TPC1_ARATH
ID TPC1_ARATH Reviewed; 733 AA.
AC Q94KI8; Q948T1; Q9ZT83;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Two pore calcium channel protein 1;
DE AltName: Full=Calcium channel protein 1;
DE Short=AtCCH1;
DE AltName: Full=Fatty acid oxygenation up-regulated protein 2;
DE AltName: Full=Voltage-dependent calcium channel protein TPC1;
DE Short=AtTPC1;
GN Name=TPC1; Synonyms=CCH1, FOU2; OrderedLocusNames=At4g03560;
GN ORFNames=F9H3.19, T5L23.5;
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], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=11577183; DOI=10.1093/pcp/pce145;
RA Furuichi T., Cunningham K.W., Muto S.;
RT "A putative two pore channel AtTPC1 mediates Ca(2+) flux in Arabidopsis
RT leaf cells.";
RL Plant Cell Physiol. 42:900-905(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15772667; DOI=10.1038/nature03381;
RA Peiter E., Maathuis F.J.M., Mills L.N., Knight H., Pelloux J.,
RA Hetherington A.M., Sanders D.;
RT "The vacuolar Ca(2+)-activated channel TPC1 regulates germination and
RT stomatal movement.";
RL Nature 434:404-408(2005).
RN [3]
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 [4]
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 [5]
RP REVIEW.
RX PubMed=12175911; DOI=10.1016/s0005-2736(02)00509-6;
RA White P.J., Bowen H.C., Demidchik V., Nichols C., Davies J.M.;
RT "Genes for calcium-permeable channels in the plasma membrane of plant root
RT cells.";
RL Biochim. Biophys. Acta 1564:299-309(2002).
RN [6]
RP FUNCTION.
RX PubMed=15464979; DOI=10.1016/j.bbrc.2004.09.015;
RA Kawano T., Kadono T., Fumoto K., Lapeyrie F., Kuse M., Isobe M.,
RA Furuichi T., Muto S.;
RT "Aluminum as a specific inhibitor of plant TPC1 Ca(2+) channels.";
RL Biochem. Biophys. Res. Commun. 324:40-45(2004).
RN [7]
RP REVIEW.
RX PubMed=17355948; DOI=10.1093/jxb/erm035;
RA Pottosin I.I., Schoenknecht G.;
RT "Vacuolar calcium channels.";
RL J. Exp. Bot. 58:1559-1569(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [9]
RP MUTAGENESIS OF ASP-454.
RX PubMed=17981874; DOI=10.1093/pcp/pcm151;
RA Bonaventure G., Gfeller A., Rodriguez V.M., Armand F., Farmer E.E.;
RT "The fou2 gain-of-function allele and the wild-type allele of two pore
RT channel 1 contribute to different extents or by different mechanisms to
RT defense gene expression in Arabidopsis.";
RL Plant Cell Physiol. 48:1775-1789(2007).
RN [10]
RP MUTAGENESIS OF ASP-454.
RX PubMed=17253984; DOI=10.1111/j.1365-313x.2006.03002.x;
RA Bonaventure G., Gfeller A., Proebsting W.M., Hoertensteiner S.,
RA Chetelat A., Martinoia E., Farmer E.E.;
RT "A gain-of-function allele of TPC1 activates oxylipin biogenesis after leaf
RT wounding in Arabidopsis.";
RL Plant J. 49:889-898(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Functions as a voltage-gated inward-rectifying Ca(2+) channel
CC (VDCC) across the vacuole membrane. Is one of the essential components
CC of the slow vacuolar (SV) channel. Acts as the major ROS-responsive
CC Ca(2+) channel and is the possible target of Al-dependent inhibition.
CC Involved in the regulation of germination and stomatal movement.
CC {ECO:0000269|PubMed:15464979, ECO:0000269|PubMed:15772667}.
CC -!- ACTIVITY REGULATION: Inhibited by Al(3+).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q94KI8; Q94KI8: TPC1; NbExp=2; IntAct=EBI-1552909, EBI-1552909;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15772667,
CC ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:15772667}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11577183}.
CC -!- DOMAIN: Each of the two internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Plants display an impairment of both the Ca(2+)
CC inhibition of stomatal guard cell opening and abscisic acid (ABA)
CC inhibition of seed germination. {ECO:0000269|PubMed:15772667}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. Two pore calcium channel subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD15312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77841.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB053952; BAB55460.1; -; mRNA.
DR EMBL; AF360372; AAK39554.1; -; mRNA.
DR EMBL; AC005142; AAD15312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF071527; AAD11598.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161497; CAB77841.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82337.1; -; Genomic_DNA.
DR PIR; B85045; B85045.
DR RefSeq; NP_567258.1; NM_116594.5.
DR PDB; 5DQQ; X-ray; 2.87 A; A=12-733.
DR PDB; 5E1J; X-ray; 3.31 A; A=1-733.
DR PDB; 5TUA; X-ray; 3.30 A; A=1-733.
DR PDB; 6CX0; X-ray; 3.50 A; A=11-733.
DR PDB; 6E1K; EM; 3.30 A; A/B=11-733.
DR PDB; 6E1M; EM; 3.30 A; A/B=11-733.
DR PDB; 6E1P; EM; 3.70 A; A/B=11-733.
DR PDB; 7FHK; EM; 3.30 A; A/C=1-733.
DR PDB; 7FHL; EM; 3.10 A; A/C=1-733.
DR PDB; 7FHN; EM; 3.30 A; A/C=1-733.
DR PDB; 7FHO; EM; 2.80 A; A/C=1-733.
DR PDB; 7TBG; EM; 2.50 A; A/B=1-733.
DR PDB; 7TDF; EM; 2.70 A; A/B=1-733.
DR PDBsum; 5DQQ; -.
DR PDBsum; 5E1J; -.
DR PDBsum; 5TUA; -.
DR PDBsum; 6CX0; -.
DR PDBsum; 6E1K; -.
DR PDBsum; 6E1M; -.
DR PDBsum; 6E1P; -.
DR PDBsum; 7FHK; -.
DR PDBsum; 7FHL; -.
DR PDBsum; 7FHN; -.
DR PDBsum; 7FHO; -.
DR PDBsum; 7TBG; -.
DR PDBsum; 7TDF; -.
DR AlphaFoldDB; Q94KI8; -.
DR SMR; Q94KI8; -.
DR BioGRID; 10969; 10.
DR DIP; DIP-39873N; -.
DR IntAct; Q94KI8; 9.
DR STRING; 3702.AT4G03560.1; -.
DR TCDB; 1.A.1.11.26; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q94KI8; -.
DR SwissPalm; Q94KI8; -.
DR PaxDb; Q94KI8; -.
DR PRIDE; Q94KI8; -.
DR ProteomicsDB; 232406; -.
DR ABCD; Q94KI8; 1 sequenced antibody.
DR EnsemblPlants; AT4G03560.1; AT4G03560.1; AT4G03560.
DR GeneID; 825655; -.
DR Gramene; AT4G03560.1; AT4G03560.1; AT4G03560.
DR KEGG; ath:AT4G03560; -.
DR Araport; AT4G03560; -.
DR TAIR; locus:2128716; AT4G03560.
DR eggNOG; KOG2301; Eukaryota.
DR HOGENOM; CLU_426053_0_0_1; -.
DR InParanoid; Q94KI8; -.
DR OMA; QHACDQR; -.
DR OrthoDB; 761764at2759; -.
DR PhylomeDB; Q94KI8; -.
DR PRO; PR:Q94KI8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94KI8; baseline and differential.
DR Genevisible; Q94KI8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; TAS:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:TAIR.
DR GO; GO:0006816; P:calcium ion transport; IMP:TAIR.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR044581; TPC1_plant.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46988; PTHR46988; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Calcium channel; Calcium transport;
KW Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole;
KW Voltage-gated channel.
FT CHAIN 1..733
FT /note="Two pore calcium channel protein 1"
FT /id="PRO_0000343169"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..120
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..199
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..245
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT INTRAMEM 246..260
FT /note="Pore-forming; Name=Pore-forming 1"
FT TOPO_DOM 261..282
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..465
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..528
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..546
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..615
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT INTRAMEM 616..630
FT /note="Pore-forming; Name=Pore-forming 2"
FT TOPO_DOM 631..651
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 322..357
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 363..398
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 686..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 454
FT /note="D->N: In fou2; shows elevated LOX and AOS activity
FT levels and an increased resistance to B.cinerea. Strongly
FT increases oxylipin biogenesis in response to wounding."
FT /evidence="ECO:0000269|PubMed:17253984,
FT ECO:0000269|PubMed:17981874"
FT CONFLICT 33
FT /note="K -> R (in Ref. 1; BAB55460)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Y -> F (in Ref. 1; BAB55460)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="N -> T (in Ref. 1; BAB55460)"
FT /evidence="ECO:0000305"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:7FHL"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5E1J"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5DQQ"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 151..173
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 200..237
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 242..247
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:5DQQ"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 296..334
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6E1K"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5TUA"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 385..389
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 418..428
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 431..452
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:5TUA"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:7FHN"
FT HELIX 461..486
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 495..516
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 527..541
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 542..547
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 549..586
FT /evidence="ECO:0007829|PDB:7FHO"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:7FHL"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:5E1J"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 616..627
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 633..643
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 649..658
FT /evidence="ECO:0007829|PDB:7FHO"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 663..683
FT /evidence="ECO:0007829|PDB:7FHO"
FT HELIX 685..691
FT /evidence="ECO:0007829|PDB:6E1M"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:6E1K"
SQ SEQUENCE 733 AA; 84873 MW; 1CA978D6B8BFF445 CRC64;
MEDPLIGRDS LGGGGTDRVR RSEAITHGTP FQKAAALVDL AEDGIGLPVE ILDQSSFGES
ARYYFIFTRL DLIWSLNYFA LLFLNFFEQP LWCEKNPKPS CKDRDYYYLG ELPYLTNAES
IIYEVITLAI LLVHTFFPIS YEGSRIFWTS RLNLVKVACV VILFVDVLVD FLYLSPLAFD
FLPFRIAPYV RVIIFILSIR ELRDTLVLLS GMLGTYLNIL ALWMLFLLFA SWIAFVMFED
TQQGLTVFTS YGATLYQMFI LFTTSNNPDV WIPAYKSSRW SSVFFVLYVL IGVYFVTNLI
LAVVYDSFKE QLAKQVSGMD QMKRRMLEKA FGLIDSDKNG EIDKNQCIKL FEQLTNYRTL
PKISKEEFGL IFDELDDTRD FKINKDEFAD LCQAIALRFQ KEEVPSLFEH FPQIYHSALS
QQLRAFVRSP NFGYAISFIL IINFIAVVVE TTLDIEESSA QKPWQVAEFV FGWIYVLEMA
LKIYTYGFEN YWREGANRFD FLVTWVIVIG ETATFITPDE NTFFSNGEWI RYLLLARMLR
LIRLLMNVQR YRAFIATFIT LIPSLMPYLG TIFCVLCIYC SIGVQVFGGL VNAGNKKLFE
TELAEDDYLL FNFNDYPNGM VTLFNLLVMG NWQVWMESYK DLTGTWWSIT YFVSFYVITI
LLLLNLVVAF VLEAFFTELD LEEEEKCQGQ DSQEKRNRRR SAGSKSRSQR VDTLLHHMLG
DELSKPECST SDT
