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HS17A_ARATH
ID   HS17A_ARATH             Reviewed;         155 AA.
AC   Q9XIE3; Q8LBH7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=17.6 kDa class I heat shock protein 1;
DE   AltName: Full=17.6 kDa heat shock protein 1;
DE            Short=AtHsp17.6A;
GN   Name=HSP17.6A; OrderedLocusNames=At1g59860; ORFNames=F23H11.18;
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;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   FUNCTION, OLIGOMERIZATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11576425; DOI=10.1046/j.1365-313x.2001.01107.x;
RA   Sun W., Bernard C., van de Cotte B., Van Montagu M., Verbruggen N.;
RT   "At-HSP17.6A, encoding a small heat-shock protein in Arabidopsis, can
RT   enhance osmotolerance upon overexpression.";
RL   Plant J. 27:407-415(2001).
RN   [7]
RP   INTERACTION WITH AKR2A, AND INDUCTION BY HEAT SHOCK.
RC   STRAIN=cv. Columbia;
RX   PubMed=21730198; DOI=10.1104/pp.111.178681;
RA   Kim D.H., Xu Z.-Y., Na Y.J., Yoo Y.-J., Lee J., Sohn E.-J., Hwang I.;
RT   "Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the
RT   targeting of chloroplast outer membrane proteins in Arabidopsis.";
RL   Plant Physiol. 157:132-146(2011).
CC   -!- FUNCTION: Possesses chaperone activity. {ECO:0000269|PubMed:11576425,
CC       ECO:0000269|PubMed:21730198}.
CC   -!- SUBUNIT: Forms oligomeric structures (Probable). Binds to AKR2A
CC       (PubMed:21730198). {ECO:0000269|PubMed:21730198, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in seed development and germination from
CC       day 16 after pollination to day 4 after imbibition (at protein level).
CC       {ECO:0000269|PubMed:11576425}.
CC   -!- INDUCTION: By heat and osmotic shock and salt stress.
CC       {ECO:0000269|PubMed:11576425}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; AC007258; AAD39328.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33629.1; -; Genomic_DNA.
DR   EMBL; AK175148; BAD42911.1; -; mRNA.
DR   EMBL; AK175265; BAD43028.1; -; mRNA.
DR   EMBL; BT024694; ABD57519.1; -; mRNA.
DR   EMBL; AY087202; AAM64758.1; -; mRNA.
DR   PIR; G96622; G96622.
DR   RefSeq; NP_176195.1; NM_104679.4.
DR   AlphaFoldDB; Q9XIE3; -.
DR   SMR; Q9XIE3; -.
DR   BioGRID; 27505; 1.
DR   STRING; 3702.AT1G59860.1; -.
DR   PaxDb; Q9XIE3; -.
DR   PRIDE; Q9XIE3; -.
DR   ProteomicsDB; 232128; -.
DR   EnsemblPlants; AT1G59860.1; AT1G59860.1; AT1G59860.
DR   GeneID; 842280; -.
DR   Gramene; AT1G59860.1; AT1G59860.1; AT1G59860.
DR   KEGG; ath:AT1G59860; -.
DR   Araport; AT1G59860; -.
DR   TAIR; locus:2025921; AT1G59860.
DR   eggNOG; KOG0710; Eukaryota.
DR   HOGENOM; CLU_046737_5_0_1; -.
DR   InParanoid; Q9XIE3; -.
DR   OMA; LILEMAV; -.
DR   OrthoDB; 1187096at2759; -.
DR   PhylomeDB; Q9XIE3; -.
DR   PRO; PR:Q9XIE3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XIE3; baseline and differential.
DR   Genevisible; Q9XIE3; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043621; F:protein self-association; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..155
FT                   /note="17.6 kDa class I heat shock protein 1"
FT                   /id="PRO_0000387483"
FT   DOMAIN          39..154
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   CONFLICT        38
FT                   /note="S -> P (in Ref. 5; AAM64758)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  17624 MW;  5021D80CF4BC7E90 CRC64;
     MSLIPSFFGN NRRINNNIFD PFSLDVWDPF KELQFPSSSS SAIANARVDW KETAEAHVFK
     ADLPGMKKEE VKVEIEDDSV LKISGERHVE KEEKQDTWHR VERSSGGFSR KFRLPENVKM
     DQVKASMENG VLTVTVPKVE TNKKKAQVKS IDISG
 
 
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