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SAP2_ARATH
ID   SAP2_ARATH              Reviewed;         173 AA.
AC   Q8H0X0; Q9SYC3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Zinc finger A20 and AN1 domain-containing stress-associated protein 2;
DE            Short=AtSAP2;
GN   Name=SAP2; OrderedLocusNames=At1g51200; ORFNames=F11M15.6, F11M15.7;
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=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   [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].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2004) 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).
CC   -!- FUNCTION: May be involved in environmental stress response.
CC       {ECO:0000250}.
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DR   EMBL; AC006085; AAD30634.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32633.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32634.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32635.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32636.1; -; Genomic_DNA.
DR   EMBL; AY056445; AAL08301.1; -; mRNA.
DR   EMBL; BT001984; AAN71995.1; -; mRNA.
DR   EMBL; BT015115; AAT71987.1; -; mRNA.
DR   PIR; G96549; G96549.
DR   RefSeq; NP_001077694.1; NM_001084225.2.
DR   RefSeq; NP_001185193.1; NM_001198264.1.
DR   RefSeq; NP_001185194.1; NM_001198265.1.
DR   RefSeq; NP_564585.1; NM_103998.3.
DR   AlphaFoldDB; Q8H0X0; -.
DR   SMR; Q8H0X0; -.
DR   BioGRID; 26768; 4.
DR   IntAct; Q8H0X0; 4.
DR   STRING; 3702.AT1G51200.3; -.
DR   PaxDb; Q8H0X0; -.
DR   PRIDE; Q8H0X0; -.
DR   ProteomicsDB; 232867; -.
DR   EnsemblPlants; AT1G51200.1; AT1G51200.1; AT1G51200.
DR   EnsemblPlants; AT1G51200.2; AT1G51200.2; AT1G51200.
DR   EnsemblPlants; AT1G51200.3; AT1G51200.3; AT1G51200.
DR   EnsemblPlants; AT1G51200.4; AT1G51200.4; AT1G51200.
DR   GeneID; 841543; -.
DR   Gramene; AT1G51200.1; AT1G51200.1; AT1G51200.
DR   Gramene; AT1G51200.2; AT1G51200.2; AT1G51200.
DR   Gramene; AT1G51200.3; AT1G51200.3; AT1G51200.
DR   Gramene; AT1G51200.4; AT1G51200.4; AT1G51200.
DR   KEGG; ath:AT1G51200; -.
DR   Araport; AT1G51200; -.
DR   TAIR; locus:2008251; AT1G51200.
DR   eggNOG; KOG3173; Eukaryota.
DR   HOGENOM; CLU_057016_5_0_1; -.
DR   OMA; PFDYHSA; -.
DR   OrthoDB; 1551371at2759; -.
DR   PhylomeDB; Q8H0X0; -.
DR   PRO; PR:Q8H0X0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8H0X0; baseline and differential.
DR   Genevisible; Q8H0X0; AT.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..173
FT                   /note="Zinc finger A20 and AN1 domain-containing stress-
FT                   associated protein 2"
FT                   /id="PRO_0000269855"
FT   ZN_FING         12..46
FT                   /note="A20-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   ZN_FING         108..154
FT                   /note="AN1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
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         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
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   CONFLICT        49
FT                   /note="A -> T (in Ref. 3; AAN71995)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   173 AA;  18429 MW;  6A8F86CA09B3CBED CRC64;
     MDHDKTGCQS PPEGPKLCTN NCGFFGSAAT MNMCSKCHKD MLFQQEQGAK FASAVSGTSS
     SSNIIKETFT AALVDIETKS VEPMTVSVQP SSVQVVAEVV APEEAAKPKG PSRCTTCNKR
     VGLTGFKCRC GSLFCGTHRY ADVHDCSFNY HAAAQEAIAK ANPVVKAEKL DKI
 
 
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