ANXD1_ARATH
ID ANXD1_ARATH Reviewed; 317 AA.
AC Q9SYT0; Q39001; Q42023; Q56Y94; Q96527;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Annexin D1;
DE AltName: Full=AnnAt1;
DE AltName: Full=Annexin A1;
GN Name=ANN1; Synonyms=ANNAT1, ANX23-ATH, ATOXY5, OXY5;
GN OrderedLocusNames=At1g35720; ORFNames=F14D7.2;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Seedling;
RX PubMed=8855345; DOI=10.1073/pnas.93.20.11268;
RA Gidrol X., Sabelli P.A., Fern Y.S., Kush A.K.;
RT "Annexin-like protein from Arabidopsis thaliana rescues delta oxyR mutant
RT of Escherichia coli from H2O2 stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11268-11273(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Clark G.B., Roux S.J.;
RT "Isolation and characterization of two different Arabidopsis annexin
RT cDNAs.";
RL (er) Plant Gene Register PGR99-065(1999).
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].
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-317.
RA Schantz R., Schantz M.L., Houlne G.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-87.
RC STRAIN=cv. Columbia;
RA Berthomieu P., Guerrier D., Giraudat J.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-317.
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 [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11457958; DOI=10.1104/pp.126.3.1072;
RA Clark G.B., Sessions A., Eastburn D.J., Roux S.J.;
RT "Differential expression of members of the annexin multigene family in
RT Arabidopsis.";
RL Plant Physiol. 126:1072-1084(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15161963; DOI=10.1105/tpc.021683;
RA Lee S., Lee E.J., Yang E.J., Lee J.E., Park A.R., Song W.H., Park O.K.;
RT "Proteomic identification of annexins, calcium-dependent membrane binding
RT proteins that mediate osmotic stress and abscisic acid signal transduction
RT in Arabidopsis.";
RL Plant Cell 16:1378-1391(2004).
RN [12]
RP FUNCTION, MUTAGENESIS OF HIS-40, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=16153598; DOI=10.1016/j.bbrc.2005.08.181;
RA Gorecka K.M., Konopka-Postupolska D., Hennig J., Buchet R., Pikula S.;
RT "Peroxidase activity of annexin 1 from Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 336:868-875(2005).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15368128; DOI=10.1007/s00425-004-1374-7;
RA Clark G.B., Lee D., Dauwalder M., Roux S.J.;
RT "Immunolocalization and histochemical evidence for the association of two
RT different Arabidopsis annexins with secretion during early seedling growth
RT and development.";
RL Planta 220:621-631(2005).
RN [14]
RP INDUCTION, AND GENE FAMILY.
RX PubMed=16531057; DOI=10.1016/j.plaphy.2006.02.002;
RA Cantero A., Barthakur S., Bushart T.J., Chou S., Morgan R.O.,
RA Fernandez M.P., Clark G.B., Roux S.J.;
RT "Expression profiling of the Arabidopsis annexin gene family during
RT germination, de-etiolation and abiotic stress.";
RL Plant Physiol. Biochem. 44:13-24(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-102;
RP THR-112; SER-155; TYR-156; TYR-284 AND SER-289.
RX PubMed=26452715; DOI=10.1016/j.febslet.2015.09.025;
RA Kim D., Ntui V.O., Zhang N., Xiong L.;
RT "Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase.";
RL FEBS Lett. 589:3321-3327(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 2-317.
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of gene product of annexin from Arabidopsis thaliana gene
RT At1g35720.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Has a peroxidase activity. May act in counteracting oxidative
CC stress. May also mediate regulated, targeted secretion of Golgi-derived
CC vesicles during seedling development. {ECO:0000269|PubMed:15368128,
CC ECO:0000269|PubMed:16153598}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at pH 7.0 and 9.0, but not at pH 5.5.
CC {ECO:0000269|PubMed:16153598};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:16153598}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=translocate
CC from cytosol to membrane upon salt treatment; this translocation is
CC calcium dependent.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in stems.
CC {ECO:0000269|PubMed:15368128, ECO:0000269|PubMed:8855345}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the elongation zone of the root and
CC in the root cap in germinating seedlings. Expressed later in the
CC internal cells of the root and in the epidermal cells and the vascular
CC tissue of the hypocotyl. By day 7, expressed in the initiating
CC trichomes on leaf primordia and in the vasculature of hypocotyl and
CC cotyledon. At the transition to reproductive growth (day 14), expressed
CC in the vasculature, epidermis, basal mesophyll cells and pith meristem
CC of leaves. {ECO:0000269|PubMed:11457958, ECO:0000269|PubMed:15368128}.
CC -!- INDUCTION: Up-regulated by cold, dehydration, salt, osmotic and
CC oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic
CC acid (SA). {ECO:0000269|PubMed:15161963, ECO:0000269|PubMed:16531057,
CC ECO:0000269|PubMed:8855345}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- PTM: Phosphorylated.
CC -!- DISRUPTION PHENOTYPE: Plants are hypersensitive to osmotic stress and
CC abscisic acid (ABA) during germination and early seedling growth.
CC {ECO:0000269|PubMed:15161963}.
CC -!- MISCELLANEOUS: Binds lipids at millimolar calcium concentration.
CC -!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family. {ECO:0000305}.
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DR EMBL; U28415; AAC49472.1; -; mRNA.
DR EMBL; AF083913; AAD34236.1; -; mRNA.
DR EMBL; AC021198; AAF79882.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31825.1; -; Genomic_DNA.
DR EMBL; BT003359; AAO29977.1; -; mRNA.
DR EMBL; AF332435; AAG48798.1; -; mRNA.
DR EMBL; AY086570; AAM63633.1; -; mRNA.
DR EMBL; AY072347; AAL61954.1; -; mRNA.
DR EMBL; X99224; CAA67608.1; -; mRNA.
DR EMBL; Z18518; CAA79214.1; -; mRNA.
DR EMBL; AK221429; BAD94442.1; -; mRNA.
DR PIR; C86479; C86479.
DR RefSeq; NP_174810.1; NM_103274.4.
DR PDB; 1YCN; X-ray; 2.51 A; A/B=2-317.
DR PDB; 2Q4C; X-ray; 2.51 A; A/B=2-317.
DR PDBsum; 1YCN; -.
DR PDBsum; 2Q4C; -.
DR AlphaFoldDB; Q9SYT0; -.
DR SMR; Q9SYT0; -.
DR BioGRID; 25708; 24.
DR DIP; DIP-61421N; -.
DR IntAct; Q9SYT0; 18.
DR MINT; Q9SYT0; -.
DR STRING; 3702.AT1G35720.1; -.
DR TCDB; 1.A.31.1.8; the annexin (annexin) family.
DR iPTMnet; Q9SYT0; -.
DR PaxDb; Q9SYT0; -.
DR PRIDE; Q9SYT0; -.
DR ProteomicsDB; 244460; -.
DR DNASU; 840476; -.
DR EnsemblPlants; AT1G35720.1; AT1G35720.1; AT1G35720.
DR GeneID; 840476; -.
DR Gramene; AT1G35720.1; AT1G35720.1; AT1G35720.
DR KEGG; ath:AT1G35720; -.
DR Araport; AT1G35720; -.
DR TAIR; locus:2011344; AT1G35720.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR InParanoid; Q9SYT0; -.
DR OMA; KVKAIWA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9SYT0; -.
DR BioCyc; ARA:AT1G35720-MON; -.
DR EvolutionaryTrace; Q9SYT0; -.
DR PRO; PR:Q9SYT0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYT0; baseline and differential.
DR Genevisible; Q9SYT0; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0035619; C:root hair tip; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:TAIR.
DR GO; GO:0110128; P:phloem sucrose unloading; IMP:TAIR.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR009118; AnnexinD_plant.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01814; ANNEXINPLANT.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cytoplasm; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..317
FT /note="Annexin D1"
FT /id="PRO_0000278815"
FT REPEAT 11..82
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 83..154
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 166..238
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 242..313
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 100
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 156
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 284
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MUTAGEN 40
FT /note="H->A: Loss of peroxidase activity."
FT /evidence="ECO:0000269|PubMed:16153598"
FT CONFLICT 59
FT /note="E -> K (in Ref. 1; AAC49472)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> I (in Ref. 7; CAA67608)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..232
FT /note="FLAL -> LPCT (in Ref. 1; AAC49472)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..294
FT /note="EK -> R (in Ref. 7; CAA67608)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..301
FT /note="TR -> NC (in Ref. 7; CAA67608)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> G (in Ref. 7; CAA67608)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="LL -> IF (in Ref. 7; CAA67608)"
FT /evidence="ECO:0000305"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2Q4C"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2Q4C"
FT TURN 123..129
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:2Q4C"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2Q4C"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:2Q4C"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:2Q4C"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:2Q4C"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:2Q4C"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1YCN"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:2Q4C"
SQ SEQUENCE 317 AA; 36204 MW; 92516D630325005F CRC64;
MATLKVSDSV PAPSDDAEQL RTAFEGWGTN EDLIISILAH RSAEQRKVIR QAYHETYGED
LLKTLDKELS NDFERAILLW TLEPGERDAL LANEATKRWT SSNQVLMEVA CTRTSTQLLH
ARQAYHARYK KSLEEDVAHH TTGDFRKLLV SLVTSYRYEG DEVNMTLAKQ EAKLVHEKIK
DKHYNDEDVI RILSTRSKAQ INATFNRYQD DHGEEILKSL EEGDDDDKFL ALLRSTIQCL
TRPELYFVDV LRSAINKTGT DEGALTRIVT TRAEIDLKVI GEEYQRRNSI PLEKAITKDT
RGDYEKMLVA LLGEDDA
