RLK5_ARATH
ID RLK5_ARATH Reviewed; 999 AA.
AC P47735; C0LGR4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Receptor-like protein kinase 5;
DE EC=2.7.10.1;
DE EC=2.7.11.1;
DE AltName: Full=Protein HAESA;
DE Flags: Precursor;
GN Name=RLK5; Synonyms=HAE; OrderedLocusNames=At4g28490; ORFNames=F21O9.180;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8220453; DOI=10.1111/j.1365-313x.1993.tb00164.x;
RA Walker J.C.;
RT "Receptor-like protein kinase genes of Arabidopsis thaliana.";
RL Plant J. 3:451-456(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
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 CHARACTERIZATION, AND MUTAGENESIS OF LYS-711.
RX PubMed=8086440; DOI=10.1016/0167-4838(94)90160-0;
RA Horn M.A., Walker J.C.;
RT "Biochemical properties of the autophosphorylation of RLK5, a receptor-like
RT protein kinase from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1208:65-74(1994).
RN [6]
RP FUNCTION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10640280;
RA Jinn T.-L., Stone J.M., Walker J.C.;
RT "HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral
RT organ abscission.";
RL Genes Dev. 14:108-117(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18660431; DOI=10.1105/tpc.108.059139;
RA Stenvik G.-E., Tandstad N.M., Guo Y., Shi C.-L., Kristiansen W.,
RA Holmgren A., Clark S.E., Aalen R.B., Butenko M.A.;
RT "The EPIP peptide of INFLORESCENCE DEFICIENT IN ABSCISSION is sufficient to
RT induce abscission in arabidopsis through the receptor-like kinases HAESA
RT and HAESA-LIKE2.";
RL Plant Cell 20:1805-1817(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18809915; DOI=10.1073/pnas.0805539105;
RA Cho S.K., Larue C.T., Chevalier D., Wang H., Jinn T.-L., Zhang S.,
RA Walker J.C.;
RT "Regulation of floral organ abscission in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15629-15634(2008).
RN [9]
RP AUTOPHOSPHORYLATION.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
RN [10]
RP INTERACTION WITH CST.
RX PubMed=21628627; DOI=10.1104/pp.111.175224;
RA Burr C.A., Leslie M.E., Orlowski S.K., Chen I., Wright C.E., Daniels M.J.,
RA Liljegren S.J.;
RT "CAST AWAY, a membrane-associated receptor-like kinase, inhibits organ
RT abscission in Arabidopsis.";
RL Plant Physiol. 156:1837-1850(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 20-620 IN COMPLEX WITH IDA,
RP GLYCOSYLATION AT ASN-98; ASN-102; ASN-150; ASN-185; ASN-269; ASN-282 AND
RP ASN-576, AND INTERACTION WITH IDA.
RX PubMed=27058169; DOI=10.7554/elife.15075;
RA Santiago J., Brandt B., Wildhagen M., Hohmann U., Hothorn L.A.,
RA Butenko M.A., Hothorn M.;
RT "Mechanistic insight into a peptide hormone signaling complex mediating
RT floral organ abscission.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Receptor with a dual specificity kinase activity acting on
CC both serine/threonine- and tyrosine-containing substrates that controls
CC floral organ abscission. May interact with the 'INFLORESCENCE DEFICIENT
CC IN ABSCISSION' (IDA) ligands family. {ECO:0000269|PubMed:10640280,
CC ECO:0000269|PubMed:18660431, ECO:0000269|PubMed:18809915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Have significantly greater activity in the presence of Mn(2+) than
CC Mg(2+).;
CC -!- SUBUNIT: Interacts with CST (PubMed:21628627). Binds to IDA
CC (PubMed:27058169). {ECO:0000269|PubMed:21628627,
CC ECO:0000269|PubMed:27058169}.
CC -!- INTERACTION:
CC P47735; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-11420624, EBI-16954682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10640280};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:10640280}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and rosettes. Expressed at the
CC base of petioles and pedicels, and in the abscission zones of the
CC floral organs. {ECO:0000269|PubMed:10640280}.
CC -!- PTM: Autophosphorylated on Ser, Thr and Tyr residues.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC HSL2. Hae and hsl2 double mutants have a strong abscission defect.
CC {ECO:0000269|PubMed:18660431, ECO:0000269|PubMed:18809915}.
CC -!- MISCELLANEOUS: The name HAESA derives from a Latin word meaning 'to
CC adhere to'.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M84660; AAA32859.1; -; mRNA.
DR EMBL; FJ708755; ACN59349.1; -; mRNA.
DR EMBL; AL021749; CAA16889.1; -; Genomic_DNA.
DR EMBL; AL161572; CAB79651.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85494.1; -; Genomic_DNA.
DR PIR; S27756; S27756.
DR RefSeq; NP_194578.1; NM_118991.3.
DR PDB; 5IXO; X-ray; 1.74 A; A=20-620.
DR PDB; 5IXQ; X-ray; 1.86 A; A=20-620.
DR PDB; 5IXT; X-ray; 1.94 A; A=20-620.
DR PDB; 5IYV; X-ray; 2.56 A; A=20-620.
DR PDB; 5IYX; X-ray; 2.43 A; A=20-620.
DR PDBsum; 5IXO; -.
DR PDBsum; 5IXQ; -.
DR PDBsum; 5IXT; -.
DR PDBsum; 5IYV; -.
DR PDBsum; 5IYX; -.
DR AlphaFoldDB; P47735; -.
DR SMR; P47735; -.
DR BioGRID; 14254; 26.
DR IntAct; P47735; 22.
DR STRING; 3702.AT4G28490.1; -.
DR iPTMnet; P47735; -.
DR PaxDb; P47735; -.
DR PRIDE; P47735; -.
DR ProteomicsDB; 228128; -.
DR EnsemblPlants; AT4G28490.1; AT4G28490.1; AT4G28490.
DR GeneID; 828967; -.
DR Gramene; AT4G28490.1; AT4G28490.1; AT4G28490.
DR KEGG; ath:AT4G28490; -.
DR Araport; AT4G28490; -.
DR TAIR; locus:2005540; AT4G28490.
DR eggNOG; ENOG502QQFB; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; P47735; -.
DR OMA; RGWKNLN; -.
DR OrthoDB; 145621at2759; -.
DR PhylomeDB; P47735; -.
DR BRENDA; 2.7.10.2; 399.
DR PRO; PR:P47735; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P47735; baseline and differential.
DR Genevisible; P47735; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0010227; P:floral organ abscission; IMP:TAIR.
DR GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 16.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..999
FT /note="Receptor-like protein kinase 5"
FT /id="PRO_0000024381"
FT TOPO_DOM 15..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 90..112
FT /note="LRR 1"
FT REPEAT 115..137
FT /note="LRR 2"
FT REPEAT 140..161
FT /note="LRR 3"
FT REPEAT 164..186
FT /note="LRR 4"
FT REPEAT 188..208
FT /note="LRR 5"
FT REPEAT 213..236
FT /note="LRR 6"
FT REPEAT 237..259
FT /note="LRR 7"
FT REPEAT 285..307
FT /note="LRR 8"
FT REPEAT 308..330
FT /note="LRR 9"
FT REPEAT 332..353
FT /note="LRR 10"
FT REPEAT 356..378
FT /note="LRR 11"
FT REPEAT 380..402
FT /note="LRR 12"
FT REPEAT 404..427
FT /note="LRR 13"
FT REPEAT 428..450
FT /note="LRR 14"
FT REPEAT 452..474
FT /note="LRR 15"
FT REPEAT 500..523
FT /note="LRR 16"
FT REPEAT 524..546
FT /note="LRR 17"
FT REPEAT 548..569
FT /note="LRR 18"
FT REPEAT 571..593
FT /note="LRR 19"
FT DOMAIN 683..968
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 972..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 819
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 689..697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 711
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 766
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 806
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 864
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 871
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IYX"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:5IXO"
FT MUTAGEN 711
FT /note="K->E: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:8086440"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5IXQ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:5IXO"
FT TURN 349..354
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:5IXO"
FT TURN 373..378
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 397..401
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 469..473
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:5IXO"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:5IXO"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:5IXO"
SQ SEQUENCE 999 AA; 109096 MW; F5793D899EA0C6A7 CRC64;
MLYCLILLLC LSSTYLPSLS LNQDATILRQ AKLGLSDPAQ SLSSWSDNND VTPCKWLGVS
CDATSNVVSV DLSSFMLVGP FPSILCHLPS LHSLSLYNNS INGSLSADDF DTCHNLISLD
LSENLLVGSI PKSLPFNLPN LKFLEISGNN LSDTIPSSFG EFRKLESLNL AGNFLSGTIP
ASLGNVTTLK ELKLAYNLFS PSQIPSQLGN LTELQVLWLA GCNLVGPIPP SLSRLTSLVN
LDLTFNQLTG SIPSWITQLK TVEQIELFNN SFSGELPESM GNMTTLKRFD ASMNKLTGKI
PDNLNLLNLE SLNLFENMLE GPLPESITRS KTLSELKLFN NRLTGVLPSQ LGANSPLQYV
DLSYNRFSGE IPANVCGEGK LEYLILIDNS FSGEISNNLG KCKSLTRVRL SNNKLSGQIP
HGFWGLPRLS LLELSDNSFT GSIPKTIIGA KNLSNLRISK NRFSGSIPNE IGSLNGIIEI
SGAENDFSGE IPESLVKLKQ LSRLDLSKNQ LSGEIPRELR GWKNLNELNL ANNHLSGEIP
KEVGILPVLN YLDLSSNQFS GEIPLELQNL KLNVLNLSYN HLSGKIPPLY ANKIYAHDFI
GNPGLCVDLD GLCRKITRSK NIGYVWILLT IFLLAGLVFV VGIVMFIAKC RKLRALKSST
LAASKWRSFH KLHFSEHEIA DCLDEKNVIG FGSSGKVYKV ELRGGEVVAV KKLNKSVKGG
DDEYSSDSLN RDVFAAEVET LGTIRHKSIV RLWCCCSSGD CKLLVYEYMP NGSLADVLHG
DRKGGVVLGW PERLRIALDA AEGLSYLHHD CVPPIVHRDV KSSNILLDSD YGAKVADFGI
AKVGQMSGSK TPEAMSGIAG SCGYIAPEYV YTLRVNEKSD IYSFGVVLLE LVTGKQPTDS
ELGDKDMAKW VCTALDKCGL EPVIDPKLDL KFKEEISKVI HIGLLCTSPL PLNRPSMRKV
VIMLQEVSGA VPCSSPNTSK RSKTGGKLSP YYTEDLNSV
