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Database: UniProt
Entry: A0A397XIW5_BRACM
LinkDB: A0A397XIW5_BRACM
Original site: A0A397XIW5_BRACM 
ID   A0A397XIW5_BRACM        Unreviewed;       229 AA.
AC   A0A397XIW5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN   ORFNames=BRARA_J00138 {ECO:0000313|EMBL:RID40068.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:RID40068.1, ECO:0000313|Proteomes:UP000264353};
RN   [1] {ECO:0000313|EMBL:RID40068.1, ECO:0000313|Proteomes:UP000264353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA   Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA   Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA   Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA   Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA   Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA   Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA   Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA   Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA   Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA   Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA   Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA   Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA   Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA   Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA   Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA   Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA   Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA   Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA   Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA   Yotsui I., Zachgo S., Schmutz J.;
RT   "WGS assembly of Brassica rapa FPsc.";
RL   Submitted (JUN-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; CM010637; RID40068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397XIW5; -.
DR   Proteomes; UP000264353; Chromosome a10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051879; F:Hsp90 protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:UniProtKB-UniRule.
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:SF24; CO-CHAPERONE PROTEIN P23; 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   3: Inferred from homology;
KW   Chaperone {ECO:0000256|RuleBase:RU369032};
KW   Cytoplasm {ECO:0000256|RuleBase:RU369032};
KW   Nucleus {ECO:0000256|RuleBase:RU369032}.
FT   DOMAIN          2..91
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          172..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  24283 MW;  503DAD0C346AB6E6 CRC64;
     MSHHPEVKWA EREDKVYLTV LLPDAKDANV KLDPEGVFEF SAKAGPENQV YELKLELNDK
     VNVEESKINI GLRSIFCIVE KAEPKWWGKL LRGGKPPHYV KVDWDKWVDE DEDPATGPGD
     MDMGGMGGMG GMDFSNFGGM GGMGGMGGMG GMGGLEGLGG MGGMAGLEGL GGMGGMGGPG
     GMGGMEEFED SDDEGEEVKS GEKKEEAQAP APATEETKTE EQTTVKSDK
//
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