CSCL5_ARATH
ID CSCL5_ARATH Reviewed; 772 AA.
AC Q9XEA1; A0A097NUN6; Q93ZR7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein OSCA1 {ECO:0000303|PubMed:25162526};
DE AltName: Full=CSC1-like protein At4g04340 {ECO:0000305};
DE AltName: Full=Hyperosmolality-gated Ca2+ permeable channel 1.1 {ECO:0000303|PubMed:25162526};
DE Short=AtOSCA1.1 {ECO:0000303|PubMed:25162526};
DE AltName: Full=Protein reduced hyperosmolality-induced [Ca(2+)]i increase 1 {ECO:0000303|PubMed:25162526};
GN Name=OSCA1 {ECO:0000303|PubMed:25162526};
GN Synonyms=OSCA1.1 {ECO:0000303|PubMed:25162526};
GN OrderedLocusNames=At4g04340 {ECO:0000312|Araport:AT4G04340};
GN ORFNames=T19B17.6 {ECO:0000312|EMBL:AAD36947.1};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF GLY-59 AND GLY-507, AND DISRUPTION PHENOTYPE.
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP GENE FAMILY.
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 (3.50 ANGSTROMS), FUNCTION,
RP HOMODIMERIZATION, TOPOLOGY, ACTIVITY REGULATION, GLYCOSYLATION AT ASN-138,
RP AND MUTAGENESIS OF ASN-124; ASN-138; GLN-339; THR-340 AND GLU-688.
RX PubMed=30190597; DOI=10.1038/s41594-018-0117-6;
RA Zhang M., Wang D., Kang Y., Wu J.X., Yao F., Pan C., Yan Z., Song C.,
RA Chen L.;
RT "Structure of the mechanosensitive OSCA channels.";
RL Nat. Struct. Mol. Biol. 25:850-858(2018).
CC -!- FUNCTION: Acts as a hyperosmolarity-gated non-selective cation channel
CC that permeates Ca(2+) ions (PubMed:25162526, PubMed:30190597). Shows
CC the following permeability sequence: K(+) > Ba(2+) = Ca(2+) > Na(+) =
CC Mg(2+) = Cs(+) (PubMed:25162526). Mechanosensitive ion channel that
CC converts mechanical stimuli into a flow of ions (PubMed:30190597).
CC {ECO:0000269|PubMed:25162526, ECO:0000269|PubMed:30190597}.
CC -!- ACTIVITY REGULATION: Activated by mechanical pressure.
CC {ECO:0000269|PubMed:30190597}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30190597}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25162526};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, roots and guard
CC cells. {ECO:0000269|PubMed:25162526}.
CC -!- DISRUPTION PHENOTYPE: Impaired osmotic Ca(2+) signaling in guard cells
CC and root cells, and attenuated water transpiration regulation and root
CC growth in response to osmotic stress. {ECO:0000269|PubMed:25162526}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; KJ920356; AIU34613.1; -; mRNA.
DR EMBL; AF069441; AAD36947.1; -; Genomic_DNA.
DR EMBL; AL161500; CAB77902.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82380.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82381.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82382.1; -; Genomic_DNA.
DR EMBL; AY056305; AAL07154.1; -; mRNA.
DR EMBL; AY093209; AAM13208.1; -; mRNA.
DR PIR; H85054; H85054.
DR RefSeq; NP_192343.1; NM_116672.4.
DR RefSeq; NP_849296.1; NM_178965.2.
DR RefSeq; NP_849297.1; NM_178966.1.
DR PDB; 6JPF; EM; 3.52 A; A/B=1-772.
DR PDBsum; 6JPF; -.
DR AlphaFoldDB; Q9XEA1; -.
DR SMR; Q9XEA1; -.
DR STRING; 3702.AT4G04340.3; -.
DR TCDB; 1.A.17.5.19; the calcium-dependent chloride channel (ca-clc) family.
DR iPTMnet; Q9XEA1; -.
DR PaxDb; Q9XEA1; -.
DR PRIDE; Q9XEA1; -.
DR ProteomicsDB; 220348; -.
DR EnsemblPlants; AT4G04340.1; AT4G04340.1; AT4G04340.
DR EnsemblPlants; AT4G04340.2; AT4G04340.2; AT4G04340.
DR EnsemblPlants; AT4G04340.3; AT4G04340.3; AT4G04340.
DR GeneID; 825754; -.
DR Gramene; AT4G04340.1; AT4G04340.1; AT4G04340.
DR Gramene; AT4G04340.2; AT4G04340.2; AT4G04340.
DR Gramene; AT4G04340.3; AT4G04340.3; AT4G04340.
DR KEGG; ath:AT4G04340; -.
DR Araport; AT4G04340; -.
DR TAIR; locus:2134882; AT4G04340.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_7_1_1; -.
DR InParanoid; Q9XEA1; -.
DR OMA; WTNNELE; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q9XEA1; -.
DR PRO; PR:Q9XEA1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEA1; baseline and differential.
DR Genevisible; Q9XEA1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:TAIR.
DR GO; GO:0071474; P:cellular hyperosmotic response; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; TAS:UniProtKB.
DR GO; GO:0090279; P:regulation of calcium ion import; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
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; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..772
FT /note="Protein OSCA1"
FT /id="PRO_0000429803"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..158
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..424
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..527
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..592
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..655
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30190597"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30190597"
FT REGION 339..344
FT /note="Cytoplasmic region required for homodimerization"
FT /evidence="ECO:0000269|PubMed:30190597"
FT REGION 686..688
FT /note="Cytoplasmic region required for homodimerization"
FT /evidence="ECO:0000269|PubMed:30190597"
FT REGION 743..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000305|PubMed:30190597"
FT MUTAGEN 59
FT /note="G->R: In osca1-1; defect in the perception of
FT hyperosmolarity; when associated with D-507."
FT /evidence="ECO:0000269|PubMed:25162526"
FT MUTAGEN 124
FT /note="N->Q: No effect on the molecular weight of OSCA1
FT when overexpressed in a heterologous system."
FT /evidence="ECO:0000269|PubMed:30190597"
FT MUTAGEN 138
FT /note="N->Q: Decreases the molecular weight of OSCA1 when
FT overexpressed in a heterologous system."
FT /evidence="ECO:0000269|PubMed:30190597"
FT MUTAGEN 339
FT /note="Q->A: Slightly prevents the formation of homodimer."
FT /evidence="ECO:0000269|PubMed:30190597"
FT MUTAGEN 340
FT /note="T->A: Prevents the formation of homodimer."
FT /evidence="ECO:0000269|PubMed:30190597"
FT MUTAGEN 507
FT /note="G->D: In osca1-1; defect in the perception of
FT hyperosmolarity; when associated with R-59."
FT /evidence="ECO:0000269|PubMed:25162526"
FT MUTAGEN 688
FT /note="E->A: Prevents the formation of homodimer."
FT /evidence="ECO:0000269|PubMed:30190597"
FT CONFLICT 667
FT /note="I -> T (in Ref. 4; AAL07154)"
FT /evidence="ECO:0000305"
FT HELIX 6..27
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 84..117
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 158..194
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 243..266
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 292..313
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 320..330
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6JPF"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 373..387
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 423..438
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 458..475
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 510..521
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 522..526
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 527..534
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 567..584
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 592..612
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 625..647
FT /evidence="ECO:0007829|PDB:6JPF"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 655..682
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 686..699
FT /evidence="ECO:0007829|PDB:6JPF"
FT HELIX 705..712
FT /evidence="ECO:0007829|PDB:6JPF"
SQ SEQUENCE 772 AA; 87607 MW; 51786B50068D96AB CRC64;
MATLKDIGVS AGINILTAFI FFIIFAFLRL QPFNDRVYFS KWYLRGLRSS PASGGGFAGR
FVNLELRSYL KFLHWMPEAL KMPERELIDH AGLDSVVYLR IYWLGLKIFA PIAMLAWAVL
VPVNWTNNEL ELAKHFKNVT SSDIDKLTIS NIPEGSNRFW AHIIMAYAFT IWTCYMLMKE
YETVANMRLQ FLASEGRRPD QFTVLVRNVP PDPDETVSEL VEHFFLVNHP DNYLTHQVVC
NANKLADLVS KKTKLQNWLD YYQLKYTRNN SQIRPITKLG CLGLCGQKVD AIEHYIAEVD
KTSKEIAEER ENVVNDQKSV MPASFVSFKT RWAAAVCAQT TQTRNPTEWL TEWAAEPRDI
YWPNLAIPYV SLTVRRLVMN VAFFFLTFFF IIPIAFVQSL ATIEGIEKVA PFLKVIIEKD
FIKSLIQGLL AGIALKLFLI FLPAILMTMS KFEGFTSVSF LERRSASRYY IFNLVNVFLG
SVIAGAAFEQ LNSFLNQSPN QIPKTIGMAI PMKATFFITY IMVDGWAGVA GEILMLKPLI
IYHLKNAFLV KTEKDREEAM NPGSIGFNTG EPQIQLYFLL GLVYAPVTPM LLPFILVFFA
LAYVVYRHQI INVYNQEYES AAAFWPDVHG RVITALIISQ LLLMGLLGTK HAASAAPFLI
ALPVITIGFH RFCKGRFEPA FVRYPLQEAM MKDTLERARE PNLNLKGYLQ DAYIHPVFKG
GDNDDDGDMI GKLENEVIIV PTKRQSRRNT PAPSRISGES SPSLAVINGK EV
