ANXD2_ARATH
ID ANXD2_ARATH Reviewed; 317 AA.
AC Q9XEE2; Q42063;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Annexin D2;
DE AltName: Full=AnnAt2;
GN Name=ANN2; Synonyms=ANNAT2; OrderedLocusNames=At5g65020; ORFNames=MXK3.27;
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., Roux S.J.;
RT "Isolation and characterization of two different Arabidopsis annexin
RT cDNAs.";
RL (er) Plant Gene Register PGR99-065(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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].
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-124.
RC STRAIN=cv. Columbia;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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 [8]
RP SUBCELLULAR LOCATION.
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-95; THR-100
RP AND TYR-129.
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 mediate regulated, targeted secretion of Golgi-derived
CC vesicles during seedling development.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=translocate
CC from cytosol to membrane in a calcium-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XEE2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed mainly in roots and flowers. Low in stems
CC and bearly detectable in leaves. {ECO:0000269|PubMed:11457958}.
CC -!- DEVELOPMENTAL STAGE: In germinating seedlings, expressed in root,
CC hypocotyl and cotyledon epidermal cells. By day 4, expression expands
CC in the root endodermis and throughout initiating lateral roots. As the
CC seedling matures, expression in the hypocotyl and cotyledons decreases
CC and by day 14, expression is restricted to creases between the shoot
CC meristem and its lateral primordia. {ECO:0000269|PubMed:11457958}.
CC -!- INDUCTION: Up-regulated by heat shock stress. Down-regulated by cold,
CC dehydration, and salt stresses. {ECO:0000269|PubMed:16531057}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) 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; AF083914; AAD34237.1; -; mRNA.
DR EMBL; AB019236; BAA97314.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97986.1; -; Genomic_DNA.
DR EMBL; AY070400; AAL49896.1; -; mRNA.
DR EMBL; AY096577; AAM20227.1; -; mRNA.
DR EMBL; AY085713; AAM62931.1; -; mRNA.
DR EMBL; Z25968; CAA81121.1; -; mRNA.
DR RefSeq; NP_201307.1; NM_125901.4. [Q9XEE2-1]
DR AlphaFoldDB; Q9XEE2; -.
DR SMR; Q9XEE2; -.
DR BioGRID; 21868; 2.
DR IntAct; Q9XEE2; 1.
DR MINT; Q9XEE2; -.
DR STRING; 3702.AT5G65020.1; -.
DR iPTMnet; Q9XEE2; -.
DR MetOSite; Q9XEE2; -.
DR PaxDb; Q9XEE2; -.
DR PRIDE; Q9XEE2; -.
DR ProteomicsDB; 246774; -. [Q9XEE2-1]
DR DNASU; 836626; -.
DR EnsemblPlants; AT5G65020.1; AT5G65020.1; AT5G65020. [Q9XEE2-1]
DR GeneID; 836626; -.
DR Gramene; AT5G65020.1; AT5G65020.1; AT5G65020. [Q9XEE2-1]
DR KEGG; ath:AT5G65020; -.
DR Araport; AT5G65020; -.
DR TAIR; locus:2177709; AT5G65020.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR InParanoid; Q9XEE2; -.
DR OMA; FALMETP; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9XEE2; -.
DR PRO; PR:Q9XEE2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XEE2; baseline and differential.
DR Genevisible; Q9XEE2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; 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:0110128; P:phloem sucrose unloading; IMP:TAIR.
DR GO; GO:0015774; P:polysaccharide transport; TAS:TAIR.
DR GO; GO:0080022; P:primary root development; 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: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 Acetylation; Alternative splicing; Annexin; Calcium;
KW Calcium/phospholipid-binding; Cytoplasm; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CHAIN 2..317
FT /note="Annexin D2"
FT /id="PRO_0000278816"
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:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 100
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26452715"
FT MOD_RES 284
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CONFLICT 118..122
FT /note="LIKVK -> FIQG (in Ref. 6; CAA81121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 36266 MW; 8A643FA4BFE780E7 CRC64;
MASLKVPSNV PLPEDDAEQL HKAFSGWGTN EKLIISILAH RNAAQRSLIR SVYAATYNED
LLKALDKELS SDFERAVMLW TLDPPERDAY LAKESTKMFT KNNWVLVEIA CTRPALELIK
VKQAYQARYK KSIEEDVAQH TSGDLRKLLL PLVSTFRYEG DDVNMMLARS EAKILHEKVS
EKSYSDDDFI RILTTRSKAQ LGATLNHYNN EYGNAINKNL KEESDDNDYM KLLRAVITCL
TYPEKHFEKV LRLSINKMGT DEWGLTRVVT TRTEVDMERI KEEYQRRNSI PLDRAIAKDT
SGDYEDMLVA LLGHGDA
