PSB8_CANLF
ID PSB8_CANLF Reviewed; 276 AA.
AC Q5W416;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Proteasome subunit beta type-8;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit beta-5i;
DE Flags: Precursor;
GN Name=PSMB8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Doberman pinscher;
RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA Ollier W.E.R., Binns M.M.;
RT "Genomic sequence of the class II region of the canine MHC: comparison with
RT the MHC of other mammalian species.";
RL Genomics 85:48-59(2005).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides (By similarity). May participate in the generation of spliced
CC peptides resulting from the ligation of two separate proteasomal
CC cleavage products that are not contiguous in the parental protein (By
CC similarity). Required for adipocyte differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P28062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB5. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Directly interacts with POMP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level).
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AJ630364; CAH63452.1; -; Genomic_DNA.
DR RefSeq; NP_001041550.1; NM_001048085.1.
DR RefSeq; XP_005627104.1; XM_005627047.2.
DR AlphaFoldDB; Q5W416; -.
DR SMR; Q5W416; -.
DR STRING; 9612.ENSCAFP00000001185; -.
DR MEROPS; T01.012; -.
DR PaxDb; Q5W416; -.
DR PRIDE; Q5W416; -.
DR Ensembl; ENSCAFT00030027519; ENSCAFP00030024012; ENSCAFG00030014780.
DR Ensembl; ENSCAFT00040036519; ENSCAFP00040031805; ENSCAFG00040019726.
DR Ensembl; ENSCAFT00845032467; ENSCAFP00845025385; ENSCAFG00845018353.
DR GeneID; 474865; -.
DR KEGG; cfa:474865; -.
DR CTD; 5696; -.
DR VEuPathDB; HostDB:ENSCAFG00845018353; -.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000159023; -.
DR HOGENOM; CLU_035750_7_1_1; -.
DR InParanoid; Q5W416; -.
DR OMA; IQIEMAH; -.
DR OrthoDB; 929961at2759; -.
DR TreeFam; TF106223; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000000832; Expressed in jejunum and 48 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035705; Proteasome_beta8.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF53; PTHR11599:SF53; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Hydrolase; Immunity; Nucleus; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026595"
FT CHAIN 73..276
FT /note="Proteasome subunit beta type-8"
FT /id="PRO_0000026596"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
SQ SEQUENCE 276 AA; 30499 MW; D7CA845F17D3AF4F CRC64;
MALLEVCGAP RGLRKACAVP ALGSQLRSDP GHYSFSLRAP ELAVPRGMQP TEFFQSLGEN
GEKNIRKEMV HGTTTLAFKF QHGVIVAVDS RATAGNYISS SRVNKVIEIN PSLLGTMSGC
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMVY QYRGMDLSMG SMICGWDKKG
PGLYYVDQNG TRLSGNMFST GSGSTYAYGV MDSGYQPSLS PEEAYELGRR AITYATHRDS
YSGGIINMYH MKEDGWVKVE STDVNELLHQ YQEANQ
