(data stored in SCRATCH zone)

SWISSPROT: RGI3_ARATH

ID   RGI3_ARATH              Reviewed;        1091 AA.
AC   C0LGR3; O65580; Q8W556;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=LRR receptor-like serine/threonine-protein kinase {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=LRR receptor-like serine/threonine-protein kinase At4g26540 {ECO:0000305};
DE   AltName: Full=Protein RECEPTOR OF RGF1 {ECO:0000303|PubMed:27229311};
DE   AltName: Full=Protein RGF1 INSENSITIVE 3 {ECO:0000303|PubMed:27229312};
DE   Flags: Precursor;
GN   Name=RGI3 {ECO:0000303|PubMed:27229312};
GN   Synonyms=RGFR1 {ECO:0000303|PubMed:27229311}; OrderedLocusNames=At4g26540;
GN   ORFNames=M3E9.30;
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE 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   [5]
RP   FUNCTION.
RX   PubMed=27229312; DOI=10.1038/cr.2016.63;
RA   Ou Y., Lu X., Zi Q., Xun Q., Zhang J., Wu Y., Shi H., Wei Z., Zhao B.,
RA   Zhang X., He K., Gou X., Li C., Li J.;
RT   "RGF1 INSENSITIVE 1 to 5, a group of LRR receptor-like kinases, are
RT   essential for the perception of root meristem growth factor 1 in
RT   Arabidopsis thaliana.";
RL   Cell Res. 26:686-698(2016).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 57-689, AND FUNCTION.
RX   PubMed=27229311; DOI=10.1038/cr.2016.62;
RA   Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA   Wen X., Li W., Han Z., Guo H., Chai J.;
RT   "Signature motif-guided identification of receptors for peptide hormones
RT   essential for root meristem growth.";
RL   Cell Res. 26:674-685(2016).
CC   -!- FUNCTION: Acts as receptor of RGF1, a peptide hormone that maintains
CC       the postembryonic root stem cell niche by regulating the expression
CC       levels and patterns of the transcription factor PLETHORA (PLT)
CC       (PubMed:27229312, PubMed:27229311). Links RGF1 signal with its
CC       downstream components (PubMed:27229311). {ECO:0000269|PubMed:27229311,
CC       ECO:0000269|PubMed:27229312}.
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   -!- INTERACTION:
CC       C0LGI5:At1g69990; NbExp=3; IntAct=EBI-20659695, EBI-20651225;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL32011.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA18216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA18216.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB79509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79509.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AL022223; CAA18216.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79509.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85216.1; -; Genomic_DNA.
DR   EMBL; AF436829; AAL32011.1; ALT_FRAME; mRNA.
DR   EMBL; FJ708754; ACN59348.1; -; mRNA.
DR   PIR; T05050; T05050.
DR   RefSeq; NP_567748.5; NM_118787.6.
DR   PDB; 5HYX; X-ray; 2.60 A; B=57-689.
DR   PDB; 5HZ0; X-ray; 2.56 A; B=57-689.
DR   PDB; 5HZ1; X-ray; 2.59 A; B=57-689.
DR   PDB; 5HZ3; X-ray; 2.86 A; B=57-689.
DR   PDBsum; 5HYX; -.
DR   PDBsum; 5HZ0; -.
DR   PDBsum; 5HZ1; -.
DR   PDBsum; 5HZ3; -.
DR   SMR; C0LGR3; -.
DR   BioGrid; 14047; 44.
DR   IntAct; C0LGR3; 44.
DR   STRING; 3702.AT4G26540.1; -.
DR   iPTMnet; C0LGR3; -.
DR   PaxDb; C0LGR3; -.
DR   PRIDE; C0LGR3; -.
DR   EnsemblPlants; AT4G26540.1; AT4G26540.1; AT4G26540.
DR   GeneID; 828760; -.
DR   Gramene; AT4G26540.1; AT4G26540.1; AT4G26540.
DR   KEGG; ath:AT4G26540; -.
DR   Araport; AT4G26540; -.
DR   TAIR; locus:2131518; AT4G26540.
DR   eggNOG; ENOG410IIZE; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   HOGENOM; HOG000116551; -.
DR   InParanoid; C0LGR3; -.
DR   OMA; WVREHVQ; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; C0LGR3; -.
DR   PRO; PR:C0LGR3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; C0LGR3; baseline and differential.
DR   Genevisible; C0LGR3; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010082; P:regulation of root meristem growth; IGI:TAIR.
DR   Gene3D; 3.80.10.10; -; 7.
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; PF13855; LRR_8; 3.
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; 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;
DR   PRODOM; C0LGR3.
DR   SWISS-2DPAGE; C0LGR3.
KW   3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW   Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1091
FT                   /note="LRR receptor-like serine/threonine-protein kinase"
FT                   /id="PRO_0000387553"
FT   TOPO_DOM        25..703
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        725..1091
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          33..56
FT                   /note="LRR 1"
FT   REPEAT          67..91
FT                   /note="LRR 2"
FT   REPEAT          92..115
FT                   /note="LRR 3"
FT   REPEAT          116..140
FT                   /note="LRR 4"
FT   REPEAT          142..166
FT                   /note="LRR 5"
FT   REPEAT          168..188
FT                   /note="LRR 6"
FT   REPEAT          190..213
FT                   /note="LRR 7"
FT   REPEAT          214..237
FT                   /note="LRR 8"
FT   REPEAT          239..261
FT                   /note="LRR 9"
FT   REPEAT          262..285
FT                   /note="LRR 10"
FT   REPEAT          287..309
FT                   /note="LRR 11"
FT   REPEAT          311..332
FT                   /note="LRR 12"
FT   REPEAT          333..357
FT                   /note="LRR 13"
FT   REPEAT          359..383
FT                   /note="LRR 14"
FT   REPEAT          385..405
FT                   /note="LRR 15"
FT   REPEAT          406..429
FT                   /note="LRR 16"
FT   REPEAT          431..453
FT                   /note="LRR 17"
FT   REPEAT          454..477
FT                   /note="LRR 18"
FT   REPEAT          478..501
FT                   /note="LRR 19"
FT   REPEAT          503..524
FT                   /note="LRR 20"
FT   REPEAT          525..548
FT                   /note="LRR 21"
FT   REPEAT          549..572
FT                   /note="LRR 22"
FT   REPEAT          574..596
FT                   /note="LRR 23"
FT   REPEAT          598..620
FT                   /note="LRR 24"
FT   REPEAT          621..644
FT                   /note="LRR 25"
FT   REPEAT          645..668
FT                   /note="LRR 26"
FT   REPEAT          669..690
FT                   /note="LRR 27"
FT   DOMAIN          760..1046
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         766..774
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        883
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         788
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         831
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         870
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         933
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        604
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        651
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        221
FT                   /note="L -> P (in Ref. 3; AAL32011)"
FT                   /evidence="ECO:0000305"
FT   STRAND          59..64
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          68..77
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          97..103
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           111..115
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          121..123
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           135..139
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          144..147
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           159..163
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          169..171
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          178..180
FT                   /evidence="ECO:0000244|PDB:5HYX"
FT   HELIX           183..187
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          193..195
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          201..205
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           208..212
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          218..220
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          223..228
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           232..236
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          242..244
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          247..250
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           256..260
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          266..268
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          271..274
FT                   /evidence="ECO:0000244|PDB:5HZ1"
FT   HELIX           280..284
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          290..292
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          299..301
FT                   /evidence="ECO:0000244|PDB:5HYX"
FT   HELIX           304..308
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          314..316
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          323..325
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           328..332
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          338..340
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          347..349
FT                   /evidence="ECO:0000244|PDB:5HZ3"
FT   HELIX           352..356
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          362..364
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           376..380
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          386..388
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          391..396
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           400..404
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          410..412
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          415..418
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           424..428
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          434..436
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          439..444
FT                   /evidence="ECO:0000244|PDB:5HZ1"
FT   HELIX           448..452
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          458..460
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          463..466
FT                   /evidence="ECO:0000244|PDB:5HZ1"
FT   HELIX           472..476
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          482..484
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          487..490
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           496..500
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          506..508
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           520..522
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          529..531
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          534..537
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          538..540
FT                   /evidence="ECO:0000244|PDB:5HZ3"
FT   HELIX           543..547
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          553..555
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           567..571
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          577..579
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          582..585
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          586..588
FT                   /evidence="ECO:0000244|PDB:5HZ1"
FT   HELIX           591..595
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          601..604
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          611..613
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           616..620
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          626..628
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           639..641
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          649..651
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          658..661
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           665..669
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   HELIX           672..676
FT                   /evidence="ECO:0000244|PDB:5HZ0"
FT   STRAND          678..683
FT                   /evidence="ECO:0000244|PDB:5HZ0"
SQ   SEQUENCE   1091 AA;  119529 MW;  061EFB0EDF281988 CRC64;
     MPPNIYRLSF FSSLLCFFFI PCFSLDQQGQ ALLSWKSQLN ISGDAFSSWH VADTSPCNWV
     GVKCNRRGEV SEIQLKGMDL QGSLPVTSLR SLKSLTSLTL SSLNLTGVIP KEIGDFTELE
     LLDLSDNSLS GDIPVEIFRL KKLKTLSLNT NNLEGHIPME IGNLSGLVEL MLFDNKLSGE
     IPRSIGELKN LQVLRAGGNK NLRGELPWEI GNCENLVMLG LAETSLSGKL PASIGNLKRV
     QTIAIYTSLL SGPIPDEIGY CTELQNLYLY QNSISGSIPT TIGGLKKLQS LLLWQNNLVG
     KIPTELGNCP ELWLIDFSEN LLTGTIPRSF GKLENLQELQ LSVNQISGTI PEELTNCTKL
     THLEIDNNLI TGEIPSLMSN LRSLTMFFAW QNKLTGNIPQ SLSQCRELQA IDLSYNSLSG
     SIPKEIFGLR NLTKLLLLSN DLSGFIPPDI GNCTNLYRLR LNGNRLAGSI PSEIGNLKNL
     NFVDISENRL VGSIPPAISG CESLEFLDLH TNSLSGSLLG TTLPKSLKFI DFSDNALSST
     LPPGIGLLTE LTKLNLAKNR LSGEIPREIS TCRSLQLLNL GENDFSGEIP DELGQIPSLA
     ISLNLSCNRF VGEIPSRFSD LKNLGVLDVS HNQLTGNLNV LTDLQNLVSL NISYNDFSGD
     LPNTPFFRRL PLSDLASNRG LYISNAISTR PDPTTRNSSV VRLTILILVV VTAVLVLMAV
     YTLVRARAAG KQLLGEEIDS WEVTLYQKLD FSIDDIVKNL TSANVIGTGS SGVVYRITIP
     SGESLAVKKM WSKEESGAFN SEIKTLGSIR HRNIVRLLGW CSNRNLKLLF YDYLPNGSLS
     SRLHGAGKGG CVDWEARYDV VLGVAHALAY LHHDCLPTII HGDVKAMNVL LGPHFEPYLA
     DFGLARTISG YPNTGIDLAK PTNRPPMAGS YGYMAPEHAS MQRITEKSDV YSYGVVLLEV
     LTGKHPLDPD LPGGAHLVKW VRDHLAEKKD PSRLLDPRLD GRTDSIMHEM LQTLAVAFLC
     VSNKANERPL MKDVVAMLTE IRHIDVGRSE TEKIKAGGCG SKEPQQFMSN EKIINSHGSS
     NCSFAFSDDS V
//

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