ID   BAGS_BOMMO              Reviewed;         677 AA.
AC   Q9BLJ6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=BAG domain-containing protein Samui;
GN   Name=Samui;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000312|EMBL:BAB39763.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=N4; TISSUE=Egg;
RX   PubMed=11422373; DOI=10.1046/j.1432-1327.2001.02244.x;
RA   Moribe Y., Niimi T., Yamashita O., Yaginuma T.;
RT   "Samui, a novel cold-inducible gene, encoding a protein with a BAG domain
RT   similar to silencer of death domains (SODD/BAG-4), isolated from Bombyx
RT   diapause eggs.";
RL   Eur. J. Biochem. 268:3432-3442(2001).
CC   -!- FUNCTION: May play a role in transmitting a signal which both protects
CC       non-diapause eggs from cold injury and terminates diapause in diapause
CC       eggs.
CC   -!- SUBUNIT: Binds to HSP70. {ECO:0000269|PubMed:11422373}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in chilled diapause eggs
CC       and to a lesser extent in chilled non-diapause eggs.
CC   -!- DEVELOPMENTAL STAGE: In diapause eggs, expressed after chilling at 5
CC       degrees Celsius for 5-6 days, persists for 30 days and then decreases.
CC   -!- INDUCTION: By cold. {ECO:0000269|PubMed:11422373}.
CC   -!- MISCELLANEOUS: 'Samui' means 'cold' in Japanese.
CC       {ECO:0000303|PubMed:11422373}.
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DR   EMBL; AB032717; BAB39763.1; -; mRNA.
DR   RefSeq; NP_001036843.1; NM_001043378.1.
DR   AlphaFoldDB; Q9BLJ6; -.
DR   SMR; Q9BLJ6; -.
DR   STRING; 7091.BGIBMGA006976-TA; -.
DR   GeneID; 692383; -.
DR   KEGG; bmor:692383; -.
DR   CTD; 692383; -.
DR   eggNOG; KOG4361; Eukaryota.
DR   HOGENOM; CLU_445699_0_0_1; -.
DR   InParanoid; Q9BLJ6; -.
DR   OrthoDB; 613947at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR   Gene3D; 1.20.58.120; -; 1.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   PANTHER; PTHR12329; PTHR12329; 1.
DR   Pfam; PF02179; BAG; 1.
DR   SMART; SM00264; BAG; 1.
DR   SUPFAM; SSF63491; SSF63491; 1.
DR   PROSITE; PS51035; BAG; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Developmental protein; Reference proteome; Stress response.
FT   CHAIN           1..677
FT                   /note="BAG domain-containing protein Samui"
FT                   /id="PRO_0000088878"
FT   DOMAIN          380..457
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369,
FT                   ECO:0000305"
FT   REGION          1..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..368
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  75979 MW;  3C8374CAF004FB49 CRC64;
     MESPVVLDKP PEYHGDRGFP FEEEEGSGAW SELAARHPDI AARLRQRPAT WARKRRPSSN
     DATDDFGDNF SGFDRFPFDD IPPEFREHFP SHWNRRFSSR DEQPQQQTPA SPTQPQQQTT
     ATQTEQTPTH SEHEQQTQIP QYGLRNTVDL GQKSPADPSL VDADDRTHRS MSAPPDTPNQ
     TKMSVHNHQE QTHQPHGETQ SNVRHIPIFV EGRDKPVINK SVDHGTHFGE AKPQYVPPPP
     PPHVDRDQYF ADDVNFHPPP NFSRSFGTPF NKTYRQGPQP FVQQKAYPQT AFARGASPQR
     SQSPKPTDEH FVKVPVHHET PKAEPPSRAQ KSPQQHQPPP PKSPQQHQPP PPKSPQQQPP
     PQREQTPPQP KTQQPSSNDP ITQILSIQTD VLNLMTDVEN FTGTKKDKRY LFLDEMLTRN
     LIKLDNIETD GKENIRQARK EAIKCIQKCI AVLEAKADSS NQQRKAQPEQ ETQVQDECQS
     HDVDMKENTQ NDQTTEIPAQ PIVENGEVEM DEATKEKPAE PQTAAAVPPQ TDNTEEANVE
     KQAVESAVAV EKDEKQEVVK VEAQEKSEEV KPEDANASGT VNPAETQPPA ADTRPEDNKS
     TGGDAEKKED KKSTPKKVTK TVKKRDKSKD KKDAPKDSNK EDKIEANSVL NPEPMPVDEK
     GDKTDSQVMD VDGAASQ