ID   PSMF1_PONAB             Reviewed;         271 AA.
AC   Q5RDN3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Proteasome inhibitor PI31 subunit;
GN   Name=PSMF1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in control of proteasome function.
CC       Inhibits the hydrolysis of protein and peptide substrates by the 20S
CC       proteasome. Also inhibits the activation of the proteasome by the
CC       proteasome regulatory proteins PA700 and PA28 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with FBXO7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC       {ECO:0000305}.
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DR   EMBL; CR857871; CAH90124.1; -; mRNA.
DR   RefSeq; NP_001125022.1; NM_001131550.1.
DR   AlphaFoldDB; Q5RDN3; -.
DR   SMR; Q5RDN3; -.
DR   STRING; 9601.ENSPPYP00000012129; -.
DR   Ensembl; ENSPPYT00000012607; ENSPPYP00000012129; ENSPPYG00000010859.
DR   GeneID; 100171902; -.
DR   KEGG; pon:100171902; -.
DR   CTD; 9491; -.
DR   eggNOG; KOG4761; Eukaryota.
DR   GeneTree; ENSGT00390000012257; -.
DR   HOGENOM; CLU_090116_0_0_1; -.
DR   InParanoid; Q5RDN3; -.
DR   OMA; NICVEPE; -.
DR   OrthoDB; 1614691at2759; -.
DR   TreeFam; TF106238; -.
DR   Proteomes; UP000001595; Chromosome 20.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR045128; PI31-like.
DR   InterPro; IPR013886; PI31_Prot_C.
DR   InterPro; IPR021625; PI31_Prot_N.
DR   PANTHER; PTHR13266; PTHR13266; 1.
DR   Pfam; PF08577; PI31_Prot_C; 1.
DR   Pfam; PF11566; PI31_Prot_N; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Methylation; Phosphoprotein;
KW   Proteasome; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   CHAIN           2..271
FT                   /note="Proteasome inhibitor PI31 subunit"
FT                   /id="PRO_0000220922"
FT   REGION          2..150
FT                   /note="Important for homodimerization and interaction with
FT                   FBXO7"
FT                   /evidence="ECO:0000250"
FT   REGION          222..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..263
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         205
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT   MOD_RES         219
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT   MOD_RES         231
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
SQ   SEQUENCE   271 AA;  29804 MW;  1FF48F68B4A93310 CRC64;
     MAGLEVLFAS AAPAITCTQD ALVCFLHWEV VTHGYYALGV GDQPGPNDKK SELLPAGWNN
     NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF
     HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR
     QPPWCDPLGP FAVGGEDLDP FGHRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG
     ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L