PIEZ1_RAT
ID PIEZ1_RAT Reviewed; 2535 AA.
AC Q0KL00;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Piezo-type mechanosensitive ion channel component 1;
DE AltName: Full=Membrane protein induced by beta-amyloid treatment;
DE Short=Mib;
DE AltName: Full=Protein FAM38A;
GN Name=Piezo1; Synonyms=Fam38a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 430-2535, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Astrocyte;
RX PubMed=16854388; DOI=10.1016/j.brainres.2006.06.050;
RA Satoh K., Hata M., Takahara S., Tsuzaki H., Yokota H., Akatsu H.,
RA Yamamoto T., Kosaka K., Yamada T.;
RT "A novel membrane protein, encoded by the gene covering KIAA0233, is
RT transcriptionally induced in senile plaque-associated astrocytes.";
RL Brain Res. 1108:19-27(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-749; SER-1372 AND SER-1633,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pore-forming subunit of a mechanosensitive non-specific
CC cation channel. Generates currents characterized by a linear current-
CC voltage relationship that are sensitive to ruthenium red and
CC gadolinium. Plays a key role in epithelial cell adhesion by maintaining
CC integrin activation through R-Ras recruitment to the ER, most probably
CC in its activated state, and subsequent stimulation of calpain
CC signaling. In the kidney, may contribute to the detection of
CC intraluminal pressure changes and to urine flow sensing. Acts as shear-
CC stress sensor that promotes endothelial cell organization and alignment
CC in the direction of blood flow through calpain activation. Plays a key
CC role in blood vessel formation and vascular structure in both
CC development and adult physiology. Acts as sensor of phosphatidylserine
CC (PS) flipping at the plasma membrane and governs morphogenesis of
CC muscle cells. In myoblasts, flippase-mediated PS enrichment at the
CC inner leaflet of plasma membrane triggers channel activation and Ca2+
CC influx followed by Rho GTPases signal transduction, leading to assembly
CC of cortical actomyosin fibers and myotube formation.
CC {ECO:0000250|UniProtKB:E2JF22}.
CC -!- SUBUNIT: Homotrimer. Interacts with PKD2. Interacts with STOML3.
CC {ECO:0000250|UniProtKB:E2JF22}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16854388}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16854388}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:16854388}. Cell membrane
CC {ECO:0000269|PubMed:16854388}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16854388}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:Q92508}. Cell membrane; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:E2JF22}. Note=In erythrocytes, located
CC in the plasma membrane. Accumulates at the leading apical lamellipodia
CC of endothelial cells in response to shear stress (By similarity).
CC Colocalizes with F-actin and MYH9 at the actomyosin cortex in
CC myoblasts. {ECO:0000250|UniProtKB:E2JF22,
CC ECO:0000250|UniProtKB:Q92508}.
CC -!- TISSUE SPECIFICITY: Moderate expression in lung and kidney. Very weak
CC expression in heart, spleen and liver. {ECO:0000269|PubMed:16854388}.
CC -!- INDUCTION: By APP. {ECO:0000269|PubMed:16854388}.
CC -!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning pressure.
CC -!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family. {ECO:0000305}.
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DR EMBL; AABR03113655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03113740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03114647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB161229; BAF03564.1; -; mRNA.
DR RefSeq; NP_001070668.2; NM_001077200.2.
DR AlphaFoldDB; Q0KL00; -.
DR SMR; Q0KL00; -.
DR STRING; 10116.ENSRNOP00000055134; -.
DR GlyGen; Q0KL00; 2 sites.
DR iPTMnet; Q0KL00; -.
DR PhosphoSitePlus; Q0KL00; -.
DR jPOST; Q0KL00; -.
DR PaxDb; Q0KL00; -.
DR PRIDE; Q0KL00; -.
DR GeneID; 361430; -.
DR KEGG; rno:361430; -.
DR UCSC; RGD:1308822; rat.
DR CTD; 9780; -.
DR RGD; 1308822; Piezo1.
DR eggNOG; KOG1893; Eukaryota.
DR InParanoid; Q0KL00; -.
DR OrthoDB; 13738at2759; -.
DR PhylomeDB; Q0KL00; -.
DR PRO; PR:Q0KL00; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0140135; F:mechanosensitive cation channel activity; ISO:RGD.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; ISO:RGD.
DR GO; GO:0006812; P:cation transport; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0050982; P:detection of mechanical stimulus; ISO:RGD.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISS:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR InterPro; IPR027272; Piezo.
DR InterPro; IPR031805; Piezo_dom.
DR InterPro; IPR031334; Piezo_RRas-bd_dom.
DR PANTHER; PTHR13167; PTHR13167; 4.
DR Pfam; PF15917; PIEZO; 1.
DR Pfam; PF12166; Piezo_RRas_bdg; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..2535
FT /note="Piezo-type mechanosensitive ion channel component 1"
FT /id="PRO_0000305782"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1049
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1146..1166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1198..1218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1223..1243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1687..1707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1721..1741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1966..1986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2007..2027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2036..2056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2065..2085
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2133..2153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2181..2201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2202..2445
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:E2JF22"
FT TRANSMEM 2446..2466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 346..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1325..1356
FT /evidence="ECO:0000255"
FT COMPBIAS 360..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92508"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92508"
FT MOD_RES 1618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E2JF22"
FT MOD_RES 1633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2425..2429
FT /evidence="ECO:0000250|UniProtKB:E2JF22"
SQ SEQUENCE 2535 AA; 290315 MW; 0D02F8B2C2EB65AB CRC64;
MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL
RALLCLSLLF LVAHVAFQIC LHTMPRLNQL LGQNCNLWAN VSQHIGVTRL DLKDIFNTTR
LVAPDLGVLV ASSLCLGLCG RLTRKARQSQ RTQELEEDDI DAAPAAGLQG APTLATKRRL
WLAPRFRITA HWLLVTSGRM LVIVLLALAG IAHPSAFSSV YLMVFLAICT WWSCHFPLSS
LGFNTLCVMV SCFGAGHLVC LYCYQTPFVQ SVLLPGSLWA RLFGLKNFVD IPNCSSPNVL
VLNTKHAWPI YVSPGILLLL YYTATSLLKL RKGRFSELRK EIPREDEEHE LELDQLEPEP
QARGTTQGAT PTTTGPDIDN CTVHVLTSQS PVRQRPVRPR LAELKEMSPL HGLGHLILDQ
SYVCALIAMM VWSIMYHSWL TFVLLLWACL IWTVRSRHQL AMLCSPCILL YGLTLCCLRY
VWAMELPELP TTLGPVSLHQ LGLEHTRYPC LDLGAMLLYL LTFWLLLRQF VKEKLLKKRK
APSTLLEVTV SDTEPTQTQT LLRSLGELVT GIYVKYWIYV CAGMFIVVSF AGRLVVYKIV
YMFLFLLCLT LFQVYYTLWR KLLRVFWWLV VAYTMLVLIA VYTFQFQDFP TYWRNLTGFT
DEQLGDLGLE QFSVSELFSS ILIPGFFLLA CILQLHYFHR PFMQLTDLEH VPPPGTRRLR
WAHRQDTVSE APLLQHQEEE EVFRDDGQSM DGPHQTTQVP EGTASKWGLV ADRLLDLASS
FSAVLTRIQV FVRCLLELHV FKLVALYTVW VALKEVSVMN LLLVVLWAFA LPYPRFRPMA
SCLSTVWTCI IIVCKMLYQL KIVNPHEYSS NCTEPFPNNT NLQPLEISQS LLYRGPVDPA
NWFGVRKGYP NLGYIQNHLQ ILLLLVFEAV VYRRQEHYRR QHQQAPLPAQ ALCADGTRQR
LDQDLLSCLK YFINFFFYKF GLEICFLMAV NVIGQRMNFM VILHGCWLVA ILTRRRREAI
ARLWPNYCLF LTLFLLYQYL LCLGMPPALC IDYPWRWSQA IPMNSALIKW LYLPDFFRAP
NSTNLISDFL LLLCASQQWQ VFSAEQTEEW QRMAGVNTDH LEPLRGEPNP IPNFIHCRSY
LDMLKVAVFR YLFWLVLVVV FVTGATRISI FGLGYLLACF YLLLFGTTLL QKDTRAQLVL
WDCLILYNVT VIISKNMLSL LSCVFVEQMQ SNFCWVIQLF SLVCTVKGYY DPKEMKTRDR
DCLLPVEEAG IIWDSICFFF LLLQRRVFLS HYFLHVSADL KATALQASRG FALYNAANIK
NINFHRQTEE RSLAQLKRQM KRIRAKQEKY RQSQASRGQL QSTDPQEPGP DSPGGSSPPR
TQWWRPWQDH ATVIHSGDYF LFESDSEEEE EALPEDPRPA AQSAFQMAYQ AWVTNAQTVL
RQRREQARRD RAEQLASGGD LSPEVELVDV PENEMAGHSH VMQRVLSTMQ FLWVLGQATV
DGLTRWLRTF TKDHRTMSDV LCAERYLLTQ ELLRGGEVHR GVLDQLYVSE DEIALSGPVE
NRDGPSTASS GLGAEEPLSS MTDDTGSPLS TGYNTRSGSE EIITDTGGLQ AGTSLHGSQE
LLANARTRMR TASELLLDRR LRIPELEEAE QFEAQQGRTL RLLRAMYQCV AAHSELLCYF
IIILNHMVTA SAASLVLPVL VFLWAMLTIP RPSKRFWMTA IVFTEVMVVT KYLFQFGFFP
WNSYIVLRRY ENKPYFPPRI LGLEKTDSYI KYDLVQLMAL FFHRSQLLCY GLWDHEEDGV
PKDHCRSSEK DQEAEEESEA KLESQPETGT GHPEEPVLTG TPKDHIQGKG SVRSKDEIQD
PPEDLKPQHR RHISIRFRRR KETQGPKGAA VVEAEHEEGE EGREAAGRKR LRRPREGLKI
REKMKAAGRR LQSFCLSLAQ SFYQPLRRFF HDILHTKYRA ATDVYALMFL ADIVDIVVII
FGFWAFGKHS AATDIASSLS DDQVPQAFLF MLLVQFGTMV IDRALYLRKT VLGNLAFQVV
LVVAIHLWMF FILPAVTERM FRQNAVAQLW YFVKCIYFAL SAYQIRCGYP TRILGNFLTK
KYNHLNLFLF QGFRLVPFLV ELRAVMDWVW TDTTLSLSNW MCVEDIYANI FIIKCSRETE
KKYPQPKGQK KKKIVKYGMG GLIILFLIAI IWFPLLFMSL IRSVVGVVNQ PIDVTVTLKL
GGYEPLFTMS AQQPSIVPFT PEDYEELSQQ FDPYPLAMQF ISQYSPEDIV TAQIEGSSGA
LWRISPPSRA QMKHELYNGT ADITLRFTWN FQRDLAKGGS VEYTNEKHTL ELAPNSTARR
QLAQLLEGRP DQSVVIPHLF PKYIRAPNGP EANPVKQLQP DEEEDYLGVR IQLRREQVGT
GTSGEQAGTK ASDFLEWWVI ELQDCQAECN LLPMVIFSDK VSPPSLGFLA GYGIVGLYVS
IVLVVGKFVR GFFSDISHSI MFEELPCVDR ILKLCQDIFL VRETRELELE EELYAKLIFL
YRSPETMIKW TREKE
