TMK1_ARATH
ID TMK1_ARATH Reviewed; 942 AA.
AC P43298; C0LGH9; Q84R13;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Receptor protein kinase TMK1 {ECO:0000303|PubMed:1332795};
DE EC=2.7.11.1 {ECO:0000269|PubMed:1332795};
DE AltName: Full=BARK1-like kinase 1 {ECO:0000303|PubMed:23921992};
DE AltName: Full=Transmembrane kinase 1 {ECO:0000303|PubMed:1332795};
DE Flags: Precursor;
GN Name=TMK1 {ECO:0000303|PubMed:1332795};
GN Synonyms=BLK1 {ECO:0000303|PubMed:23921992};
GN OrderedLocusNames=At1g66150 {ECO:0000312|Araport:AT1G66150};
GN ORFNames=F15E12.4 {ECO:0000312|EMBL:AAG51302.1};
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=1332795; DOI=10.2307/3869412;
RA Chang C., Schaller G.E., Patterson S.E., Kwok S.F., Meyerowitz E.M.,
RA Bleecker A.B.;
RT "The TMK1 gene from Arabidopsis codes for a protein with structural and
RT biochemical characteristics of a receptor protein kinase.";
RL Plant Cell 4:1263-1271(1992).
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=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 [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;
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND GLYCOSYLATION.
RX PubMed=8224199; DOI=10.1016/0014-5793(93)80676-l;
RA Schaller G.E., Bleecker A.B.;
RT "Receptor-like kinase activity in membranes of Arabidopsis thaliana.";
RL FEBS Lett. 333:306-310(1993).
RN [8]
RP GENE FAMILY.
RX PubMed=12972053; DOI=10.1016/s1369-5266(03)00089-x;
RA Dievart A., Clark S.E.;
RT "Using mutant alleles to determine the structure and function of leucine-
RT rich repeat receptor-like kinases.";
RL Curr. Opin. Plant Biol. 6:507-516(2003).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23613767; DOI=10.1371/journal.pone.0060990;
RA Dai N., Wang W., Patterson S.E., Bleecker A.B.;
RT "The TMK subfamily of receptor-like kinases in Arabidopsis display an
RT essential role in growth and a reduced sensitivity to auxin.";
RL PLoS ONE 8:E60990-E60990(2013).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23921992; DOI=10.1093/pcp/pct106;
RA Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y.,
RA Kim S.H.;
RT "Identification of Arabidopsis BAK1-associating receptor-like kinase 1
RT (BARK1) and characterization of its gene expression and brassinosteroid-
RT regulated root phenotypes.";
RL Plant Cell Physiol. 54:1620-1634(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ABP1.
RX PubMed=24578577; DOI=10.1126/science.1245125;
RA Xu T., Dai N., Chen J., Nagawa S., Cao M., Li H., Zhou Z., Chen X.,
RA De Rycke R., Rakusova H., Wang W., Jones A.M., Friml J., Patterson S.E.,
RA Bleecker A.B., Yang Z.;
RT "Cell surface ABP1-TMK auxin-sensing complex activates ROP GTPase
RT signaling.";
RL Science 343:1025-1028(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-469, GLYCOSYLATION AT ASN-158
RP AND ASN-285, DISULFIDE BOND, AND DOMAIN.
RX PubMed=23147790; DOI=10.1038/cr.2012.159;
RA Liu P., Hu Z., Zhou B., Liu S., Chai J.;
RT "Crystal structure of an LRR protein with two solenoids.";
RL Cell Res. 23:303-305(2013).
CC -!- FUNCTION: Transmembrane kinase receptor (PubMed:1332795).
CC Phosphorylates only serine and threonine residues (PubMed:8224199).
CC Involved in auxin signal transduction and cell expansion and
CC proliferation regulation (PubMed:23613767). Forms with ABP1 a cell
CC surface auxin perception complex that activates ROP signaling pathways
CC (PubMed:24578577). Required for auxin promotion of pavement cell
CC interdigitation (PubMed:24578577). Auxin promotes the formation of the
CC ABP1-TMK1 protein complex (PubMed:24578577).
CC {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577,
CC ECO:0000269|PubMed:8224199, ECO:0000303|PubMed:1332795}.
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 Evidence={ECO:0000269|PubMed:1332795, ECO:0000269|PubMed:8224199};
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; Evidence={ECO:0000269|PubMed:1332795,
CC ECO:0000269|PubMed:8224199};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8224199};
CC -!- SUBUNIT: Interacts (via extracellular domain) with ABP1.
CC {ECO:0000269|PubMed:24578577}.
CC -!- INTERACTION:
CC P43298; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-2023970, EBI-16954682;
CC P43298; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-2023970, EBI-20651261;
CC P43298; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-2023970, EBI-20651541;
CC P43298; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-2023970, EBI-16946048;
CC P43298; Q9SUQ3: At4g23740; NbExp=3; IntAct=EBI-2023970, EBI-16912451;
CC P43298; C0LGR9: At4g31250; NbExp=2; IntAct=EBI-2023970, EBI-16955262;
CC P43298; Q9FMD7: At5g16590; NbExp=2; IntAct=EBI-2023970, EBI-16903983;
CC P43298; Q9FL63: At5g24100; NbExp=3; IntAct=EBI-2023970, EBI-20657062;
CC P43298; C0LGU5: At5g45780; NbExp=3; IntAct=EBI-2023970, EBI-16964970;
CC P43298; P33487: ERABP1; NbExp=3; IntAct=EBI-2023970, EBI-16094614;
CC P43298; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-2023970, EBI-16905069;
CC P43298; C0LGU7: MDIS1; NbExp=2; IntAct=EBI-2023970, EBI-16196163;
CC P43298; Q9XIC7: SERK2; NbExp=3; IntAct=EBI-2023970, EBI-6299033;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23613767,
CC ECO:0000269|PubMed:24578577}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques and
CC flowers. {ECO:0000269|PubMed:1332795, ECO:0000269|PubMed:23613767}.
CC -!- DOMAIN: The leucine-rich repeat (LRR) domain is disrupted by a non-LRR
CC region, resulting in the formation of two LRR solenoid structures
CC shaped like the Arabic number '7'. This is strikingly different from
CC the horseshoe structures of the canonical LRR proteins.
CC {ECO:0000269|PubMed:23147790}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:1332795}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8224199}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23613767). Tmk1 and
CC tmk2 double mutants, tmk1 and tmk3 double mutants and tmk1, tmk2 and
CC tmk3 triple mutants have no visible phenotypes (PubMed:23613767). Tmk1
CC and tmk4 double mutants, tmk1, tmk2 and tmk4 triple mutants and tmk1,
CC tmk3 and tmk4 triple mutants have a severe reduction in organ size, a
CC substantial delay in growth and development, and a decrease in
CC fertility (PubMed:23613767). Tmk1, tmk2, tmk3 and tmk4 quadruple
CC mutants are embryo lethal (PubMed:23613767, PubMed:24578577).
CC {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; L00670; AAA32876.1; -; Genomic_DNA.
DR EMBL; FJ708669; ACN59264.1; -; mRNA.
DR EMBL; AC026480; AAG51302.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34468.1; -; Genomic_DNA.
DR EMBL; BT006178; AAP04161.1; -; mRNA.
DR EMBL; AK228659; BAF00566.1; -; mRNA.
DR PIR; JQ1674; JQ1674.
DR RefSeq; NP_176789.1; NM_105286.4.
DR PDB; 4HQ1; X-ray; 1.55 A; A=1-469.
DR PDBsum; 4HQ1; -.
DR AlphaFoldDB; P43298; -.
DR SMR; P43298; -.
DR BioGRID; 28151; 26.
DR DIP; DIP-46512N; -.
DR IntAct; P43298; 39.
DR STRING; 3702.AT1G66150.1; -.
DR iPTMnet; P43298; -.
DR PaxDb; P43298; -.
DR PRIDE; P43298; -.
DR ProteomicsDB; 228452; -.
DR EnsemblPlants; AT1G66150.1; AT1G66150.1; AT1G66150.
DR GeneID; 842930; -.
DR Gramene; AT1G66150.1; AT1G66150.1; AT1G66150.
DR KEGG; ath:AT1G66150; -.
DR Araport; AT1G66150; -.
DR TAIR; locus:2013825; AT1G66150.
DR eggNOG; ENOG502QPQ4; Eukaryota.
DR HOGENOM; CLU_000288_114_6_1; -.
DR InParanoid; P43298; -.
DR OMA; DPCADWI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; P43298; -.
DR PRO; PR:P43298; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P43298; baseline and differential.
DR Genevisible; P43298; AT.
DR GO; GO:0005576; C:extracellular region; ISS:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IDA:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
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; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 7.
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; Disulfide bond; Glycoprotein;
KW Kinase; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..942
FT /note="Receptor protein kinase TMK1"
FT /id="PRO_0000024388"
FT TOPO_DOM 24..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..942
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 63..87
FT /note="LRR 1"
FT /evidence="ECO:0000305"
FT REPEAT 88..110
FT /note="LRR 2"
FT /evidence="ECO:0000305"
FT REPEAT 111..133
FT /note="LRR 3"
FT /evidence="ECO:0000305"
FT REPEAT 135..159
FT /note="LRR 4"
FT /evidence="ECO:0000305"
FT REPEAT 161..182
FT /note="LRR 5"
FT /evidence="ECO:0000305"
FT REPEAT 185..209
FT /note="LRR 6"
FT /evidence="ECO:0000305"
FT REPEAT 211..231
FT /note="LRR 7"
FT /evidence="ECO:0000305"
FT REPEAT 232..253
FT /note="LRR 8"
FT /evidence="ECO:0000305"
FT REPEAT 254..278
FT /note="LRR 9"
FT /evidence="ECO:0000305"
FT REPEAT 280..300
FT /note="LRR 10"
FT /evidence="ECO:0000305"
FT REPEAT 361..384
FT /note="LRR 11"
FT /evidence="ECO:0000305"
FT REPEAT 385..408
FT /note="LRR 12"
FT /evidence="ECO:0000305"
FT REPEAT 409..436
FT /note="LRR 13"
FT /evidence="ECO:0000305"
FT DOMAIN 588..869
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 437..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 594..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23147790"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23147790"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..60
FT /evidence="ECO:0000269|PubMed:23147790"
FT DISULFID 314..321
FT /evidence="ECO:0000269|PubMed:23147790"
FT DISULFID 351..359
FT /evidence="ECO:0000269|PubMed:23147790"
FT CONFLICT 849
FT /note="A -> S (in Ref. 3; BAF00566 and 5; AAP04161)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="S -> G (in Ref. 2; ACN59264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 102388 MW; 93E300B52FF549DE CRC64;
MKKRRTFLLF SFTFLLLLSL SKADSDGDLS AMLSLKKSLN PPSSFGWSDP DPCKWTHIVC
TGTKRVTRIQ IGHSGLQGTL SPDLRNLSEL ERLELQWNNI SGPVPSLSGL ASLQVLMLSN
NNFDSIPSDV FQGLTSLQSV EIDNNPFKSW EIPESLRNAS ALQNFSANSA NVSGSLPGFL
GPDEFPGLSI LHLAFNNLEG ELPMSLAGSQ VQSLWLNGQK LTGDITVLQN MTGLKEVWLH
SNKFSGPLPD FSGLKELESL SLRDNSFTGP VPASLLSLES LKVVNLTNNH LQGPVPVFKS
SVSVDLDKDS NSFCLSSPGE CDPRVKSLLL IASSFDYPPR LAESWKGNDP CTNWIGIACS
NGNITVISLE KMELTGTISP EFGAIKSLQR IILGINNLTG MIPQELTTLP NLKTLDVSSN
KLFGKVPGFR SNVVVNTNGN PDIGKDKSSL SSPGSSSPSG GSGSGINGDK DRRGMKSSTF
IGIIVGSVLG GLLSIFLIGL LVFCWYKKRQ KRFSGSESSN AVVVHPRHSG SDNESVKITV
AGSSVSVGGI SDTYTLPGTS EVGDNIQMVE AGNMLISIQV LRSVTNNFSS DNILGSGGFG
VVYKGELHDG TKIAVKRMEN GVIAGKGFAE FKSEIAVLTK VRHRHLVTLL GYCLDGNEKL
LVYEYMPQGT LSRHLFEWSE EGLKPLLWKQ RLTLALDVAR GVEYLHGLAH QSFIHRDLKP
SNILLGDDMR AKVADFGLVR LAPEGKGSIE TRIAGTFGYL APEYAVTGRV TTKVDVYSFG
VILMELITGR KSLDESQPEE SIHLVSWFKR MYINKEASFK KAIDTTIDLD EETLASVHTV
AELAGHCCAR EPYQRPDMGH AVNILSSLVE LWKPSDQNPE DIYGIDLDMS LPQALKKWQA
YEGRSDLESS TSSLLPSLDN TQMSIPTRPY GFAESFTSVD GR
