SD129_ARATH
ID SD129_ARATH Reviewed; 805 AA.
AC O64782; Q8LEY0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SD1-29 {ECO:0000305};
DE EC=2.7.12.1 {ECO:0000269|PubMed:31922267};
DE AltName: Full=Protein LIPOOLIGOSACCHARIDE-SPECIFIC REDUCED ELICITATION {ECO:0000303|PubMed:31922267};
DE AltName: Full=S-domain-1 (SD1) receptor kinase 29 {ECO:0000303|PubMed:18552232};
DE Short=SD1-29 {ECO:0000303|PubMed:18552232};
DE Flags: Precursor;
GN Name=SD129 {ECO:0000303|PubMed:18552232};
GN Synonyms=LORE {ECO:0000303|PubMed:31922267};
GN OrderedLocusNames=At1g61380 {ECO:0000312|EMBL:AEE33829.1};
GN ORFNames=T1F9.13 {ECO:0000312|EMBL:AAC13903.1};
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 [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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, NOMENCLATURE, AND INTERACTION WITH PUB9; PUB13; PUB14; PUB29;
RP PUB38; PUB44 AND PUB45.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25729922; DOI=10.1038/ni.3124;
RA Ranf S., Gisch N., Schaeffer M., Illig T., Westphal L., Knirel Y.A.,
RA Sanchez-Carballo P.M., Zaehringer U., Hueckelhoven R., Lee J., Scheel D.;
RT "A lectin S-domain receptor kinase mediates lipopolysaccharide sensing in
RT Arabidopsis thaliana.";
RL Nat. Immunol. 16:426-433(2015).
RN [7]
RP FUNCTION.
RX PubMed=29431629; DOI=10.1104/pp.17.01637;
RA Shang-Guan K., Wang M., Htwe N.M.P.S., Li P., Li Y., Qi F., Zhang D.,
RA Cao M., Kim C., Weng H., Cen H., Black I.M., Azadi P., Carlson R.W.,
RA Stacey G., Liang Y.;
RT "Lipopolysaccharides trigger two successive bursts of reactive oxygen
RT species at distinct cellular locations.";
RL Plant Physiol. 176:2543-2556(2018).
RN [8]
RP INDUCTION.
RX PubMed=30940349; DOI=10.1016/j.bbrc.2019.03.170;
RA Djami-Tchatchou A.T., Dubery I.A.;
RT "miR393 regulation of lectin receptor-like kinases associated with LPS
RT perception in Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 513:88-92(2019).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PBL34; PBL35 AND PBL36,
RP PHOSPHORYLATION AT TYR-600, AND MUTAGENESIS OF LYS-516; TYR-600 AND
RP ASP-613.
RX PubMed=31922267; DOI=10.15252/embj.2019102856;
RA Luo X., Wu W., Liang Y., Xu N., Wang Z., Zou H., Liu J.;
RT "Tyrosine phosphorylation of the lectin receptor-like kinase LORE regulates
RT plant immunity.";
RL EMBO J. 39:e102856-e102856(2020).
CC -!- FUNCTION: S-domain receptor protein kinase involved in
CC lipopolysaccharide (LPS) sensing (PubMed:25729922, PubMed:29431629,
CC PubMed:31922267). Specifically detects LPS of Pseudomonas and
CC Xanthomonas species (PubMed:25729922). LPS are major components of the
CC outer membrane of Gram-negative bacteria and are important microbe-
CC associated molecular patterns (MAMPs) that trigger biphasic production
CC of reactive oxygen species (ROS) and immune responses in plants
CC (PubMed:25729922, PubMed:29431629). Seems to be only partially
CC associated with the second LPS-triggered ROS burst (PubMed:29431629).
CC Mediates defense signaling in response to the medium-chain 3-hydroxy
CC fatty acid 3-OH-C10:0, a pathogen-associated molecular pattern (PAMP)
CC which induces autophosphorylation at Tyr-600 (PubMed:31922267).
CC Autophosphorylation at Tyr-600 is required for downstream
CC phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35
CC and PBL36, and activation of plant immunity (PubMed:31922267).
CC {ECO:0000269|PubMed:25729922, ECO:0000269|PubMed:29431629,
CC ECO:0000269|PubMed:31922267}.
CC -!- FUNCTION: (Microbial infection) Targeted by the bacterial type III
CC effector protein tyrosine phosphatase HopAO1 from Pseudomonas syringae
CC (PubMed:31922267). HopAO1 dephosphorylates Tyr-600, which suppresses
CC the immune response (PubMed:31922267). {ECO:0000269|PubMed:31922267}.
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:31922267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:31922267};
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=2.7.12.1; Evidence={ECO:0000269|PubMed:31922267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:31922267};
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:31922267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC Evidence={ECO:0000269|PubMed:31922267};
CC -!- SUBUNIT: Interacts with PUB9, PUB13, PUB14, PUB29, PUB38, PUB44 and
CC PUB45 (PubMed:18552232). Interacts with PBL34, PBL35 and PBL36
CC (PubMed:31922267). {ECO:0000269|PubMed:18552232,
CC ECO:0000269|PubMed:31922267}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25729922,
CC ECO:0000269|PubMed:31922267}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Repressed by miR393a (microRNA) in response to bacterial
CC lipopolysaccharides (LPS) treatment. {ECO:0000269|PubMed:29431629}.
CC -!- PTM: Autophosphorylated at Tyr-600 (PubMed:31922267).
CC Autophosphorylation at Tyr-600 is required for downstream
CC phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35
CC and PBL36, and activation of plant immunity (PubMed:31922267).
CC {ECO:0000269|PubMed:31922267}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are hyper-susceptible to infection by the
CC bacterial pathogen Pseudomonas syringae. {ECO:0000269|PubMed:25729922}.
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; AC004255; AAC13903.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33829.1; -; Genomic_DNA.
DR EMBL; AY090241; AAL90905.1; -; mRNA.
DR EMBL; BT000638; AAN18204.1; -; mRNA.
DR EMBL; AY085162; AAM61715.1; -; mRNA.
DR RefSeq; NP_564775.1; NM_104819.2.
DR AlphaFoldDB; O64782; -.
DR SMR; O64782; -.
DR STRING; 3702.AT1G61380.1; -.
DR PaxDb; O64782; -.
DR PRIDE; O64782; -.
DR ProteomicsDB; 232752; -.
DR EnsemblPlants; AT1G61380.1; AT1G61380.1; AT1G61380.
DR GeneID; 842432; -.
DR Gramene; AT1G61380.1; AT1G61380.1; AT1G61380.
DR KEGG; ath:AT1G61380; -.
DR Araport; AT1G61380; -.
DR TAIR; locus:2197729; AT1G61380.
DR HOGENOM; CLU_000288_116_1_1; -.
DR InParanoid; O64782; -.
DR OMA; CQANSQG; -.
DR OrthoDB; 407794at2759; -.
DR PhylomeDB; O64782; -.
DR PRO; PR:O64782; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64782; baseline and differential.
DR Genevisible; O64782; 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:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; IMP:TAIR.
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; IDA:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0032497; P:detection of lipopolysaccharide; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..805
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase SD1-29"
FT /id="PRO_0000401302"
FT TOPO_DOM 22..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..141
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 277..313
FT /note="EGF-like"
FT DOMAIN 332..418
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 488..773
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 577..594
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 613
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 494..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 600
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:31922267"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 281..293
FT /evidence="ECO:0000250"
FT DISULFID 287..301
FT /evidence="ECO:0000250"
FT DISULFID 371..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 375..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT MUTAGEN 516
FT /note="K->E: Loss of autophosphorylation; when associated
FT with V-613."
FT /evidence="ECO:0000269|PubMed:31922267"
FT MUTAGEN 600
FT /note="Y->F: Unable to phosphorylate PBL34."
FT MUTAGEN 613
FT /note="D->V: Loss of autophosphorylation; when associated
FT with E-516."
FT /evidence="ECO:0000269|PubMed:31922267"
FT CONFLICT 53
FT /note="Q -> R (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="Q -> E (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> S (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> Q (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="K -> Q (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="N -> D (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="F -> I (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="D -> N (in Ref. 4; AAM61715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 89897 MW; 52CDD70D3B575B78 CRC64;
MGMVLFACLL LLIIFPTCGY AAINTSSPLS IRQTLSSPGG FYELGFFSPN NTQNQYVGIW
FKKIVPRVVV WVANRDTPVT SSAANLTISS NGSLILLDGK QDVIWSTGKA FTSNKCHAEL
LDTGNFVVID DVSGNKLWQS FEHLGNTMLP QSSLMYDTSN GKKRVLTTWK SNSDPSPGEF
SLEITPQIPT QGLIRRGSVP YWRCGPWAKT RFSGISGIDA SYVSPFSVVQ DTAAGTGSFS
YSTLRNYNLS YVTLTPEGKM KILWDDGNNW KLHLSLPENP CDLYGRCGPY GLCVRSDPPK
CECLKGFVPK SDEEWGKGNW TSGCVRRTKL SCQAKSSMKT QGKDTDIFYR MTDVKTPDLH
QFASFLNAEQ CYQGCLGNCS CTAFAYISGI GCLVWNGELA DTVQFLSSGE FLFIRLASSE
LAGSSRRKII VGTTVSLSIF LILVFAAIML WRYRAKQNDA WKNGFERQDV SGVNFFEMHT
IRTATNNFSP SNKLGQGGFG PVYKGKLVDG KEIGVKRLAS SSGQGTEEFM NEITLISKLQ
HRNLVRLLGY CIDGEEKLLI YEFMVNKSLD IFIFDPCLKF ELDWPKRFNI IQGIARGLLY
LHRDSRLRVI HRDLKVSNIL LDDRMNPKIS DFGLARMFQG TQYQDNTRRV VGTLGYMSPE
YAWAGLFSEK SDIYSFGVLM LEIISGKRIS RFIYGDESKG LLAYTWDSWC ETGGSNLLDR
DLTDTCQAFE VARCVQIGLL CVQHEAVDRP NTLQVLSMLT SATDLPVPKQ PIFAVHTLND
MPMLQANSQD FLSVNEMTES MIQGR
