAR_065825"
FT VARIANT 1053
FT /note="R -> P (in dbSNP:rs10274334)"
FT /id="VAR_024567"
FT VARIANT 1272
FT /note="K -> E (in dbSNP:rs1470859)"
FT /id="VAR_024568"
FT VARIANT 1691
FT /note="C -> S (in HTX8; dbSNP:rs886037834)"
FT /evidence="ECO:0000269|PubMed:27616478"
FT /id="VAR_077879"
FT VARIANT 2057
FT /note="R -> H (in dbSNP:rs17131834)"
FT /id="VAR_061523"
FT VARIANT 2410
FT /note="E -> K (in dbSNP:rs2290386)"
FT /id="VAR_021944"
FT VARIANT 2603
FT /note="L -> F (in dbSNP:rs59848490)"
FT /id="VAR_061524"
FT VARIANT 2685
FT /note="A -> T (in dbSNP:rs13231277)"
FT /id="VAR_050554"
SQ SEQUENCE 2849 AA; 315435 MW; A0E60E88E7DDAA75 CRC64;
MAEEAAQNIS DDQERCLQAA CCLSFGGELS VSTDKSWGLH LCSCSPPGGG LWVEVYANHV
LLMSDGKCGC PWCALNGKAE DRESQSPSSS ASRQKNIWKT TSEAALSVVN EKTQAVVNEK
TQAPLDCDNS ADRIPHKPFI IIARAWSSGG PRFHHRRLCA TGTADSTFSA LLQLQGTTSA
AAPCSLKMEA SCCVLRLLCC AEDVATGLLP GTVTMETPTK VARPTQTSSQ RVPLWPISHF
PTSPRSSHGL PPGIPRTPSF TASQSGSEIL YPPTQHPPVA ILARNSDNFM NPVLNCSLEV
EARAPPNLGF RVHMASGEAL CLMMDFGDSS GVEMRLHNMS EAMAVTAYHQ YSKGIFFHLL
HFQLDMSTYK EAETQNTTLN VYLCQSENSC LEDSDPSNLG YELISAFVTK GVYMLKAVIY
NEFHGTEVEL GPYYVEIGHE AVSAFMNSSS VHEDEVLVFA DSQVNQKSTV VIHHFPSIPS
YNVSFISQTQ VGDSQAWHSM TVWYKMQSVS VYTNGTVFAT DTDITFTAVT KETIPLEFEW
YFGEDPPVRT TSRSIKKRLS IPQWYRVMVK ASNRMSSVVS EPHVIRVQKK IVANRLTSPS
SALVNASVAF ECWINFGTDV AYLWDFGDGT VSLGSSSSSH VYSREGEFTV EVLAFNNVSA
STLRQQLFIV CEPCQPPLVK NMGPGKVQIW RSQPVRLGVT FEAAVFCDIS QGLSYTWNLM
DSEGLPVSLP AAVDTHRQTL ILPSHTLEYG NYTALAKVQI EGSVVYSNYC VGLEVRAQAP
VSVISEGTHL FFSRTTSSPI VLRGTQSFDP DDPGATLRYH WECATAGSPA HPCFDSSTAH
QLDAAAPTVS FEAQWLSDSY DQFLVMLRVS SGGRNSSETR VFLSPYPDSA FRFVHISWVS
FKDTFVNWND ELSLQAMCED CSEIPNLSYS WDLFLVNATE KNRIEVPFCR VVGLLGSLGL
GAISESSQLN LLPTEPGTAD PDATTTPFSR EPSPVTLGQP ATSAPRGTPT EPMTGVYWIP
PAGDSAVLGE APEEGSLDLE PGPQSKGSLM TGRSERSQPT HSPDPHLSDF EAYYSDIQEA
IPSGGRQPAK DTSFPGSGPS LSAEESPGDG DNLVDPSLSA GRAEPVLMID WPKALLGRAV
FQGYSSSGIT EQTVTIKPYS LSSGETYVLQ VSVASKHGLL GKAQLYLTVN PAPRDMACQV
QPHHGLEAHT VFSVFCMSGK PDFHYEFSYQ IGNTSKHTLY HGRDTQYYFV LPAGEHLDNY
KVMVSTEITD GKGSKVQPCT VVVTVLPRYH GNDCLGEDLY NSSLKNLSTL QLMGSYTEIR
NYITVITRIL SRLSKEDKTA SCNQWSRIQD ALISSVCRLA FVDQEEMIGS VLMLRDLVSF
SNKLGFMSAV LILKYTRALL AQGQFSGPFV IDKGVRLELI GLISRVWEVS EQENSKEEVY
RHEEGITVIS DLLLGCLSLN HVSTGQMEFR TLLHYNLQSS VQSLGSVQVH LPGDLAGHSP
AGAETQSPCY ISQLILFKKN PYPGSQAPGQ IGGVVGLNLY TCSSRRPINR QWLRKPVMVE
FGEEDGLDNR RNKTTFVLLR DKVNLHQFTE LSENPQESLQ IEIEFSKPVT RAFPVMLLVR
FSEKPTPSDF LVKQIYFWDE SIVQIYIPAA SQKDASVGYL SLLDADYDRK PPNRYLAKAV
NYTVHFQWIR CLFWDKREWK SERFSPQPGT SPEKVNCSYH RLAAFALLRR KLKASFEVSD
ISKLQSHPEN LLPSIFIMGS VILYGFLVAK SRQVDHHEKK KAGYIFLQEA SLPGHQLYAV
VIDTGFRAPA RLTSKVYIVL CGDNGLSETK ELSCPEKPLF ERNSRHTFIL SAPAQLGLLR
KIRLWHDSRG PSPGWFISHV MVKELHTGQG WFFPAQCWLS AGRHDGRVER ELTCLQGGLG
FRKLFYCKFT EYLEDFHVWL SVYSRPSSSR YLHTPRLTVS FSLLCVYACL TALVAAGGQE
QPHLDVSPTL GSFRVGLLCT LLASPGAQLL SLLFRLSKEA PGSARVEPHS PLRGGAQTEA
PHGPNSWGRI PDAQEPRKQP ASAILSGSGR AQRKAASDNG TACPAPKLQV HGADHSRTSL
MGKSHCCPPH TQAPSSGLEG LMPQWSRALQ PWWSSAVWAI CGTASLACSL GTGFLAYRFG
QEQCVQWLHL LSLSVVCCIF ITQPLMVCLM ALGFAWKRRA DNHFFTESLC EATRDLDSEL
AERSWTRLPF SSSCSIPDCA GEVEKVLAAR QQARHLRWAH PPSKAQLRGT RQRMRRESRT
RAALRDISMD ILMLLLLLCV IYGRFSQDEY SLNQAIRKEF TRNARNCLGG LRNIADWWDW
SLTTLLDGLY PGGTPSARVP GAQPGALGGK CYLIGSSVIR QLKVFPRHLC KPPRPFSALI
EDSIPTCSPE VGGPENPYLI DPENQNVTLN GPGGCGTRED CVLSLGRTRT EAHTALSRLR
ASMWIDRSTR AVSVHFTLYN PPTQLFTSVS LRVEILPTGS LVPSSLVESF SIFRSDSALQ
YHLMLPQLVF LALSLIHLCV QLYRMMDKGV LSYWRKPRNW LELSVVGVSL TYYAVSGHLV
TLAGDVTNQF HRGLCRAFMD LTLMASWNQR ARWLRGILLF LFTLKCVYLP GIQNTMASCS
SMMRHSLPSI FVAGLVGALM LAALSHLHRF LLSMWVLPPG TFTDAFPGLL FHFPRRSQKD
CLLGLSKSDQ RAMACYFGIL LIVSATLCFG MLRGFLMTLP QKRKSFQSKS FVRLKDVTAY
MWEKVLTFLR LETPKLEEAE MVENHNYYLD EFANLLDELL MKINGLSDSL QLPLLEKTSN
NTGEARTEES PLVDISSYQA AEPADIKDF
