ANXD4_ARATH
ID ANXD4_ARATH Reviewed; 319 AA.
AC Q9ZVJ6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Annexin D4;
DE AltName: Full=AnnAt4;
GN Name=ANN4; Synonyms=ANNAT4; OrderedLocusNames=At2g38750; ORFNames=T6A23.5;
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].
RA Clark G.B., Rives A.E., Beauchamp L.M., Roux S.J.;
RT "Isolation and characterization of two novel Arabidopsis annexin cDNAs.";
RL (er) Plant Gene Register PGR99-168(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [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 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 TISSUE SPECIFICITY.
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 [7]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND 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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-211 AND
RP SER-277.
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).
CC -!- FUNCTION: May be involved in osmotic stress and abscisic acid signaling
CC in a calcium-dependent manner. {ECO:0000269|PubMed:15161963}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in roots and flowers. Lower in
CC stems and leaves. {ECO:0000269|PubMed:11457958}.
CC -!- INDUCTION: Up-regulated by salt, osmotic and oxidative stresses. Up-
CC regulated by abscisic acid (ABA) and salicylic acid (SA). Down-
CC regulated by heat shock and dehydration stresses.
CC {ECO:0000269|PubMed:15161963, ECO:0000269|PubMed:16531057}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
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 -!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family. {ECO:0000305}.
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DR EMBL; AF188363; AAF14581.1; -; mRNA.
DR EMBL; AC005499; AAC67343.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09580.1; -; Genomic_DNA.
DR EMBL; AY087194; AAM64750.1; -; mRNA.
DR EMBL; AY042835; AAK68775.1; -; mRNA.
DR EMBL; AY081483; AAM10045.1; -; mRNA.
DR PIR; H84808; H84808.
DR RefSeq; NP_181409.1; NM_129432.3.
DR AlphaFoldDB; Q9ZVJ6; -.
DR SMR; Q9ZVJ6; -.
DR BioGRID; 3799; 13.
DR IntAct; Q9ZVJ6; 7.
DR MINT; Q9ZVJ6; -.
DR STRING; 3702.AT2G38750.1; -.
DR iPTMnet; Q9ZVJ6; -.
DR PaxDb; Q9ZVJ6; -.
DR PRIDE; Q9ZVJ6; -.
DR EnsemblPlants; AT2G38750.1; AT2G38750.1; AT2G38750.
DR GeneID; 818457; -.
DR Gramene; AT2G38750.1; AT2G38750.1; AT2G38750.
DR KEGG; ath:AT2G38750; -.
DR Araport; AT2G38750; -.
DR TAIR; locus:2064222; AT2G38750.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_1_0_1; -.
DR InParanoid; Q9ZVJ6; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9ZVJ6; -.
DR PRO; PR:Q9ZVJ6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVJ6; baseline and differential.
DR Genevisible; Q9ZVJ6; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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:0003729; F:mRNA binding; HDA: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; -; 3.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR037104; Annexin_sf.
DR Pfam; PF00191; Annexin; 3.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 2.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW Annexin; Calcium; Calcium/phospholipid-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Stress response.
FT CHAIN 1..319
FT /note="Annexin D4"
FT /id="PRO_0000278818"
FT REPEAT 1..75
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 86..157
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 169..240
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 241..316
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 287
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
SQ SEQUENCE 319 AA; 36221 MW; 06E38E2FA513017E CRC64;
MALPLELESL TEAISAGMGM GVDENALIST LGKSQKEHRK LFRKASKSFF VEDEERAFEK
CHDHFVRHLK LEFSRFNTAV VMWAMHPWER DARLVKKALK KGEEAYNLIV EVSCTRSAED
LLGARKAYHS LFDQSMEEDI ASHVHGPQRK LLVGLVSAYR YEGNKVKDDS AKSDAKILAE
AVASSGEEAV EKDEVVRILT TRSKLHLQHL YKHFNEIKGS DLLGGVSKSS LLNEALICLL
KPALYFSKIL DASLNKDADK TTKKWLTRVF VTRADHSDEM NEIKEEYNNL YGETLAQRIQ
EKIKGNYRDF LLTLLSKSD
