ID H3A4V8_LATCH Unreviewed; 260 AA.
AC H3A4V8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN Name=LOC102365115 {ECO:0000313|Ensembl:ENSLACP00000004679.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004679.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004679.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a
CC chymotrypsin-like activity. {ECO:0000256|ARBA:ARBA00003802}.
CC -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC complex which is characterized by its ability to cleave peptides with
CC Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. {ECO:0000256|RuleBase:RU004203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC -!- SUBUNIT: Component of the proteasome complex.
CC {ECO:0000256|RuleBase:RU004203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC Nucleus {ECO:0000256|RuleBase:RU004203}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC {ECO:0000256|RuleBase:RU004203}.
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DR EMBL; AFYH01244520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A4V8; -.
DR STRING; 7897.ENSLACP00000004679; -.
DR MEROPS; T01.012; -.
DR Ensembl; ENSLACT00000004718.1; ENSLACP00000004679.1; ENSLACG00000004162.1.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000157841; -.
DR HOGENOM; CLU_035750_7_3_1; -.
DR InParanoid; H3A4V8; -.
DR OMA; RAFSFGC; -.
DR TreeFam; TF106223; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03761; proteasome_beta_type_5; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF10; PROTEASOME SUBUNIT BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 260 AA; 28817 MW; FCDADEF7CDAB35AE CRC64;
MALADVLRVE SAAFQFGLPG SLVLGPGPVG LSLVALKLIG LGEEEENQVP KIKFLHRTTT
LAFKFFHGVL VAVDSHTMVG SYIDSQTVKK VIEINPYLLG TMVGGAADCS FWERLLARQC
CIYELRNNER ISVAAASKLL AHMVYQYKGM GLSKGTMICG WDKQGPGLYF VDSEGNWITG
DNFSVGSGSV YAYGVLDRGY HFDLSVEEAN DLARCAIYHT TYRDAYSGRV VNIYHVREDG
WFCVFQDNIL QLREEFQEAA
//
