ANXD7_ARATH
ID ANXD7_ARATH Reviewed; 316 AA.
AC Q9LX07; Q9C5V2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Annexin D7;
DE AltName: Full=AnnAt7;
GN Name=ANNAT7; Synonyms=ANN7; OrderedLocusNames=At5g10230;
GN ORFNames=F18D22.4, T31P16_220;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 in flowers.
CC {ECO:0000269|PubMed:11457958}.
CC -!- INDUCTION: Up-regulated by cold, heat shock and salt stresses.
CC {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}.
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DR EMBL; AY014799; AAG61156.1; -; mRNA.
DR EMBL; AL356332; CAB92064.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91510.1; -; Genomic_DNA.
DR EMBL; BT029226; ABJ98558.1; -; mRNA.
DR PIR; T50027; T50027.
DR RefSeq; NP_196585.1; NM_121061.3.
DR AlphaFoldDB; Q9LX07; -.
DR SMR; Q9LX07; -.
DR STRING; 3702.AT5G10230.1; -.
DR iPTMnet; Q9LX07; -.
DR PaxDb; Q9LX07; -.
DR PRIDE; Q9LX07; -.
DR ProteomicsDB; 244436; -.
DR EnsemblPlants; AT5G10230.1; AT5G10230.1; AT5G10230.
DR GeneID; 830887; -.
DR Gramene; AT5G10230.1; AT5G10230.1; AT5G10230.
DR KEGG; ath:AT5G10230; -.
DR Araport; AT5G10230; -.
DR TAIR; locus:2184123; AT5G10230.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR InParanoid; Q9LX07; -.
DR OMA; WGTDEAC; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9LX07; -.
DR PRO; PR:Q9LX07; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX07; baseline and differential.
DR Genevisible; Q9LX07; AT.
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: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 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 D7"
FT /id="PRO_0000278821"
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..237
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 241..312
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 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 298
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="3"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 304
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 100
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 283
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CONFLICT 23
FT /note="A -> S (in Ref. 1; AAG61156)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="D -> Y (in Ref. 1; AAG61156)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="K -> R (in Ref. 1; AAG61156)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="D -> V (in Ref. 1; AAG61156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 36496 MW; DE85B365CEEA8B2C CRC64;
MASLKVPATV PLPEEDAEQL YKAFKGWGTN ERMIISILAH RNATQRSFIR AVYAANYNKD
LLKELDRELS GDFERAVMLW TFEPAERDAY LAKESTKMFT KNNWVLVEIA CTRSALELFN
AKQAYQARYK TSLEEDVAYH TSGDIRKLLV PLVSTFRYDG DEVNMTLARS EAKILHEKIK
EKAYADDDLI RILTTRSKAQ ISATLNHYKN NFGTSMSKYL KEDSENEYIQ LLKAVIKCLT
YPEKYFEKVL RQAINKLGTD EWGLTRVVTT RAEFDMERIK EEYIRRNSVP LDRAIAKDTH
GDYEDILLAL LGHDHA
