ID   PSMG1_PAPAN             Reviewed;         290 AA.
AC   B0CM32;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Proteasome assembly chaperone 1;
GN   Name=PSMG1;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
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}.
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DR   EMBL; DP000537; ABY63624.1; -; Genomic_DNA.
DR   RefSeq; NP_001162555.1; NM_001169084.1.
DR   AlphaFoldDB; B0CM32; -.
DR   STRING; 9555.ENSPANP00000012973; -.
DR   GeneID; 100137593; -.
DR   KEGG; panu:100137593; -.
DR   CTD; 8624; -.
DR   eggNOG; ENOG502QTPH; Eukaryota.
DR   OrthoDB; 1232038at2759; -.
DR   Proteomes; UP000028761; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
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..290
FT                   /note="Proteasome assembly chaperone 1"
FT                   /id="PRO_0000329455"
FT   REGION          1..39
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         56
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
FT   MOD_RES         266
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O95456"
SQ   SEQUENCE   290 AA;  33053 MW;  0FAAA42B7A1987B8 CRC64;
     MAATFFGEVV KAPCRAGTED EEEEEEEEGR RETPEDREVR QQLARKREVR LLRRQTKTSL
     EVSLLEKYPC SKFIIAIGNN AVAFLSSFVM NSGVWEEVGC AKLWNEWCRT ADTTHLSSTE
     AFCGFYHLKS NPSVFLCQCS CYVAEDQQYQ WLEKVFGSCP RKNMQITILT CRHVTDYKTL
     ESTGSLPSPF LKALKTQNFK DPACCPLLEQ PNIVHDLPAA VLSYCQVWKI PAILYLCYTD
     VMKLDLITVE AFKPILSTRS LKGLVKNISQ STEILKKLMT TNEIQSNIYT