BAG1A_SCHPO
ID BAG1A_SCHPO Reviewed; 195 AA.
AC O60125;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=BAG family molecular chaperone regulator 1A;
DE Short=BAG-1A;
GN Name=bag101; Synonyms=bag1, bag1-a; ORFNames=SPBC16G5.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9873016; DOI=10.1074/jbc.274.2.781;
RA Takayama S., Xie Z., Reed J.C.;
RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
RT regulators.";
RL J. Biol. Chem. 274:781-786(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting
CC substrate release. {ECO:0000250}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones.
CC {ECO:0000250}.
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DR EMBL; CU329671; CAA19031.1; -; Genomic_DNA.
DR EMBL; AF095789; AAD16126.1; -; mRNA.
DR PIR; T39603; T39603.
DR RefSeq; NP_596760.1; NM_001023780.2.
DR AlphaFoldDB; O60125; -.
DR SMR; O60125; -.
DR BioGRID; 276391; 23.
DR STRING; 4896.SPBC16G5.11c.1; -.
DR iPTMnet; O60125; -.
DR MaxQB; O60125; -.
DR PaxDb; O60125; -.
DR EnsemblFungi; SPBC16G5.11c.1; SPBC16G5.11c.1:pep; SPBC16G5.11c.
DR GeneID; 2539843; -.
DR KEGG; spo:SPBC16G5.11c; -.
DR PomBase; SPBC16G5.11c; bag101.
DR VEuPathDB; FungiDB:SPBC16G5.11c; -.
DR eggNOG; KOG4361; Eukaryota.
DR HOGENOM; CLU_1397083_0_0_1; -.
DR InParanoid; O60125; -.
DR OMA; HYGNQRI; -.
DR PhylomeDB; O60125; -.
DR PRO; PR:O60125; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; ISO:PomBase.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR017093; BAG-1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..195
FT /note="BAG family molecular chaperone regulator 1A"
FT /id="PRO_0000088879"
FT DOMAIN 6..72
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 109..190
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 195 AA; 22206 MW; 66F40F559EF03E19 CRC64;
MSEKTSTVTI HYGNQRFPVA VNLNETLSEL IDDLLETTEI SEKKVKLFYA GKRLKDKKAS
LSKLGLKNHS KILCIRPHKQ QRGSKEKDTV EPAPKAEAEN PVFSRISGEI KAIDQYVDKE
LSPMYDNYVN KPSNDPKQKN KQKLMISELL LQQLLKLDGV DVLGSEKLRF ERKQLVSKIQ
KMLDHVDQTS QEVAA
