BZP10_ARATH
ID BZP10_ARATH Reviewed; 411 AA.
AC O22763; C0Z2B4; Q8RXJ3; Q9FUD4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Basic leucine zipper 10;
DE Short=AtbZIP10;
DE Short=bZIP protein 10;
DE AltName: Full=Basic leucine zipper OPAQUE 2 homolog 1;
DE Short=Basic leucine zipper O2 homolog 1;
GN Name=BZIP10; Synonyms=BZO2H1; OrderedLocusNames=At4g02640;
GN ORFNames=T10P11.9;
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] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, INTERACTION WITH ABI3, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12657652; DOI=10.1074/jbc.m210538200;
RA Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I., Carbonero P.,
RA Vicente-Carbajosa J.;
RT "Synergistic activation of seed storage protein gene expression in
RT Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
RL J. Biol. Chem. 278:21003-21011(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
RA Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
RT "Evolutionary pattern of angiosperm bZIP factors homologous to the maize
RT Opaque2 regulatory protein.";
RL J. Mol. Evol. 56:105-116(2003).
RN [3]
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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-411 (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH BZIP53.
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT by specific heterodimerisation of bZIP transcription factors.";
RL EMBO J. 25:3133-3143(2006).
RN [11]
RP FUNCTION IN DEFENSE RESPONSES HYALOPERONOSPORA PARASITICA, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH LSD1.
RC STRAIN=cv. Columbia;
RX PubMed=16957775; DOI=10.1038/sj.emboj.7601312;
RA Kaminaka H., Naeke C., Epple P., Dittgen J., Schuetze K., Chaban C.,
RA Holt B.F. III, Merkle T., Schaefer E., Harter K., Dangl J.L.;
RT "bZIP10-LSD1 antagonism modulates basal defense and cell death in
RT Arabidopsis following infection.";
RL EMBO J. 25:4400-4411(2006).
RN [12]
RP INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP11; BZIP44; BZIP53 AND BZIP63.
RX PubMed=16709202; DOI=10.1111/j.1365-313x.2006.02731.x;
RA Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "Two-hybrid protein-protein interaction analysis in Arabidopsis
RT protoplasts: establishment of a heterodimerization map of group C and group
RT S bZIP transcription factors.";
RL Plant J. 46:890-900(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH BZIP53 AND ABI3.
RX PubMed=19531597; DOI=10.1105/tpc.108.062968;
RA Alonso R., Onate-Sanchez L., Weltmeier F., Ehlert A., Diaz I., Dietrich K.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "A pivotal role of the basic leucine zipper transcription factor bZIP53 in
RT the regulation of Arabidopsis seed maturation gene expression based on
RT heterodimerization and protein complex formation.";
RL Plant Cell 21:1747-1761(2009).
RN [14]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
RA Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K., Wang X.,
RA Chaban C., Hanson J., Teige M., Harter K., Vicente-Carbajosa J.,
RA Smeekens S., Droege-Laser W.;
RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription factor
RT network: availability of heterodimerization partners controls gene
RT expression during stress response and development.";
RL Plant Mol. Biol. 69:107-119(2009).
RN [15]
RP FUNCTION, AND INTERACTION WITH BZIP53.
RX PubMed=19261733; DOI=10.1104/pp.109.136531;
RA Roschzttardtz H., Fuentes I., Vasquez M., Corvalan C., Leon G., Gomez I.,
RA Araya A., Holuigue L., Vicente-Carbajosa J., Jordana X.;
RT "A nuclear gene encoding the iron-sulfur subunit of mitochondrial complex
RT II is regulated by B3 domain transcription factors during seed development
RT in Arabidopsis.";
RL Plant Physiol. 150:84-95(2009).
RN [16]
RP INTERACTION WITH BZIP1 AND BZIP63.
RX PubMed=20080816; DOI=10.1093/mp/ssp115;
RA Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
RT "The arabidopsis bZIP1 transcription factor is involved in sugar signaling,
RT protein networking, and DNA binding.";
RL Mol. Plant 3:361-373(2010).
CC -!- FUNCTION: Transcription factor that binds to the C-box-like motif (5'-
CC TGCTGACGTCA-3') and G-box-like motif (5'-CCACGTGGCC-3'), ABRE elements,
CC of gene promoters. Binds to the 5'-ACGT-3' motif of seed storage
CC protein (SSP) encoding gene promoters (e.g. At2S and CRU3) and promotes
CC their expression in seeds when in complex with ABI3 and BZIP53.
CC Involved in the defense responses to the biotrophic pathogen
CC Hyaloperonospora parasitica and oxidative stress responses; mediates
CC positively cell death (PubMed:12657652, PubMed:16957775,
CC PubMed:19261733, PubMed:19531597). Promotes BZIP53-mediated response to
CC hypoosmolarity stress that leads to POX1/PRODH1 accumulation
CC (PubMed:16810321). {ECO:0000269|PubMed:12657652,
CC ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:16957775,
CC ECO:0000269|PubMed:19261733, ECO:0000269|PubMed:19531597}.
CC -!- SUBUNIT: Forms a heterodimer with BZIP1, BZIP2, BZIP9, BZIP11, BZIP44,
CC BZIP53 and BZIP63. Interacts with ABI3 and forms a complex made of
CC ABI3, BZIP53 and BZIP10. Binding with LSD1 leads to cytoplasmic
CC retention. {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:16709202,
CC ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:16957775,
CC ECO:0000269|PubMed:19261733, ECO:0000269|PubMed:19531597,
CC ECO:0000269|PubMed:20080816}.
CC -!- INTERACTION:
CC O22763; Q9FGX2: BZIP1; NbExp=3; IntAct=EBI-942648, EBI-942623;
CC O22763; O65683: BZIP11; NbExp=3; IntAct=EBI-942648, EBI-942769;
CC O22763; Q9SI15: BZIP2; NbExp=3; IntAct=EBI-942648, EBI-942735;
CC O22763; C0Z2L5: BZIP44; NbExp=3; IntAct=EBI-942648, EBI-942804;
CC O22763; Q9LZP8: BZIP53; NbExp=8; IntAct=EBI-942648, EBI-942845;
CC O22763-3; B9DGI8-2: BZIP63; NbExp=3; IntAct=EBI-15191815, EBI-15191817;
CC O22763-3; Q9SFV2: FHA2; NbExp=3; IntAct=EBI-15191815, EBI-15191747;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:16957775}. Cytoplasm {ECO:0000269|PubMed:16957775}.
CC Note=Shuttles between the nucleus and the cytoplasm. Retained outside
CC the nucleus by LSD1 to prevent cell death.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O22763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O22763-2; Sequence=VSP_042640;
CC Name=3;
CC IsoId=O22763-3; Sequence=VSP_042639;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems, young leaves,
CC trichomes, hydathodes, siliques, seeds, and flowers, mostly in vascular
CC tissues. {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
CC -!- DEVELOPMENTAL STAGE: First observed in carpels and seeds at early
CC stages of development, mostly in embryo and, at lower extent, in the
CC endosperm. Accumulates and peaks at maturation. Fade out during late
CC seed development steps, restricted to the inner layer of the seed coat,
CC and, at very low levels, in the mature embryo and the remaining
CC endosperm. Also present in the lignified inner subepidermal layer of
CC the valves. In the anthers, restricted to the connective tissue at
CC pre- and post-dehiscence stages and detected in the vascular tissue of
CC the stamen filament. {ECO:0000269|PubMed:12657652,
CC ECO:0000269|PubMed:18841482}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010859; CAC79657.1; -; mRNA.
DR EMBL; AF310222; AAG25727.1; -; mRNA.
DR EMBL; AC002330; AAC78255.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80757.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82207.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82208.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67475.1; -; Genomic_DNA.
DR EMBL; AK318728; BAH56843.1; -; mRNA.
DR EMBL; AY080854; AAL87327.1; -; mRNA.
DR EMBL; BT025558; ABF58976.1; -; mRNA.
DR EMBL; AY088417; AAM65954.1; -; mRNA.
DR PIR; T01085; T01085.
DR RefSeq; NP_001329303.1; NM_001340390.1. [O22763-2]
DR RefSeq; NP_192173.1; NM_116498.4. [O22763-1]
DR RefSeq; NP_849290.1; NM_178959.3. [O22763-3]
DR AlphaFoldDB; O22763; -.
DR SMR; O22763; -.
DR BioGRID; 13508; 24.
DR IntAct; O22763; 22.
DR MINT; O22763; -.
DR STRING; 3702.AT4G02640.2; -.
DR iPTMnet; O22763; -.
DR PaxDb; O22763; -.
DR PRIDE; O22763; -.
DR ProteomicsDB; 240555; -. [O22763-1]
DR EnsemblPlants; AT4G02640.1; AT4G02640.1; AT4G02640. [O22763-1]
DR EnsemblPlants; AT4G02640.2; AT4G02640.2; AT4G02640. [O22763-3]
DR EnsemblPlants; AT4G02640.4; AT4G02640.4; AT4G02640. [O22763-2]
DR GeneID; 828219; -.
DR Gramene; AT4G02640.1; AT4G02640.1; AT4G02640. [O22763-1]
DR Gramene; AT4G02640.2; AT4G02640.2; AT4G02640. [O22763-3]
DR Gramene; AT4G02640.4; AT4G02640.4; AT4G02640. [O22763-2]
DR KEGG; ath:AT4G02640; -.
DR Araport; AT4G02640; -.
DR TAIR; locus:2132372; AT4G02640.
DR eggNOG; ENOG502QX6A; Eukaryota.
DR HOGENOM; CLU_037575_1_1_1; -.
DR InParanoid; O22763; -.
DR OMA; MFFEEIA; -.
DR OrthoDB; 1008484at2759; -.
DR PhylomeDB; O22763; -.
DR PRO; PR:O22763; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22763; baseline and differential.
DR Genevisible; O22763; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:2000693; P:positive regulation of seed maturation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0002240; P:response to molecule of oomycetes origin; IMP:TAIR.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Hypersensitive response;
KW Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Seed storage protein; Storage protein; Transcription;
KW Transcription regulation.
FT CHAIN 1..411
FT /note="Basic leucine zipper 10"
FT /id="PRO_0000416558"
FT DOMAIN 215..278
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..236
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 243..257
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 362..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..226
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 141..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M1G6"
FT VAR_SEQ 164
FT /note="Q -> QGSLMTP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12569427, ECO:0000303|Ref.7"
FT /id="VSP_042639"
FT VAR_SEQ 406..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_042640"
SQ SEQUENCE 411 AA; 45358 MW; 9C651436D8D167CF CRC64;
MNSIFSIDDF SDPFWETPPI PLNPDSSKPV TADEVSQSQP EWTFEMFLEE ISSSAVSSEP
LGNNNNAIVG VSSAQSLPSV SGQNDFEDDS RFRDRDSGNL DCAAPMTTKT VIVDSDDYRR
VLKNKLETEC ATVVSLRVGS VKPEDSTSSP ETQLQPVQSS PLTQGELGVT SSLPAEVKKT
GVSMKQVTSG SSREYSDDED LDEENETTGS LKPEDVKKSR RMLSNRESAR RSRRRKQEQT
SDLETQVNDL KGEHSSLLKQ LSNMNHKYDE AAVGNRILKA DIETLRAKVK MAEETVKRVT
GMNPMLLGRS SGHNNNNRMP ITGNNRMDSS SIIPAYQPHS NLNHMSNQNI GIPTILPPRL
GNNFAAPPSQ TSSPLQRIRN GQNHHVTPSA NPYGWNTEPQ NDSAWPKKCV D
