AKT2_ARATH
ID AKT2_ARATH Reviewed; 802 AA.
AC Q38898; Q0WMS8; Q42408; Q9M0L6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Potassium channel AKT2/3;
GN Name=AKT2; Synonyms=AKT3; OrderedLocusNames=At4g22200; ORFNames=T10I14.30;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8552711; DOI=10.1104/pp.109.3.1093;
RA Cao Y., Ward J.M., Kelly W.B., Ichida A.M., Gaber R.F., Anderson J.A.,
RA Uozumi N., Schroeder J.I., Crawford N.M.;
RT "Multiple genes, tissue specificity, and expression-dependent modulation
RT contribute to the functional diversity of potassium channels in Arabidopsis
RT thaliana.";
RL Plant Physiol. 109:1093-1106(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8549795; DOI=10.1016/0014-5793(95)01417-9;
RA Ketchum K.A., Slayman C.W.;
RT "Isolation of an ion channel gene from Arabidopsis thaliana using the H5
RT signature sequence from voltage-dependent K+ channels.";
RL FEBS Lett. 378:19-26(1996).
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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=10377458; DOI=10.1073/pnas.96.13.7581;
RA Marten I., Hoth S., Deeken R., Ache P., Ketchum K.A., Hoshi T., Hedrich R.;
RT "AKT3, a phloem-localized K+ channel, is blocked by protons.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7581-7586(1999).
RN [7]
RP INTERACTION WITH KAT1.
RX PubMed=9916143; DOI=10.1007/s002329900476;
RA Baizabal-Aguirre V.M., Clemens S., Uozumi N., Schroeder J.I.;
RT "Suppression of inward-rectifying K+ channels KAT1 and AKT2 by dominant
RT negative point mutations in the KAT1 alpha-subunit.";
RL J. Membr. Biol. 167:119-125(1999).
RN [8]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=10852932; DOI=10.2307/3871214;
RA Lacombe B., Pilot G., Michard E., Gaymard F., Sentenac H., Thibaud J.-B.;
RT "A shaker-like K(+) channel with weak rectification is expressed in both
RT source and sink phloem tissues of Arabidopsis.";
RL Plant Cell 12:837-851(2000).
RN [9]
RP INTERACTION WITH PP2CA.
RX PubMed=11181729; DOI=10.1093/jxb/52.354.181;
RA Vranova E., Taehtiharju S., Sriprang R., Willekens H., Heino P.,
RA Palva E.T., Inze D., Van Camp W.;
RT "The AKT3 potassium channel protein interacts with the AtPP2CA protein
RT phosphatase 2C.";
RL J. Exp. Bot. 52:181-182(2001).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [11]
RP FUNCTION.
RX PubMed=12447548; DOI=10.1007/s00425-002-0895-1;
RA Deeken R., Geiger D., Fromm J., Koroleva O., Ache P., Langenfeld-Heyser R.,
RA Sauer N., May S.T., Hedrich R.;
RT "Loss of the AKT2/3 potassium channel affects sugar loading into the phloem
RT of Arabidopsis.";
RL Planta 216:334-344(2002).
RN [12]
RP INTERACTION WITH PP2CA, DEPHOSPHORYLATION BY PP2CA, AND TISSUE SPECIFICITY.
RX PubMed=12034902; DOI=10.1105/tpc.000943;
RA Cherel I., Michard E., Platet N., Mouline K., Alcon C., Sentenac H.,
RA Thibaud J.-B.;
RT "Physical and functional interaction of the Arabidopsis K(+) channel AKT2
RT and phosphatase AtPP2CA.";
RL Plant Cell 14:1133-1146(2002).
RN [13]
RP MUTAGENESIS OF HIS-243; SER-286 AND ILE-289.
RX PubMed=12172027; DOI=10.1105/tpc.003244;
RA Geiger D., Becker D., Lacombe B., Hedrich R.;
RT "Outer pore residues control the H(+) and K(+) sensitivity of the
RT Arabidopsis potassium channel AKT3.";
RL Plant Cell 14:1859-1868(2002).
RN [14]
RP FUNCTION, INTERACTION WITH AKT1 AND KAT3, AND INDUCTION.
RX PubMed=12678562; DOI=10.1023/a:1022597102282;
RA Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
RT "Regulated expression of Arabidopsis shaker K(+) channel genes involved in
RT K(+) uptake and distribution in the plant.";
RL Plant Mol. Biol. 51:773-787(2003).
RN [15]
RP SUBCELLULAR LOCATION, INTERACTION WITH CIPK6, AND DISRUPTION PHENOTYPE.
RX PubMed=21445098; DOI=10.1038/cr.2011.50;
RA Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K.,
RA Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I., Thibaud J.B.,
RA Kudla J.;
RT "Calcium-dependent modulation and plasma membrane targeting of the AKT2
RT potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase
RT complex.";
RL Cell Res. 21:1116-1130(2011).
RN [16]
RP INTERACTION WITH SLAC1.
RX PubMed=27002025; DOI=10.1105/tpc.16.01050;
RA Zhang A., Ren H.M., Tan Y.Q., Qi G.N., Yao F.Y., Wu G.L., Yang L.W.,
RA Hussain J., Sun S.J., Wang Y.F.;
RT "S-type anion channels SLAC1 and SLAH3 function as essential negative
RT regulators of inward K+ channels and stomatal opening in Arabidopsis.";
RL Plant Cell 28:949-955(2016).
CC -!- FUNCTION: Highly selective and weak inward-rectifying potassium
CC channel. Plays a role in both loading and unloading potassium into/from
CC the phloem sap. Seems to control sugar loading into phloem via a
CC voltage-dependent process. Blocked by physiological concentrations of
CC external calcium and by external acidification. May interact with the
CC cytoskeleton or with regulatory proteins. Dephosphorylation by PP2CA
CC not only leads to the inhibition of potassium currents but also to an
CC increase of the voltage-dependence of the channel. Regulated by the
CC CBL4/CIPK6 calcium sensor/protein kinase complex via a kinase
CC interaction-dependent but phosphorylation-independent translocation of
CC the channel to the plasma membrane. {ECO:0000269|PubMed:12447548,
CC ECO:0000269|PubMed:12678562}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. Interacts with the
CC phosphatase PPC2A and the kinase CIPK6. May interact with AKT1, KAT1
CC and KAT3. Interacts with SLAC1 (PubMed:27002025).
CC {ECO:0000269|PubMed:11181729, ECO:0000269|PubMed:12034902,
CC ECO:0000269|PubMed:12678562, ECO:0000269|PubMed:21445098,
CC ECO:0000269|PubMed:27002025, ECO:0000269|PubMed:9916143}.
CC -!- INTERACTION:
CC Q38898; Q38998: AKT1; NbExp=3; IntAct=EBI-1552774, EBI-974289;
CC Q38898; Q38898: AKT2; NbExp=3; IntAct=EBI-1552774, EBI-1552774;
CC Q38898; Q39128: KAT1; NbExp=4; IntAct=EBI-1552774, EBI-1552490;
CC Q38898; Q38849: KAT2; NbExp=3; IntAct=EBI-1552774, EBI-2117720;
CC Q38898; P49598: PP2CA; NbExp=5; IntAct=EBI-1552774, EBI-1764934;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21445098}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21445098}. Note=Targeted to the cell membrane when
CC interacting with CIPK6 and CBL4.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the phloem tissues throughout
CC the plant but also, at a lower level, in leaf epiderm, mesophyll and
CC guard cells. {ECO:0000269|PubMed:10377458, ECO:0000269|PubMed:10852932,
CC ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:8552711}.
CC -!- INDUCTION: In shoots, strongly induced by abscisic acid (ABA) treatment
CC and reduced after NaCl treatment or potassium starvation.
CC {ECO:0000269|PubMed:12678562}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The pore-
CC forming region H5 is enclosed by the transmembrane segments S5 and S6
CC in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC seems to be involved in potassium selectivity.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization.
CC -!- PTM: Dephosphorylated by PP2CA.
CC -!- DISRUPTION PHENOTYPE: Delayed development and flowering.
CC {ECO:0000269|PubMed:21445098}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA96154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA16770.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB79175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U40154; AAA97865.1; -; mRNA.
DR EMBL; U44744; AAA96153.1; ALT_INIT; Genomic_DNA.
DR EMBL; U44745; AAA96154.1; ALT_INIT; mRNA.
DR EMBL; AL021712; CAA16770.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161556; CAB79175.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84571.1; -; Genomic_DNA.
DR EMBL; AK229735; BAF01572.1; -; mRNA.
DR PIR; S68699; S68699.
DR RefSeq; NP_567651.1; NM_118342.3.
DR AlphaFoldDB; Q38898; -.
DR SMR; Q38898; -.
DR BioGRID; 13600; 14.
DR IntAct; Q38898; 10.
DR STRING; 3702.AT4G22200.1; -.
DR TCDB; 1.A.1.4.6; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q38898; -.
DR PaxDb; Q38898; -.
DR PRIDE; Q38898; -.
DR ProteomicsDB; 244997; -.
DR EnsemblPlants; AT4G22200.1; AT4G22200.1; AT4G22200.
DR GeneID; 828311; -.
DR Gramene; AT4G22200.1; AT4G22200.1; AT4G22200.
DR KEGG; ath:AT4G22200; -.
DR Araport; AT4G22200; -.
DR TAIR; locus:2132065; AT4G22200.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q38898; -.
DR OrthoDB; 281394at2759; -.
DR PhylomeDB; Q38898; -.
DR PRO; PR:Q38898; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38898; baseline and differential.
DR Genevisible; Q38898; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR045319; KAT/AKT.
DR InterPro; IPR021789; KHA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; PTHR45743; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Endoplasmic reticulum; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..802
FT /note="Potassium channel AKT2/3"
FT /id="PRO_0000054122"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 266..285
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 540..569
FT /note="ANK 1"
FT REPEAT 573..602
FT /note="ANK 2"
FT REPEAT 606..636
FT /note="ANK 3"
FT REPEAT 637..666
FT /note="ANK 4"
FT REPEAT 670..699
FT /note="ANK 5"
FT DOMAIN 725..802
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 394..513
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 243
FT /note="H->D: Abolishes the proton sensitivity; lack of
FT susceptibility to extracellular potassium; when associated
FT with E-286."
FT /evidence="ECO:0000269|PubMed:12172027"
FT MUTAGEN 286
FT /note="S->E: Abolishes the proton and the potassium
FT sensitivity; lack of susceptibility to extracellular
FT potassium; when associated with D-243."
FT /evidence="ECO:0000269|PubMed:12172027"
FT MUTAGEN 289
FT /note="I->R: No change in proton sensitivity."
FT /evidence="ECO:0000269|PubMed:12172027"
SQ SEQUENCE 802 AA; 91308 MW; 6F138F9149ED3CD7 CRC64;
MDLKYSASHC NLSSDMKLRR FHQHRGKGRE EEYDASSLSL NNLSKLILPP LGVASYNQNH
IRSSGWIISP MDSRYRCWEF YMVLLVAYSA WVYPFEVAFL NSSPKRNLCI ADNIVDLFFA
VDIVLTFFVA YIDERTQLLV REPKQIAVRY LSTWFLMDVA STIPFDAIGY LITGTSTLNI
TCNLLGLLRF WRLRRVKHLF TRLEKDIRYS YFWIRCFRLL SVTLFLVHCA GCSYYLIADR
YPHQGKTWTD AIPNFTETSL SIRYIAAIYW SITTMTTVGY GDLHASNTIE MVFITVYMLF
NLGLTAYLIG NMTNLVVEGT RRTMEFRNSI EAASNFVNRN RLPPRLKDQI LAYMCLRFKA
ESLNQQHLID QLPKSIYKSI CQHLFLPSVE KVYLFKGVSR EILLLLVSKM KAEYIPPRED
VIMQNEAPDD VYIIVSGEVE IIDSEMERES VLGTLRCGDI FGEVGALCCR PQSYTFQTKS
LSQLLRLKTS FLIETMQIKQ QDNATMLKNF LQHHKKLSNL DIGDLKAQQN GENTDVVPPN
IASNLIAVVT TGNAALLDEL LKAKLSPDIT DSKGKTPLHV AASRGYEDCV LVLLKHGCNI
HIRDVNGNSA LWEAIISKHY EIFRILYHFA AISDPHIAGD LLCEAAKQNN VEVMKALLKQ
GLNVDTEDHH GVTALQVAMA EDQMDMVNLL ATNGADVVCV NTHNEFTPLE KLRVVEEEEE
EERGRVSIYR GHPLERRERS CNEAGKLILL PPSLDDLKKI AGEKFGFDGS ETMVTNEDGA
EIDSIEVIRD NDKLYFVVNK II
