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Database: UniProt
Entry: C6TIY1_SOYBN
LinkDB: C6TIY1_SOYBN
Original site: C6TIY1_SOYBN 
ID   C6TIY1_SOYBN            Unreviewed;       200 AA.
AC   C6TIY1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN   Name=100796372 {ECO:0000313|EnsemblPlants:KRG96432};
GN   ORFNames=GLYMA_19G210600 {ECO:0000313|EMBL:KRG96432.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:ACU22871.1};
RN   [1] {ECO:0000313|EMBL:ACU22871.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRG96432.1, ECO:0000313|EnsemblPlants:KRG96432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG96432};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96432.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [3] {ECO:0000313|EnsemblPlants:KRG96432}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG96432};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KRG96432.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96432.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a co-chaperone for HSP90.
CC       {ECO:0000256|RuleBase:RU369032}.
CC   -!- SUBUNIT: Interacts with HSP90 in an ATP-dependent manner.
CC       {ECO:0000256|RuleBase:RU369032}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369032}.
CC       Nucleus {ECO:0000256|RuleBase:RU369032}.
CC   -!- SIMILARITY: Belongs to the p23/wos2 family.
CC       {ECO:0000256|ARBA:ARBA00025733, ECO:0000256|RuleBase:RU369032}.
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DR   EMBL; BT097620; ACU22871.1; -; mRNA.
DR   EMBL; CM000852; KRG96432.1; -; Genomic_DNA.
DR   RefSeq; NP_001241395.1; NM_001254466.2.
DR   AlphaFoldDB; C6TIY1; -.
DR   SMR; C6TIY1; -.
DR   STRING; 3847.C6TIY1; -.
DR   PaxDb; 3847-GLYMA19G39800-1; -.
DR   EnsemblPlants; KRG96432; KRG96432; GLYMA_19G210600.
DR   GeneID; 100796372; -.
DR   Gramene; KRG96432; KRG96432; GLYMA_19G210600.
DR   KEGG; gmx:100796372; -.
DR   InParanoid; C6TIY1; -.
DR   OMA; NHHYELK; -.
DR   OrthoDB; 782824at2759; -.
DR   Proteomes; UP000008827; Chromosome 19.
DR   ExpressionAtlas; C6TIY1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd06465; p23_hB-ind1_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR045250; p23-like.
DR   PANTHER; PTHR22932:SF22; CS DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
PE   2: Evidence at transcript level;
KW   Chaperone {ECO:0000256|RuleBase:RU369032};
KW   Cytoplasm {ECO:0000256|RuleBase:RU369032};
KW   Nucleus {ECO:0000256|RuleBase:RU369032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          2..91
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          160..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  21838 MW;  F97D7E69D962257A CRC64;
     MSRHPEVKWA QRLDKVYITV QLADSKNAKV DLTPDGIFTF SGSAGAEDHQ YELKLELFDK
     VNVEESKINV GVRSIFCVVQ KAEDGWWKRL LRGEGKPPHY VKVDWDKWVD EDEDDGNNGE
     VDLGGMDFSK FGGMGADAMG AMGGMGAGAM GGMDFSKFGG MGDAMDDIDE SDDEEQEVSK
     PLEQDAGEAS TEKKEAAPST
//
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