ANXD6_ARATH
ID ANXD6_ARATH Reviewed; 318 AA.
AC Q9LX08; A0MFF3; Q681H6; Q9C5V3;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Annexin D6;
DE AltName: Full=AnnAt6;
GN Name=ANN6; Synonyms=ANNAT6; OrderedLocusNames=At5g10220;
GN ORFNames=F18D22.3, T31P16_210;
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 heat shock, dehydration 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28695.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={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; AY014798; AAG61155.1; -; mRNA.
DR EMBL; AL356332; CAB92063.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91509.1; -; Genomic_DNA.
DR EMBL; AK175641; BAD43404.1; -; mRNA.
DR EMBL; AK175892; BAD43655.1; -; mRNA.
DR EMBL; AK175572; BAD43335.1; -; mRNA.
DR EMBL; DQ446938; ABE66149.1; -; mRNA.
DR EMBL; DQ653279; ABK28695.1; ALT_SEQ; mRNA.
DR PIR; T50026; T50026.
DR RefSeq; NP_196584.1; NM_121060.4.
DR AlphaFoldDB; Q9LX08; -.
DR SMR; Q9LX08; -.
DR BioGRID; 16164; 3.
DR IntAct; Q9LX08; 1.
DR STRING; 3702.AT5G10220.1; -.
DR PaxDb; Q9LX08; -.
DR PRIDE; Q9LX08; -.
DR ProteomicsDB; 244435; -.
DR EnsemblPlants; AT5G10220.1; AT5G10220.1; AT5G10220.
DR GeneID; 830886; -.
DR Gramene; AT5G10220.1; AT5G10220.1; AT5G10220.
DR KEGG; ath:AT5G10220; -.
DR Araport; AT5G10220; -.
DR TAIR; locus:2184108; AT5G10220.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR InParanoid; Q9LX08; -.
DR OMA; CKLWVGH; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9LX08; -.
DR PRO; PR:Q9LX08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX08; baseline and differential.
DR Genevisible; Q9LX08; 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: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 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..318
FT /note="Annexin D6"
FT /id="PRO_0000278820"
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 168..239
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 243..314
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 256
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 260
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="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 301
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 285
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT CONFLICT 33
FT /note="M -> I (in Ref. 4; BAD43335/BAD43655/BAD43404)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> S (in Ref. 1; AAG61155)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="L -> M (in Ref. 1; AAG61155)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="F -> L (in Ref. 1; AAG61155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36570 MW; 3E4B2A1BBC8C56E1 CRC64;
MASLKIPANI PLPEEDSEQL HKAFKGWGTN EGMIISILAH RNATQRSFIR AVYAANYNKD
LLKELDGELS GDFERVVMLW TLDPTERDAY LANESTKLFT KNIWVLVEIA CTRPSLEFFK
TKQAYHVRYK TSLEEDVAYH TSGNIRKLLV PLVSTFRYDG NADEVNVKLA RSEAKTLHKK
ITEKAYTDED LIRILTTRSK AQINATLNHF KDKFGSSINK FLKEDSNDDY VQLLKTAIKC
LTYPEKYFEK VLRRAINRMG TDEWALTRVV TTRAEVDLER IKEEYLRRNS VPLDRAIAND
TSGDYKDMLL ALLGHDHA
