WAK1_ARATH
ID WAK1_ARATH Reviewed; 735 AA.
AC Q39191; O81820; Q56WT2; Q9LMP0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Wall-associated receptor kinase 1;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=WAK1; Synonyms=PRO25; OrderedLocusNames=At1g21250; ORFNames=F16F4.6;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10380805; DOI=10.1023/a:1006197318246;
RA He Z.-H., Cheeseman I., He D., Kohorn B.D.;
RT "A cluster of five cell wall-associated receptor kinase genes, Wak1-5, are
RT expressed in specific organs of Arabidopsis.";
RL Plant Mol. Biol. 39:1189-1196(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 50-735, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=1438303; DOI=10.1073/pnas.89.22.10989;
RA Kohorn B.D., Lane S., Smith T.A.;
RT "An Arabidopsis serine/threonine kinase homologue with an epidermal growth
RT factor repeat selected in yeast for its specificity for a thylakoid
RT membrane protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10989-10992(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 419-735.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8702686; DOI=10.1074/jbc.271.33.19789;
RA He Z.-H., Fujiki M., Kohorn B.D.;
RT "A cell wall-associated, receptor-like protein kinase.";
RL J. Biol. Chem. 271:19789-19793(1996).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9681026; DOI=10.1046/j.1365-313x.1998.00092.x;
RA He Z.-H., He D., Kohorn B.D.;
RT "Requirement for the induced expression of a cell wall associated receptor
RT kinase for survival during the pathogen response.";
RL Plant J. 14:55-63(1998).
RN [9]
RP INDUCTION.
RX PubMed=11027363; DOI=10.1073/pnas.97.21.11655;
RA Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T.,
RA Somerville S.C., Manners J.M.;
RT "Coordinated plant defense responses in Arabidopsis revealed by microarray
RT analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
RN [10]
RP INTERACTION WITH GRP3 AND GRP3S, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11335717; DOI=10.1074/jbc.m101283200;
RA Park A.R., Cho S.K., Yun U.J., Jin M.Y., Lee S.H., Sachetto-Martins G.,
RA Park O.K.;
RT "Interaction of the Arabidopsis receptor protein kinase Wak1 with a
RT glycine-rich protein, AtGRP-3.";
RL J. Biol. Chem. 276:26688-26693(2001).
RN [11]
RP FUNCTION, INDUCTION, DEVELOPMENTAL STAGE, AND BINDING TO PECTIN.
RX PubMed=11226187; DOI=10.2307/3871278;
RA Wagner T.A., Kohorn B.D.;
RT "Wall-associated kinases are expressed throughout plant development and are
RT required for cell expansion.";
RL Plant Cell 13:303-318(2001).
RN [12]
RP INTERACTION WITH KAPP.
RX PubMed=11554472; DOI=10.1023/a:1010691701578;
RA Anderson C.M., Wagner T.A., Perret M., He Z.-H., He D., Kohorn B.D.;
RT "WAKs: cell wall-associated kinases linking the cytoplasm to the
RT extracellular matrix.";
RL Plant Mol. Biol. 47:197-206(2001).
RN [13]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12068092; DOI=10.1104/pp.011028;
RA Verica J.A., He Z.-H.;
RT "The cell wall-associated kinase (WAK) and WAK-like kinase gene family.";
RL Plant Physiol. 129:455-459(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH OEE2.
RX PubMed=12767910; DOI=10.1016/s0006-291x(03)00851-9;
RA Yang E.J., Oh Y.A., Lee E.S., Park A.R., Cho S.K., Yoo Y.J., Park O.K.;
RT "Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich
RT protein 3/wall-associated kinase 1 in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 305:862-868(2003).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=12913180; DOI=10.1104/pp.103.022129;
RA Sivaguru M., Ezaki B., He Z.-H., Tong H.-Y., Osawa H., Baluska F.,
RA Volkmann D., Matsumoto H.;
RT "Aluminum-induced gene expression and protein localization of a cell wall-
RT associated receptor kinase in Arabidopsis.";
RL Plant Physiol. 132:2256-2266(2003).
RN [16]
RP BINDING TO PECTIN.
RX PubMed=15769808; DOI=10.1093/pcp/pci026;
RA Decreux A., Messiaen J.;
RT "Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-
RT induced conformation.";
RL Plant Cell Physiol. 46:268-278(2005).
RN [17]
RP BINDING TO PECTIN, AND MUTAGENESIS OF ARG-67; ARG-91; LYS-101; LYS-102 AND
RP ARG-166.
RX PubMed=16631829; DOI=10.1016/j.phytochem.2006.03.009;
RA Decreux A., Thomas A., Spies B., Brasseur R., Van Cutsem P., Messiaen J.;
RT "In vitro characterization of the homogalacturonan-binding domain of the
RT wall-associated kinase WAK1 using site-directed mutagenesis.";
RL Phytochemistry 67:1068-1079(2006).
CC -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC signaling receptor of extracellular matrix component. Binding to pectin
CC may have significance in the control of cell expansion, morphogenesis
CC and development. Required during plant's response to pathogen infection
CC and in plant defense against heavy metal toxicity. Phosphorylates the
CC oxygen-evolving enhancer protein 2 (OEE2) in an GRP-3-dependent manner.
CC {ECO:0000269|PubMed:11226187, ECO:0000269|PubMed:12767910,
CC ECO:0000269|PubMed:12913180}.
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;
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 -!- SUBUNIT: Interacts with the glycine-rich proteins GRP3 and GRP3S, and
CC the type 2C protein phosphatase KAPP. Component of a 500 kDa complex,
CC composed of WAK1, GRP3 and KAPP. Interacts with the oxygen-evolving
CC enhancer protein 2 (OEE2). {ECO:0000269|PubMed:11335717,
CC ECO:0000269|PubMed:11554472, ECO:0000269|PubMed:12767910}.
CC -!- INTERACTION:
CC Q39191; Q9SL15: GRP3; NbExp=5; IntAct=EBI-2320121, EBI-1541435;
CC Q39191; Q9ZSJ6: GRP3S; NbExp=2; IntAct=EBI-2320121, EBI-2319984;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8702686}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:8702686}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in green tissues such as
CC stems and leaves. Detected at organ junctions.
CC {ECO:0000269|PubMed:10380805, ECO:0000269|PubMed:11335717,
CC ECO:0000269|PubMed:1438303, ECO:0000269|PubMed:9681026}.
CC -!- DEVELOPMENTAL STAGE: Expressed in shoot and root apical meristems, and
CC in expanding leaves and sepals. {ECO:0000269|PubMed:11226187}.
CC -!- INDUCTION: Induced by salicylic acid (SA) or INA, methyl jasmonate,
CC ethylene, wounding and pathogen infection. Accumulated in roots after
CC Aluminum exposure. Up-regulated by GRP3. {ECO:0000269|PubMed:10380805,
CC ECO:0000269|PubMed:11027363, ECO:0000269|PubMed:11226187,
CC ECO:0000269|PubMed:11335717, ECO:0000269|PubMed:12913180,
CC ECO:0000269|PubMed:9681026}.
CC -!- MISCELLANEOUS: Binding to polygalacturonic acid (PGA) multimers is
CC calcium-dependent.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32844.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF81356.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ009696; CAA08794.1; -; Genomic_DNA.
DR EMBL; AC036104; AAF81356.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30079.1; -; Genomic_DNA.
DR EMBL; AY039917; AAK64021.1; -; mRNA.
DR EMBL; BT001967; AAN71966.1; -; mRNA.
DR EMBL; L04999; AAA32844.1; ALT_FRAME; mRNA.
DR EMBL; AK221950; BAD94420.1; -; mRNA.
DR PIR; H86345; A46373.
DR RefSeq; NP_564137.1; NM_101978.5.
DR AlphaFoldDB; Q39191; -.
DR SMR; Q39191; -.
DR BioGRID; 23960; 3.
DR IntAct; Q39191; 3.
DR STRING; 3702.AT1G21250.1; -.
DR iPTMnet; Q39191; -.
DR PaxDb; Q39191; -.
DR PRIDE; Q39191; -.
DR ProteomicsDB; 242652; -.
DR EnsemblPlants; AT1G21250.1; AT1G21250.1; AT1G21250.
DR GeneID; 838721; -.
DR Gramene; AT1G21250.1; AT1G21250.1; AT1G21250.
DR KEGG; ath:AT1G21250; -.
DR Araport; AT1G21250; -.
DR TAIR; locus:2014902; AT1G21250.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR InParanoid; Q39191; -.
DR OMA; VISATWI; -.
DR OrthoDB; 496739at2759; -.
DR PhylomeDB; Q39191; -.
DR PRO; PR:Q39191; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39191; baseline and differential.
DR Genevisible; Q39191; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
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:0007166; P:cell surface receptor signaling pathway; IPI:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..735
FT /note="Wall-associated receptor kinase 1"
FT /id="PRO_0000253300"
FT TOPO_DOM 25..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 234..281
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 282..328
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..692
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 67..254
FT /note="Polygalacturonic acid-binding"
FT ACT_SITE 534
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 415..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 482
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 581
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 238..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 247..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 266..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 286..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 297..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 314..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 67
FT /note="R->Q: Decreases the binding to dimeric PGA; when
FT associated with T-101 and T-102."
FT /evidence="ECO:0000269|PubMed:16631829"
FT MUTAGEN 91
FT /note="R->Q: Decreases the binding to dimeric PGA; when
FT associated with Q-166. Decreases the binding to multimeric
FT PGA; when associated with T-101; T-102 and Q-166."
FT /evidence="ECO:0000269|PubMed:16631829"
FT MUTAGEN 101
FT /note="K->T: Decreases the binding to dimeric PGA; when
FT associated with Q-67 and T-102. Abolishes the binding to
FT dimeric PGA; when associated with T-102 and Q-166."
FT /evidence="ECO:0000269|PubMed:16631829"
FT MUTAGEN 102
FT /note="K->T: Decreases the binding to dimeric PGA; when
FT associated with Q-67 and T-101. Abolishes the binding to
FT dimeric PGA; when associated with T-101 and Q-166."
FT /evidence="ECO:0000269|PubMed:16631829"
FT MUTAGEN 166
FT /note="R->Q: Decreases the binding to dimeric PGA; when
FT associated with Q-91. Abolishes the binding to dimeric PGA;
FT when associated with T-101 and T-202."
FT /evidence="ECO:0000269|PubMed:16631829"
FT CONFLICT 212
FT /note="S -> C (in Ref. 5; AAA32844)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="T -> I (in Ref. 5; AAA32844)"
FT /evidence="ECO:0000305"
FT CONFLICT 386..387
FT /note="Missing (in Ref. 5; AAA32844)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="S -> P (in Ref. 5; AAA32844)"
FT /evidence="ECO:0000305"
FT CONFLICT 663..668
FT /note="RLMGEE -> TNGRG (in Ref. 5; AAA32844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 81211 MW; AAD41A28296093E6 CRC64;
MKVQEGLFLV AIFFSLACTQ LVKGQHQPGE NCQNKCGNIT IEYPFGISSG CYYPGNESFS
ITCKEDRPHV LSDIEVANFN HSGQLQVLLN RSSTCYDEQG KKTEEDSSFT LENLSLSANN
KLTAVGCNAL SLLDTFGMQN YSTACLSLCD SPPEADGECN GRGCCRVDVS APLDSYTFET
TSGRIKHMTS FHDFSPCTYA FLVEDDKFNF SSTEDLLNLR NVMRFPVLLD WSVGNQTCEQ
VGSTSICGGN STCLDSTPRN GYICRCNEGF DGNPYLSAGC QDVNECTTSS TIHRHNCSDP
KTCRNKVGGF YCKCQSGYRL DTTTMSCKRK EFAWTTILLV TTIGFLVILL GVACIQQRMK
HLKDTKLREQ FFEQNGGGML TQRLSGAGPS NVDVKIFTED GMKKATNGYA ESRILGQGGQ
GTVYKGILPD NSIVAIKKAR LGDSSQVEQF INEVLVLSQI NHRNVVKLLG CCLETEVPLL
VYEFITNGTL FDHLHGSMID SSLTWEHRLK IAIEVAGTLA YLHSSASIPI IHRDIKTANI
LLDVNLTAKV ADFGASRLIP MDKEELETMV QGTLGYLDPE YYNTGLLNEK SDVYSFGVVL
MELLSGQKAL CFKRPQSSKH LVSYFATATK ENRLDEIIGG EVMNEDNLKE IQEAARIAAE
CTRLMGEERP RMKEVAAKLE ALRVEKTKHK WSDQYPEENE HLIGGHILSA QGETSSSIGY
DSIKNVAILD IETGR
