CSC1_ARATH
ID CSC1_ARATH Reviewed; 771 AA.
AC Q5XEZ5; A0A097NUP4; O65460; Q56YV1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Calcium permeable stress-gated cation channel 1 {ECO:0000303|PubMed:24503647};
DE Short=AtCSC1 {ECO:0000303|PubMed:24503647};
DE AltName: Full=Hyperosmolality-gated Ca2+ permeable channel 1.2 {ECO:0000303|PubMed:25162526};
DE Short=AtOSCA1.2 {ECO:0000303|PubMed:25162526};
GN Name=CSC1 {ECO:0000303|PubMed:24503647};
GN Synonyms=OSCA1.2 {ECO:0000303|PubMed:25162526};
GN OrderedLocusNames=At4g22120 {ECO:0000312|Araport:AT4G22120};
GN ORFNames=F1N20.220;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=25162526; DOI=10.1038/nature13593;
RA Yuan F., Yang H., Xue Y., Kong D., Ye R., Li C., Zhang J.,
RA Theprungsirikul L., Shrift T., Krichilsky B., Johnson D.M., Swift G.B.,
RA He Y., Siedow J.N., Pei Z.M.;
RT "OSCA1 mediates osmotic-stress-evoked Ca(2+) increases vital for
RT osmosensing in Arabidopsis.";
RL Nature 514:367-371(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=24503647; DOI=10.1038/cr.2014.14;
RA Hou C., Tian W., Kleist T., He K., Garcia V., Bai F., Hao Y., Luan S.,
RA Li L.;
RT "DUF221 proteins are a family of osmosensitive calcium-permeable cation
RT channels conserved across eukaryotes.";
RL Cell Res. 24:632-635(2014).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS), FUNCTION, ACTIVITY
RP REGULATION, HOMODIMERIZATION, TOPOLOGY, AND MUTAGENESIS OF GLU-531.
RX PubMed=30382939; DOI=10.7554/elife.41845;
RA Jojoa-Cruz S., Saotome K., Murthy S.E., Tsui C.C.A., Sansom M.S.,
RA Patapoutian A., Ward A.B.;
RT "Cryo-EM structure of the mechanically activated ion channel OSCA1.2.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel
CC (PubMed:24503647, PubMed:30382939). Specifically conducts cations
CC including Ca(2+), K(+) and Na(+) in vitro. Inactivation or closure of
CC the channel is calcium-dependent (PubMed:24503647). Mechanosensitive
CC ion channel that converts mechanical stimuli into a flow of ions
CC (PubMed:30382939). {ECO:0000269|PubMed:24503647,
CC ECO:0000269|PubMed:30382939}.
CC -!- ACTIVITY REGULATION: Activated by hyperosmotic shock after mannitol or
CC NaCl treatment (PubMed:24503647). Activated by mechanical pressure
CC (PubMed:30382939). {ECO:0000269|PubMed:24503647,
CC ECO:0000269|PubMed:30382939}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30382939}.
CC -!- INTERACTION:
CC Q5XEZ5; Q5XEZ5: CSC1; NbExp=2; IntAct=EBI-26954901, EBI-26954901;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79167.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ920357; AIU34614.1; -; mRNA.
DR EMBL; AL022140; CAA18115.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161556; CAB79167.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84554.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84555.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84556.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84557.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84558.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84559.1; -; Genomic_DNA.
DR EMBL; BT015821; AAU94384.1; -; mRNA.
DR EMBL; BT020529; AAW50707.1; -; mRNA.
DR EMBL; AK221219; BAD93792.1; -; mRNA.
DR PIR; T49119; T49119.
DR RefSeq; NP_001078425.1; NM_001084956.2.
DR RefSeq; NP_001119027.1; NM_001125555.2.
DR RefSeq; NP_001119028.1; NM_001125556.2.
DR RefSeq; NP_001119029.1; NM_001125557.1.
DR RefSeq; NP_001190796.1; NM_001203867.2.
DR RefSeq; NP_193943.2; NM_118333.5.
DR PDB; 6IJZ; EM; 3.68 A; A/B=1-771.
DR PDB; 6MGV; EM; 3.10 A; A/B=1-771.
DR PDB; 6MGW; EM; 3.50 A; A/B=1-771.
DR PDBsum; 6IJZ; -.
DR PDBsum; 6MGV; -.
DR PDBsum; 6MGW; -.
DR AlphaFoldDB; Q5XEZ5; -.
DR SMR; Q5XEZ5; -.
DR STRING; 3702.AT4G22120.2; -.
DR TCDB; 1.A.17.5.10; the calcium-dependent chloride channel (ca-clc) family.
DR iPTMnet; Q5XEZ5; -.
DR PaxDb; Q5XEZ5; -.
DR PRIDE; Q5XEZ5; -.
DR ProteomicsDB; 222653; -.
DR EnsemblPlants; AT4G22120.1; AT4G22120.1; AT4G22120.
DR EnsemblPlants; AT4G22120.2; AT4G22120.2; AT4G22120.
DR EnsemblPlants; AT4G22120.3; AT4G22120.3; AT4G22120.
DR EnsemblPlants; AT4G22120.4; AT4G22120.4; AT4G22120.
DR EnsemblPlants; AT4G22120.5; AT4G22120.5; AT4G22120.
DR EnsemblPlants; AT4G22120.6; AT4G22120.6; AT4G22120.
DR GeneID; 828301; -.
DR Gramene; AT4G22120.1; AT4G22120.1; AT4G22120.
DR Gramene; AT4G22120.2; AT4G22120.2; AT4G22120.
DR Gramene; AT4G22120.3; AT4G22120.3; AT4G22120.
DR Gramene; AT4G22120.4; AT4G22120.4; AT4G22120.
DR Gramene; AT4G22120.5; AT4G22120.5; AT4G22120.
DR Gramene; AT4G22120.6; AT4G22120.6; AT4G22120.
DR KEGG; ath:AT4G22120; -.
DR Araport; AT4G22120; -.
DR TAIR; locus:2120673; AT4G22120.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_7_1_1; -.
DR InParanoid; Q5XEZ5; -.
DR OMA; LTIGFHH; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q5XEZ5; -.
DR PRO; PR:Q5XEZ5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XEZ5; baseline and differential.
DR Genevisible; Q5XEZ5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:TAIR.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..771
FT /note="Calcium permeable stress-gated cation channel 1"
FT /id="PRO_0000429798"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..158
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..427
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..526
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..591
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..650
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30382939"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30382939"
FT REGION 741..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 531
FT /note="E->A: Decreases the stretch-activated single-channel
FT conductance by 1.6-fold."
FT /evidence="ECO:0000269|PubMed:30382939"
FT CONFLICT 524
FT /note="G -> S (in Ref. 5; BAD93792)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="L -> F (in Ref. 5; BAD93792)"
FT /evidence="ECO:0000305"
FT HELIX 4..28
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 41..46
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 157..194
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 243..268
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 291..312
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 319..329
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 423..437
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 441..451
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 457..475
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 478..488
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 525..531
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 535..547
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:6MGW"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 566..583
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 591..611
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 624..645
FT /evidence="ECO:0007829|PDB:6MGV"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 660..676
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 678..681
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 685..698
FT /evidence="ECO:0007829|PDB:6MGV"
FT HELIX 704..709
FT /evidence="ECO:0007829|PDB:6MGV"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:6MGV"
SQ SEQUENCE 771 AA; 87894 MW; AEB22EA6726D45C3 CRC64;
MATLQDIGVS AGINILSAFV FFIIFAVLRL QPFNDRVYFS KWYLKGLRSS PARGGAFAQR
FVNLDFRSYM KFLNWMPEAL KMPEPELIDH AGLDSVVYLR IYWLGLKIFT PIAVLAWAVL
VPVNWTNNTL EMAKQLRNVT SSDIDKLSVS NIPEYSMRFW THIVMAYAFT IWTCYVLMKE
YETIANMRLQ FVASEARRPD QFTVLVRNVP PDADESVSEL VEHFFLVNHP DHYLTHQVVC
NANKLADLVK KKKKLQNWLD YYQLKYARNN SQRIMVKLGF LGLWGQKVDA IEHYIAEIDK
ISKEISKERE EVVNDPKAIM PAAFVSFKTR WAAAVCAQTQ QTRNPTQWLT EWAPEPRDVF
WSNLAIPYVS LTVRRLIMHV AFFFLTFFFI VPIAFVQSLA TIEGIVKAAP FLKFIVDDKF
MKSVIQGFLP GIALKLFLAF LPSILMIMSK FEGFTSISSL ERRAAFRYYI FNLVNVFLAS
VIAGAAFEQL NSFLNQSANQ IPKTIGVAIP MKATFFITYI MVDGWAGVAG EILMLKPLIM
FHLKNAFLVK TDKDREEAMD PGSIGFNTGE PRIQLYFLLG LVYAPVTPML LPFILVFFAL
AYIVYRHQII NVYNQEYESA AAFWPDVHGR VIAALVISQL LLMGLLGTKH AALAAPFLIA
LPVLTIGFHH FCKGRYEPAF IRYPLQEAMM KDTLETAREP NLNLKGYLQN AYVHPVFKGD
EDDYDIDDKL GKFEDEAIIV PTKRQSRRNT PAPSIISGDD SPSLPFSGKL V
