ANXD8_ARATH
ID ANXD8_ARATH Reviewed; 316 AA.
AC Q94CK4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Annexin D8;
DE AltName: Full=AnnAt8;
GN Name=ANNAT8; Synonyms=ANN8; OrderedLocusNames=At5g12380; ORFNames=T2L20;
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 [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 [2]
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 [3]
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 -!- INDUCTION: Up-regulated by 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC42899.1; Type=Erroneous gene model prediction; 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; AL592312; CAC42899.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91803.1; -; Genomic_DNA.
DR RefSeq; NP_568271.2; NM_121276.3.
DR AlphaFoldDB; Q94CK4; -.
DR SMR; Q94CK4; -.
DR BioGRID; 16391; 1.
DR IntAct; Q94CK4; 1.
DR STRING; 3702.AT5G12380.1; -.
DR PaxDb; Q94CK4; -.
DR PRIDE; Q94CK4; -.
DR ProteomicsDB; 245007; -.
DR EnsemblPlants; AT5G12380.1; AT5G12380.1; AT5G12380.
DR GeneID; 831113; -.
DR Gramene; AT5G12380.1; AT5G12380.1; AT5G12380.
DR KEGG; ath:AT5G12380; -.
DR Araport; AT5G12380; -.
DR TAIR; locus:505006606; AT5G12380.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_0_1_1; -.
DR OMA; ERAICLW; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q94CK4; -.
DR PRO; PR:Q94CK4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CK4; differential.
DR Genevisible; Q94CK4; 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:0042742; P:defense response to bacterium; IEP: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; IMP: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 D8"
FT /id="PRO_0000393336"
FT REPEAT 10..81
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 82..153
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 165..236
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 240..311
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT BINDING 257
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="3"
FT /evidence="ECO:0000250|UniProtKB:P93157"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 128
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9XEE2"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
FT MOD_RES 282
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SYT0"
SQ SEQUENCE 316 AA; 35762 MW; 2E6E1DA2C7764F51 CRC64;
MATIVSPPHF SPVEDAENIK AACQGWGTNE NAIISILGHR NLFQRKLIRQ AYQEIYHEDL
IHQLKSELSG NFERAICLWV LDPPERDALL ANLALQKPIP DYKVLVEIAC MRSPEDMLAA
RRAYRCLYKH SLEEDLASRT IGDIRRLLVA MVSAYKYDGE EIDEMLAQSE AAILHDEILG
KAVDHEETIR VLSTRSSMQL SAIFNRYKDI YGTSITKDLL NHPTNEYLSA LRAAIRCIKN
PTRYYAKVLR NSINTVGTDE DALNRVIVTR AEKDLTNITG LYFKRNNVSL DQAIAKETSG
DYKAFLLALL GHGKQL
