ANXD5_ARATH
ID ANXD5_ARATH Reviewed; 316 AA.
AC Q9C9X3; A0MEF1; Q1PFF4; Q9C5V4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Annexin D5;
DE AltName: Full=AnnAt5;
GN Name=ANN5; Synonyms=ANNAT5; OrderedLocusNames=At1g68090; ORFNames=T23K23.6;
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], AND 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 [2]
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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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).
CC -!- TISSUE SPECIFICITY: Expressed mainly in roots and flowers. Lower in
CC stems and leaves. {ECO:0000269|PubMed:11457958}.
CC -!- INDUCTION: Up-regulated by cold, heat shock, dehydration and salt
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=ABK28456.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY014797; AAG61154.1; -; mRNA.
DR EMBL; AC012563; AAG52011.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34748.1; -; Genomic_DNA.
DR EMBL; DQ446409; ABE65753.1; -; mRNA.
DR EMBL; DQ652921; ABK28456.1; ALT_SEQ; mRNA.
DR PIR; B96704; B96704.
DR RefSeq; NP_564920.1; NM_105479.2.
DR AlphaFoldDB; Q9C9X3; -.
DR SMR; Q9C9X3; -.
DR BioGRID; 28358; 6.
DR IntAct; Q9C9X3; 4.
DR STRING; 3702.AT1G68090.1; -.
DR PaxDb; Q9C9X3; -.
DR PRIDE; Q9C9X3; -.
DR ProteomicsDB; 240595; -.
DR EnsemblPlants; AT1G68090.1; AT1G68090.1; AT1G68090.
DR GeneID; 843137; -.
DR Gramene; AT1G68090.1; AT1G68090.1; AT1G68090.
DR KEGG; ath:AT1G68090; -.
DR Araport; AT1G68090; -.
DR TAIR; locus:2200281; AT1G68090.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR InParanoid; Q9C9X3; -.
DR OMA; CMEGMGT; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9C9X3; -.
DR PRO; PR:Q9C9X3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9X3; baseline and differential.
DR Genevisible; Q9C9X3; AT.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; 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:0009639; P:response to red or far red light; 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 Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Annexin; Calcium; Calcium/phospholipid-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CHAIN 2..316
FT /note="Annexin D5"
FT /id="PRO_0000278819"
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 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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 284
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CONFLICT 27
FT /note="R -> T (in Ref. 2; AAG52011)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="I -> M (in Ref. 1; AAG61154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35993 MW; 9DA843E54323CCC4 CRC64;
MATMKIPMTV PSPRVDADQL FKAFKGRGCD TSVIINILAH RNATQRALIE QEYETKFSDD
LRKRLHSELH GHLKKAVLLW MPEAVERDAS ILKRSLRGAV TDHKAIAEII CTRSGSQLRQ
IKQVYSNTFG VKLEEDIESE ASGNHKRVLL AYLNTTRYEG PEIDNASVEN DARTLKSAVA
RKHKSDDQTL IQIFTDRSRT HLVAVRSTYR SMYGKELGKA IRDETRGNFE HVLLTILQCA
ENSCFYFAKA LRKSMKGLGT DDTALIRIVV TRAEVDMQFI ITEYRKRYKK TLYNAVHSDT
TSHYRTFLLS LLGPNV
