ID   PSMG1_BOVIN             Reviewed;         288 AA.
AC   Q0P5F2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Proteasome assembly chaperone 1;
GN   Name=PSMG1 {ECO:0000250|UniProtKB:O95456};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI20127.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI20127.1};
RC   TISSUE=Fetal cerebellum {ECO:0000312|EMBL:AAI20127.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone protein which promotes assembly of the 20S
CC       proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2
CC       heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes
CC       assembly of the proteasome alpha subunits into the heteroheptameric
CC       alpha ring and prevents alpha ring dimerization (By similarity).
CC       {ECO:0000250|UniProtKB:O95456}.
CC   -!- SUBUNIT: Forms a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer
CC       interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits
CC       (By similarity). {ECO:0000250|UniProtKB:O95456}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95456}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:O95456}.
CC   -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC       maturation. {ECO:0000250|UniProtKB:O95456}.
CC   -!- SIMILARITY: Belongs to the PSMG1 family. {ECO:0000255}.
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DR   EMBL; BC120126; AAI20127.1; -; mRNA.
DR   RefSeq; NP_001069815.1; NM_001076347.1.
DR   AlphaFoldDB; Q0P5F2; -.
DR   STRING; 9913.ENSBTAP00000018085; -.
DR   PaxDb; Q0P5F2; -.
DR   Ensembl; ENSBTAT00000018085; ENSBTAP00000018085; ENSBTAG00000013600.
DR   GeneID; 614817; -.
DR   KEGG; bta:614817; -.
DR   CTD; 8624; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013600; -.
DR   VGNC; VGNC:33478; PSMG1.
DR   eggNOG; ENOG502QTPH; Eukaryota.
DR   GeneTree; ENSGT00500000044950; -.
DR   HOGENOM; CLU_083637_0_0_1; -.
DR   InParanoid; Q0P5F2; -.
DR   OMA; FDCLQHR; -.
DR   OrthoDB; 1232038at2759; -.
DR   TreeFam; TF331909; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000013600; Expressed in oocyte and 105 other tissues.
DR   GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:UniProtKB.
DR   GO; GO:0080129; P:proteasome core complex assembly; IBA:GO_Central.
DR   InterPro; IPR016565; Proteasome_assmbl_chp_1.
DR   PANTHER; PTHR15069; PTHR15069; 1.
DR   Pfam; PF16094; PAC1; 1.
DR   PIRSF; PIRSF010076; Psome_chaperone-1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Endoplasmic reticulum; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   CHAIN           2..288
FT                   /note="Proteasome assembly chaperone 1"
FT                   /id="PRO_0000322546"
FT   REGION          12..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         264
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
SQ   SEQUENCE   288 AA;  33015 MW;  F0118329AE8B2EB8 CRC64;
     MAATFFGEVV RTPCRAGTEE EEEEEDGNRE TPEDREVRRQ LARKREVRLF RRQTKTTLEV
     SLLEKHPCSK FIIAIGNNAV AFLSSFVMNS GAWEEVGCAK LWNEWCRTTD TAHLSPTEAF
     CVFYHLKSNP SVMLCQCSCY VAEDQQYQWL EKVFGSCPRK NMQVTILTCR HVTDYKTSES
     TSSLHTPFLK ALKTQNFKEP PFCSLLEQPN IVHDLPAAVL SYCQVWRIPA VLYLCYTDVM
     KLDLITIEAF KPVLSSKSLK CLVKNIPQST EILKKLMTTN EIQSNIYT