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SAP7_ARATH
ID   SAP7_ARATH              Reviewed;         175 AA.
AC   Q9SZ69;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Zinc finger A20 and AN1 domain-containing stress-associated protein 7;
DE            Short=AtSAP7;
GN   Name=SAP7; OrderedLocusNames=At4g12040; ORFNames=F16J13.110;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   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   [4]
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   [5]
RP   GENE FAMILY.
RX   PubMed=17033811; DOI=10.1007/s00438-006-0165-1;
RA   Vij S., Tyagi A.K.;
RT   "Genome-wide analysis of the stress associated protein (SAP) gene family
RT   containing A20/AN1 zinc-finger(s) in rice and their phylogenetic
RT   relationship with Arabidopsis.";
RL   Mol. Genet. Genomics 276:565-575(2006).
RN   [6]
RP   STRUCTURE BY NMR OF 106-156.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of ZF-AN1 domain from Arabidopsis thaliana.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: May be involved in environmental stress response.
CC       {ECO:0000250}.
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DR   EMBL; AL049638; CAB40945.1; -; Genomic_DNA.
DR   EMBL; AL161533; CAB78247.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83089.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83090.1; -; Genomic_DNA.
DR   EMBL; AF325093; AAK17161.1; -; mRNA.
DR   EMBL; AF361575; AAK32743.1; -; mRNA.
DR   EMBL; AY081720; AAL87373.1; -; mRNA.
DR   EMBL; AY088226; AAM65767.1; -; mRNA.
DR   PIR; T06611; T06611.
DR   RefSeq; NP_192941.1; NM_117274.3.
DR   RefSeq; NP_849364.1; NM_179033.1.
DR   PDB; 1WG2; NMR; -; A=106-156.
DR   PDBsum; 1WG2; -.
DR   AlphaFoldDB; Q9SZ69; -.
DR   SMR; Q9SZ69; -.
DR   BioGRID; 12110; 1.
DR   STRING; 3702.AT4G12040.2; -.
DR   PaxDb; Q9SZ69; -.
DR   PRIDE; Q9SZ69; -.
DR   ProteomicsDB; 226645; -.
DR   EnsemblPlants; AT4G12040.1; AT4G12040.1; AT4G12040.
DR   EnsemblPlants; AT4G12040.2; AT4G12040.2; AT4G12040.
DR   GeneID; 826812; -.
DR   Gramene; AT4G12040.1; AT4G12040.1; AT4G12040.
DR   Gramene; AT4G12040.2; AT4G12040.2; AT4G12040.
DR   KEGG; ath:AT4G12040; -.
DR   Araport; AT4G12040; -.
DR   TAIR; locus:2118036; AT4G12040.
DR   eggNOG; KOG3173; Eukaryota.
DR   HOGENOM; CLU_057016_5_0_1; -.
DR   InParanoid; Q9SZ69; -.
DR   OMA; SKAANRC; -.
DR   OrthoDB; 1551371at2759; -.
DR   PhylomeDB; Q9SZ69; -.
DR   EvolutionaryTrace; Q9SZ69; -.
DR   PRO; PR:Q9SZ69; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZ69; baseline and differential.
DR   Genevisible; Q9SZ69; AT.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 4.10.1110.10; -; 1.
DR   InterPro; IPR035896; AN1-like_Znf.
DR   InterPro; IPR002653; Znf_A20.
DR   InterPro; IPR000058; Znf_AN1.
DR   Pfam; PF01754; zf-A20; 1.
DR   Pfam; PF01428; zf-AN1; 1.
DR   SMART; SM00259; ZnF_A20; 1.
DR   SMART; SM00154; ZnF_AN1; 1.
DR   SUPFAM; SSF118310; SSF118310; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
DR   PROSITE; PS51039; ZF_AN1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..175
FT                   /note="Zinc finger A20 and AN1 domain-containing stress-
FT                   associated protein 7"
FT                   /id="PRO_0000066579"
FT   ZN_FING         13..47
FT                   /note="A20-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   ZN_FING         110..156
FT                   /note="AN1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:1WG2"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1WG2"
FT   TURN            144..147
FT                   /evidence="ECO:0007829|PDB:1WG2"
SQ   SEQUENCE   175 AA;  18991 MW;  CD7BC05996932C60 CRC64;
     MGSEENNSTS FPPTEPKLCD NGCGFFGSPS NMNLCSKCYR SLRAEEDQTA VAKAAVKNSL
     KLPSCSIIAP GQKHPLEIKP AHLETVVVTA EPSSVPVAAE QDEAEPSRPV RPNNRCFSCN
     KKVGVMGFKC KCGSTFCGSH RYPEKHECSF DFKEVGRDAI AKANPLVKAD KVQRI
 
 
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