ABI5_ORYSJ
ID ABI5_ORYSJ Reviewed; 388 AA.
AC Q8RZ35; A2TGS0; B9EUT0; Q0JHJ8;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=bZIP transcription factor ABI5 homolog {ECO:0000305};
DE Short=OsABI5 {ECO:0000303|PubMed:17604002};
DE AltName: Full=bZIP transcription factor 10 {ECO:0000303|PubMed:18065552};
DE Short=OsBZIP10 {ECO:0000303|PubMed:18065552};
GN Name=ABI5 {ECO:0000303|PubMed:17604002};
GN Synonyms=BZIP10 {ECO:0000303|PubMed:18065552},
GN OREB1 {ECO:0000303|PubMed:21055780};
GN OrderedLocusNames=Os01g0859300 {ECO:0000312|EMBL:BAS75326.1},
GN LOC_Os01g64000 {ECO:0000305};
GN ORFNames=OsJ_04142 {ECO:0000312|EMBL:EEE55706.1},
GN P0489B03.11 {ECO:0000312|EMBL:BAB90559.1},
GN P0679C12.1 {ECO:0000312|EMBL:BAB91752.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP FUNCTION, SUBUNIT, HOMODIMERIZATION, INTERACTION WITH VP1, AND TISSUE
RP SPECIFICITY.
RX PubMed=17604002; DOI=10.1016/j.bbrc.2007.05.226;
RA Zou M., Guan Y., Ren H., Zhang F., Chen F.;
RT "Characterization of alternative splicing products of bZIP transcription
RT factors OsABI5.";
RL Biochem. Biophys. Res. Commun. 360:307-313(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GF14D,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID,
RP PHOSPHORYLATION AT SER-44, AND MUTAGENESIS OF SER-43; SER-44; SER-47;
RP 72-PHE-VAL-73; 76-ILE-TRP-77; SER-118; SER-120 AND SER-385.
RX PubMed=21055780; DOI=10.1016/j.phytochem.2010.10.005;
RA Hong J.Y., Chae M.J., Lee I.S., Lee Y.N., Nam M.H., Kim D.Y., Byun M.O.,
RA Yoon I.S.;
RT "Phosphorylation-mediated regulation of a rice ABA responsive element
RT binding factor.";
RL Phytochemistry 72:27-36(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18236009; DOI=10.1007/s11103-008-9298-4;
RA Zou M., Guan Y., Ren H., Zhang F., Chen F.;
RT "A bZIP transcription factor, OsABI5, is involved in rice fertility and
RT stress tolerance.";
RL Plant Mol. Biol. 66:675-683(2008).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18065552; DOI=10.1104/pp.107.112821;
RA Nijhawan A., Jain M., Tyagi A.K., Khurana J.P.;
RT "Genomic survey and gene expression analysis of the basic leucine zipper
RT transcription factor family in rice.";
RL Plant Physiol. 146:333-350(2008).
RN [10]
RP FUNCTION, INTERACTION WITH SAPK2, SUBCELLULAR LOCATION, AND INDUCTION BY
RP ABSCISIC ACID.
RX PubMed=22071266; DOI=10.1093/jxb/err338;
RA Kim H., Hwang H., Hong J.W., Lee Y.N., Ahn I.P., Yoon I.S., Yoo S.D.,
RA Lee S., Lee S.C., Kim B.G.;
RT "A rice orthologue of the ABA receptor, OsPYL/RCAR5, is a positive
RT regulator of the ABA signal transduction pathway in seed germination and
RT early seedling growth.";
RL J. Exp. Bot. 63:1013-1024(2012).
RN [11]
RP INTERACTION WITH PP2C51 AND SAPK2, AND SUBCELLULAR LOCATION.
RX PubMed=28000033; DOI=10.1007/s11103-016-0568-2;
RA Bhatnagar N., Min M.K., Choi E.H., Kim N., Moon S.J., Yoon I., Kwon T.,
RA Jung K.H., Kim B.G.;
RT "The protein phosphatase 2C clade A protein OsPP2C51 positively regulates
RT seed germination by directly inactivating OsbZIP10.";
RL Plant Mol. Biol. 93:389-401(2017).
CC -!- FUNCTION: Transcription factor that possesses transactivation activity
CC in yeast (PubMed:17604002, PubMed:21055780, PubMed:18236009). Involved
CC in abscisic acid (ABA) signaling pathway. Binds to the G-box motif 5'-
CC CACGTG-3' of TRAB1 gene promoter (PubMed:17604002). Involved in the
CC regulation of pollen maturation. May act as negative regulator of salt
CC stress response (PubMed:18236009). Together with PYL5, PP2C30 and
CC SAPK2, is part of an ABA signaling unit that modulates seed germination
CC and early seedling growth (PubMed:22071266).
CC {ECO:0000269|PubMed:17604002, ECO:0000269|PubMed:18236009,
CC ECO:0000269|PubMed:21055780, ECO:0000269|PubMed:22071266}.
CC -!- SUBUNIT: Forms homodimers. Interacts with VP1 (PubMed:17604002).
CC Interacts with GF14D (PubMed:21055780). Interacts with PP2C51
CC (PubMed:28000033). Interacts with SAPK2 (PubMed:22071266,
CC PubMed:28000033). {ECO:0000269|PubMed:17604002,
CC ECO:0000269|PubMed:21055780, ECO:0000269|PubMed:22071266,
CC ECO:0000269|PubMed:28000033}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:18236009, ECO:0000269|PubMed:21055780,
CC ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:28000033}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=OsABI5-2 {ECO:0000303|PubMed:17604002};
CC IsoId=Q8RZ35-1; Sequence=Displayed;
CC Name=2; Synonyms=OsABI5-1 {ECO:0000303|PubMed:17604002};
CC IsoId=Q8RZ35-2; Sequence=VSP_059586;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and panicles
CC (PubMed:17604002). Expressed in seeds (PubMed:21055780).
CC {ECO:0000269|PubMed:17604002, ECO:0000269|PubMed:21055780}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) (PubMed:21055780,
CC PubMed:18236009, PubMed:22071266). Induced by salt stress. Down-
CC regulated by cold and drought stresses (PubMed:18236009).
CC {ECO:0000269|PubMed:18236009, ECO:0000269|PubMed:21055780,
CC ECO:0000269|PubMed:22071266}.
CC -!- PTM: Phosphorylated at Ser-44 by SAPK6. {ECO:0000269|PubMed:21055780}.
CC -!- MISCELLANEOUS: Plants silencing ABI5 exhibit low fertility rate due to
CC abnormal development of mature pollen. Plants silencing ABI5 display
CC increased tolerance to salt stress. {ECO:0000269|PubMed:18236009}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF06780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS75326.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE55706.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF199630; ABM90394.1; -; mRNA.
DR EMBL; EF199631; ABM90395.1; -; mRNA.
DR EMBL; JQ001818; AFK74501.1; -; mRNA.
DR EMBL; AP003794; BAB90559.1; -; Genomic_DNA.
DR EMBL; AP003287; BAB91752.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06780.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014957; BAS75326.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000138; EEE55706.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015628684.1; XM_015773198.1. [Q8RZ35-1]
DR RefSeq; XP_015628691.1; XM_015773205.1.
DR AlphaFoldDB; Q8RZ35; -.
DR SMR; Q8RZ35; -.
DR STRING; 4530.OS01T0859300-01; -.
DR iPTMnet; Q8RZ35; -.
DR PRIDE; Q8RZ35; -.
DR EnsemblPlants; Os01t0859300-01; Os01t0859300-01; Os01g0859300. [Q8RZ35-1]
DR EnsemblPlants; Os01t0859300-02; Os01t0859300-02; Os01g0859300. [Q8RZ35-2]
DR GeneID; 4325061; -.
DR Gramene; Os01t0859300-01; Os01t0859300-01; Os01g0859300. [Q8RZ35-1]
DR Gramene; Os01t0859300-02; Os01t0859300-02; Os01g0859300. [Q8RZ35-2]
DR KEGG; osa:4325061; -.
DR eggNOG; ENOG502QPJH; Eukaryota.
DR HOGENOM; CLU_043238_1_1_1; -.
DR InParanoid; Q8RZ35; -.
DR OrthoDB; 961244at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0010152; P:pollen maturation; IMP:Gramene.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:Gramene.
DR GO; GO:0009409; P:response to cold; IMP:Gramene.
DR GO; GO:0009651; P:response to salt stress; IMP:Gramene.
DR GO; GO:0009414; P:response to water deprivation; IMP:Gramene.
DR GO; GO:0009845; P:seed germination; IMP:UniProtKB.
DR GO; GO:0090351; P:seedling development; IMP:UniProtKB.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043452; BZIP46-like.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR22952; PTHR22952; 1.
DR Pfam; PF00170; bZIP_1; 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 Abscisic acid signaling pathway; Alternative splicing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..388
FT /note="bZIP transcription factor ABI5 homolog"
FT /id="PRO_0000444338"
FT DOMAIN 302..365
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 304..323
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 330..344
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21055780"
FT VAR_SEQ 349..358
FT /note="Missing (in isoform 2)"
FT /id="VSP_059586"
FT MUTAGEN 43
FT /note="S->D: Reduces transactivation activity 4-fold; when
FT associated with D-44 and D-47."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 44
FT /note="S->A: Loss of phosphorylation by SAPK6."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 44
FT /note="S->D: Reduces transactivation activity 4-fold; when
FT associated with D-43 and D-47."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 47
FT /note="S->D: Reduces transactivation activity 4-fold; when
FT associated with D-43 and D-44."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 72..73
FT /note="FV->SS: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 76..77
FT /note="IW->QS: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 118
FT /note="S->A: Loss of transactivation activity; when
FT associated with A-120."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 120
FT /note="S->A: Loss of transactivation activity; when
FT associated with A-118."
FT /evidence="ECO:0000269|PubMed:21055780"
FT MUTAGEN 385
FT /note="S->A: Disrupts the interaction with GF14D."
FT /evidence="ECO:0000269|PubMed:21055780"
SQ SEQUENCE 388 AA; 41480 MW; AAC177A89DD879E2 CRC64;
MASEMSKNVK VTDDQEVTSQ ERDQSGGTKV GGEEEIAPLA RQSSILSLTL EELQNSLCEP
GRNFGSMNMD EFVANIWNAE EFQATTGGCK GAMEEAKVVD SGSGSGDAGG SGLCRQGSFS
LPLPLCQKTV EEVWTEINQA PAHTSAPASA LQPHAGSGGV AANDRQVTLG EMTLEDFLVK
AGVVRGSFTG QAAMGSGMVN GPVNPMQQGQ GGPMMFPVGP VNAMYPVMGD GMGYPGGYNG
MAIVPPPPPA QGAMVVVSPG SSDGMSAMTH ADMMNCIGNG MMIENGTRKR PHREDGCAEK
TVERRQRRMI KNRESAARSR ARKQAYTVEL EAELNYLKQE NARLKEAEKT VLLTKKQMLV
EKMMEQSKEK MNANRGGSQL RRSGSCMW
