ID   PSMG1_CALJA             Reviewed;         288 AA.
AC   B0KW86;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Proteasome assembly chaperone 1;
GN   Name=PSMG1;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JAN-2008) 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}.
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC       maturation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PSMG1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000566; ABY79109.1; -; Genomic_DNA.
DR   RefSeq; XP_002761471.1; XM_002761425.3.
DR   AlphaFoldDB; B0KW86; -.
DR   STRING; 9483.ENSCJAP00000027701; -.
DR   Ensembl; ENSCJAT00000029274; ENSCJAP00000027701; ENSCJAG00000015016.
DR   GeneID; 100398558; -.
DR   KEGG; cjc:100398558; -.
DR   CTD; 8624; -.
DR   eggNOG; ENOG502QTPH; Eukaryota.
DR   GeneTree; ENSGT00500000044950; -.
DR   HOGENOM; CLU_083637_0_0_1; -.
DR   InParanoid; B0KW86; -.
DR   OMA; FDCLQHR; -.
DR   OrthoDB; 1232038at2759; -.
DR   TreeFam; TF331909; -.
DR   Proteomes; UP000008225; Chromosome 21.
DR   Bgee; ENSCJAG00000015016; Expressed in ovary and 6 other tissues.
DR   GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR   GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR   GO; GO:0080129; P:proteasome core complex assembly; IEA:Ensembl.
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   3: Inferred from homology;
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_0000329454"
FT   REGION          1..37
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;  32849 MW;  A3046AC9261DFB99 CRC64;
     MAATFFGEVV KAPCRAGTED EEEEDEGRRE TPEDREVRQQ LARKREVRLL RRQTKTSLEV
     SLLEKYPCSK FIIAIGNNAV AFLSSFVMNS GVWEEVGCAK LWNEWCRTTD TIHLSSTEAF
     CVFYHLKSNP SVFLCQCSCY VAEDQQYQWL EKVFGSCPRK NMQITILTCR HVTDYKTSES
     TGSLPSPFLK ALKTQNFKDP ACCPLLEQPN IVHDLPAAVL SYCQVWKIPA ILYLCYTDVM
     KLDLITVEAF KPLLSTRSLK GLVKNIPQST EILKKLMTTN EIQSNIYT