ID F1RFB1_PIG Unreviewed; 4316 AA.
AC F1RFB1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Polycystin 1, transient receptor potential channel interacting {ECO:0000313|Ensembl:ENSSSCP00000008588.2};
GN Name=PKD1 {ECO:0000313|Ensembl:ENSSSCP00000008588.2,
GN ECO:0000313|VGNC:VGNC:91471};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000008588.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000008588.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000008588.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000008588.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the polycystin family.
CC {ECO:0000256|ARBA:ARBA00007200}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR PaxDb; 9823-ENSSSCP00000008588; -.
DR Ensembl; ENSSSCT00000008812.3; ENSSSCP00000008588.2; ENSSSCG00000008041.5.
DR VGNC; VGNC:91471; PKD1.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000158702; -.
DR HOGENOM; CLU_000173_0_0_1; -.
DR TreeFam; TF316484; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000008041; Expressed in subcutaneous adipose tissue and 43 other cell types or tissues.
DR ExpressionAtlas; F1RFB1; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0140494; C:migrasome; IEA:Ensembl.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0002133; C:polycystin complex; IEA:Ensembl.
DR GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0050982; P:detection of mechanical stimulus; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0048806; P:genitalia development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0060428; P:lung epithelium development; IEA:Ensembl.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0072177; P:mesonephric duct development; IEA:Ensembl.
DR GO; GO:0072218; P:metanephric ascending thin limb development; IEA:Ensembl.
DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
DR GO; GO:0072287; P:metanephric distal tubule morphogenesis; IEA:Ensembl.
DR GO; GO:0072237; P:metanephric proximal tubule development; IEA:Ensembl.
DR GO; GO:0160040; P:mitocytosis; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00146; PKD; 13.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR000434; PC1.
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; IPR006228; Polycystin_cat.
DR InterPro; IPR046791; Polycystin_dom.
DR InterPro; IPR014010; REJ_dom.
DR InterPro; IPR002889; WSC_carb-bd.
DR NCBIfam; TIGR00864; PCC; 1.
DR PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR PANTHER; PTHR46730:SF3; POLYCYSTIN-1; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00801; PKD; 14.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR Pfam; PF02010; REJ; 1.
DR Pfam; PF01822; WSC; 1.
DR PRINTS; PR00500; POLYCYSTIN1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00089; PKD; 15.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF49299; PKD domain; 12.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50093; PKD; 12.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
DR PROSITE; PS51212; WSC; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..4316
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003273864"
FT TRANSMEM 3087..3107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3293..3314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3334..3356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3563..3585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3678..3697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3906..3925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3945..3968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3988..4009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 4035..4057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..271
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 299..359
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 415..531
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 969..1025
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1061..1140
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1138..1226
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1249..1304
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1329..1394
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1420..1479
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1497..1561
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1583..1638
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1731..1817
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1843..1901
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 2085..2159
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 2157..2848
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 3130..3245
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 621..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3491..3511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4168..4225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4258..4316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4173..4206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4268..4282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4316 AA; 462740 MW; F53C73637460E067 CRC64;
MPPAAPARLA LALGLGLWLG ALAGVPGRGC GPCAPPCLCG PAPGAACRVN CSGLGLRTLG
PALRIPADAT ALDVSHNLLR ALDVGLLENL SALTELDISN NRISALEEGI FANLFNLSEI
NLSGNPLECD CGLAWLPRWA EERRVRLLRP EAATCAGPGP LAGQPLLSVP LLDGSCGEEY
IACVPDDSSG AVALAAFSAA HEGPPAPEAC SAFCFAAGQD LAALSEQHGC LCGAARPPGA
SSACLRFCSG TRPPPSAACR GPTLLHNVFP ASPGAALLGP RGPLASGQPA AFRVIASLPG
SSTRWDFGDG SPEVAVAGPE ATHRFLLPGR YLVTAVLALG AGSARLHTEV QVQAAPAALE
LVCLASVHSG ETLQLGLRNR GGSGLEAAYS IMALGEEPAR VVHPLCPSDT EIFPGNGRCY
RLVAEKAAWL QAQEQCRAWA GAALAMVDSP AVQHFLVSRV TRSLDVWIGF SAVERAEIGP
APRDEAFSLE SCQNWLPGEP HPATAERCVR LGPAGQCNTD LCSAPHSYVC ELRPGGPVWD
AENFFVGAPS GDLQAPLSPL AQQEALSAPQ EPVEVMVFPG LSPSREAFLT AAEFGTQTLG
RPAQLRLQVY RPLGGADWGP STPPFLAGAL RNSSEPQSRS SENRTEPAPA CTPAGHPCPR
ANVCLPLGAP CHLQACANTS TAGLGLPGVA SALWKEFLFS VPAGPPAQYS VTFHGQDSPL
LPGDLVSLQH DAGPGALLRC PPAPGHPGTQ APYFSTNASA WLARLPAQLE AAPAGLTCAL
RLLAATEQFT PLLGLSPNPG LQQPGRYEVR AMVGNGVSRH NLSCSFNVLS PVAGLRVIYP
PPHDGRLYVP TNGSALVLQV DSGANATAMA RWPGGNVSAP FEATCPIMVA ALVPGCDCEV
NATLFSVLVL PRLNEGEHEV DVVVENGAGR ANLSLQVKAE EPIRGLRATP SPEARVLQGV
LVRYSPAVEA GSDVVFRWTI DDKQSLTFHN VVFNVIYQSA AIFKLSLTAS NHVSNVTVNY
NVTVERMHKM RGLRVSAVPP VLPLNATLAL AAEVLVDSAV EVVFLWTFGD GEQVIGQFKP
PYNESFQVPD PTVAQVLVEH NVTHTYTDPG EYNLTLLVSN AFENLTQQVP VSVRAALPIV
AVAMGSRVLV AGWPVTFFPH PLPLPGGVLY TWDFGDGSPA VTQPQPEVNH TFASRGVYPI
LLQVNNTVSS VVAGVSVRVF EELRGLTVSL SPAVEQGAPV VVRAILDGGD NVTWTFDMGD
GTVLSGPEAM VEHVYLRAQN CTVTVGASSP AGHLAQSLPV QVFVLEVLWI DPTACIPPQP
HARLTAHVTG DPAHYTFDWT FGDGSSNTTV RGDPTVTHNF TRSGTFPLAL VLSSRVNKAH
YFRSVCVEPE VGNVTLWPER QFVRLGDEAR LVAHAWPLFP YHYAWDFGTE DITACVGGPE
ATFTYRAPGP HLVTVAVSNN ISSANDSALV EVQEPVDLTG IEVNGSHVLE LGQPYLFSVV
GRGHPAAYLW ELGDGGRLEG PAVTHAYDST GSFAVRVAGW NDVSRGEARL NVTVQRRVRG
LSVNASRTVV PLNGSVSFGT WLEAGSDVHY SWVLCDRCTP IPGGPTISYT FRSVGTFNII
VTAENEVGAA QDSIFVYVLQ HIEGLQVVGG GGSCCFPTNH TLQLQAMVRD GTNISYSWTA
QRDGGTALAG SGKTFSLTVL EAGTYLVQLR ATNMLGSTSA NRTVEFLEPV GWLAAAASPN
PAAVHTSVAL RAELAGGSSI TYSWSPEEGL SWETLEPSTT YTFSTPGLHL VTVTAKNQLG
SANATVEVAV QVPVSGLSIR VGELDRSFVA TGSSVPLWGH LASGTEVSWC WTVPGGSRHG
QHVAVVFPDA GTFSIQLNAS NAVSWVVATH NLTAEEPVVG LVLWSSRKVV EPGQLVHFQI
LLATGSVVSL HLQVSGAGPE ALPGPHFSRS FPQVGDYTVS VQAENHVSRA QAQVRVSVLE
AVGGLQVPDC CEPAFATGAE RNFTARVQRG SRVAYAWYFS LQKVQGDSLV ILSGRDVTYT
PVAAGLLEIH VRAFNELGGM NRTLVVEVQD VIQHVALRGD RCFTNRSARF EAVTSPSPRR
VAYRWDFGDG ALVEDTDVPW AAHSYLQPGD YRVEVNASNL VSFFVAQATV TVHVLACREP
EVDVALPPQV LMRRSQRNYL EAHVDLRNCV SYQTEYRWEV YRTASCQRPS RPARLTLPGV
DVSRPQLVVP RLALPVGHYC FVFVVSFGDT PLAQSVQANV TVAPERLVPI VEGGSYRVWS
DTQDLVLDGS KSYDPNLEDG DQTPLNFHWA CVASTQGEAG GCVLNFGPRG SSVVTIPRER
LRAGVEYTFN LTVWKAGRRE EATSQTVLIR RGRVPIVSLE CVSCKAQAVY AVSRSSYVYL
EGRCDSCSGG STRGRWAART FSNETLVLDE TTTSTGNAGM RLVVRRGVLR DGEGYIFTLT
VLGRAGEEQG CASIRLSPNR PPLGGSCRLF PLEAVRALTT KVHFECGGWQ DAEDAGAPLL
YALLLRRCRR GHCEEFCVYK GSLSTYGAVL PPGFAPHFTV GLAVVVQDQL GAAVVALNRS
LAITLPEPPG DPPGRPPDLT AWLYGLTETM LPGLLRQADP QHVIEYSLAL ITVLNEHEQA
LAVAVEPEPR WQLRAQIRKN ITETLVSLRV HTVDDIQQVA AALAQCTVSS RELVCHSCLK
ETLHKLEGMM RILQAETAAG TGTPTAIADS ILNITGDLIH LASSDVQGPQ PSELGAEPPA
LMVASRAYHL SSALMGILTR SRVLNEEPLT LAGEEIVAQG KRSDPLSLLC QGNASGPGCH
FSIPAAFSGA LSNLSDVVQL ILLVDSNPFP VGYISNYTVS TKVASMAFQT QAGAQIPIGQ
LASERAITVK VPNNPEQAAQ VRSIPAGSAV IQPRASVSVV VTPESSNPEA GLHLQLMYSV
MNDYYLPEEP EPYLAVYLHS APWPNEHNCS ASRRISREAL EGEDHRAYTF FIAPGTRDLG
GSYYLNLTSH FRWSALEVSV GLYTSLCQYF SEEERAWRTE GLVPLEETSP SQAVCLTRHL
TAFGASLFVP PSHVHFIFPE PASGGNYIVL LTCTVCLVTY VVMAVILRKL DQLDVSRVRV
IPFCGKGGRF KYEILVKTGW GRGSGTTAHV GIMLYGADSR SGHRHLDGDG AFHRNSLDIF
QIATPHSLGS VWKIRVWHDN KGLSPAWFLQ HVIVRDLQSA HSTFFLVNDW LSVETEANGG
LVEKEVLAAS DAALRRFRRL LVAELQRGFF DKHVWLSMWD RPPRSRFTRV QRATCCALLL
CLFLGANAVW YGVVGDAAYG MGPVSGLIPL SVDTIAVGLV SSVAVYPVYL AILFLFRMSR
SKVAGGPGPT PAGQPVLDVD SRLDSSTLDS SVLAFPGLRA EAFAGQIHHD LFLEDSKSLV
CEGTLSWPDL LSDTSVAGST LQRLARGQTG CALGPEEDSL SLVSPSSPAK YFSASDEDLI
RQILAEGASS LAPTQDTRGE TDLLSDLSGA PGERTQTLML QSRGTGGLPS PGLTWEQPRS
AKLSRTGLVE GLRKRLLPAW CASLAHGLSL LLVAVAVGVS GWVGASFPPS VSVMWLLSSS
TSFLASFLCW EPLKVLLEAL YFALVAKRLH PDEDDTLVES PAVTPVSERV PRVRPPHGFA
LFLAKEEARK VKRLHGMLRG LLVYMFFLLV TLLANYGDTA CHNHAYRLQN AIKQELDSQA
FLAITRSDEF WPWMSHVLLP YIHGNQSRPE LGPPRLRQVR LQEALCSDLP GPGALTCSAA
SGGFSTSDYG VGWGSVTHNG SKTWAYSAPD LLGVWYWGSC AVYDSGGYVQ ELGPSLEESR
AQLGFLQLHN WIDNRSRAVF VELTRYSPAV GLHAAVTLRL EFPAAGQAVT AVSVRPFALR
RLSAGLSMPL LTSVGLLLFA MYFAVAEVRS WRREGRVRAR RPGTWARWLL VALTAAAALV
RLAQLGAADN QWTRFLRRRP HHFTSFEQVA QLSAVAHGLA ASLLFLLLVK AAQQLRFVRQ
WSIFGKTLCR ALPELVGAAI GLVVLAVAYV QLAFLLVSSC VDSLRSAARA LLVLCPGAGG
PALCPDESWR LSPLLCTGLW ALRLWGALRL GAILLRWRYH ALRGELYRPA WEPQDYEMVE
LFLRRLRLWM GFSKVKEFRH KVRFEGVEPL PSRSSRGSKS SPDVPPPSGG SDASRPSTSS
SQLDGLSGGL GRPGARGEPE PEPEPSRLQA VFEALLAQFD RLNQATEDVY QLERRLQSLR
GRRSREPPAS PAPGPSPGPL PVLPSRLARA SRGTGLATGA SRASLLAKNK IHPSST
//
