ID   PSMD3_ANOST             Reviewed;         500 AA.
AC   Q9U5Z8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable 26S proteasome non-ATPase regulatory subunit 3;
DE            Short=26S proteasome subunit S3;
DE   AltName: Full=26S proteasome regulatory subunit RPN3;
DE   AltName: Full=Diphenol oxidase A2 component;
DE            Short=DOX-A2;
GN   Name=DOXA2; Synonyms=DOX-A2;
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=StMal;
RX   PubMed=10835480; DOI=10.1007/s002390010053;
RA   Garvey C.F., Malcolm C.A.;
RT   "Anopheles stephensi Dox-A2 shares common ancestry with genes from distant
RT   groups of eukaryotes encoding a 26S proteasome subunit and is in a
RT   conserved gene cluster.";
RL   J. Mol. Evol. 50:497-509(2000).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC       the 20S proteasome, capped at one or both ends by the 19S regulatory
CC       complex (RC). The RC is composed of at least 18 different subunits in
CC       two subcomplexes, the base and the lid, which form the portions
CC       proximal and distal to the 20S proteolytic core, respectively (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be the diphenol oxidase A2 component
CC       involved in catecholamine metabolism, melanin formation and
CC       sclerotization of the cuticle. {ECO:0000305|PubMed:10835480}.
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DR   EMBL; AJ250874; CAB61220.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U5Z8; -.
DR   SMR; Q9U5Z8; -.
DR   STRING; 30069.Q9U5Z8; -.
DR   VEuPathDB; VectorBase:ASTE010126; -.
DR   VEuPathDB; VectorBase:ASTEI071952; -.
DR   VEuPathDB; VectorBase:LOC118513332; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035267; PSMD3.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF08375; Rpn3_C; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Probable 26S proteasome non-ATPase regulatory
FT                   subunit 3"
FT                   /id="PRO_0000173820"
FT   DOMAIN          253..432
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          462..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  56841 MW;  4B98EA0F702EEB5C CRC64;
     MVSQTATPTA TAASEPIVDV EMESAEDAET AKKDAELLAV QEIRDHARQI DKAVVSKEPR
     FILRVLRSLP TTRRKLALVV VGSLAVQLYP AGPERDGNQW AYIEDYPAGA QEPEGLHDPG
     SDKSPFAQEV DAYFHLLLLV RLLDKNDLPK ATKCSQDLMA KIVGQNRRSL DLIAAKCYFY
     HSRVSELNND LESIRSFLHS RLRTATLRND FEGQAVLINC LLRNYLHYSL YDQADKLVNK
     SVFPETASNN ECARFLYYLG RIKAAKLEYS VAHKQLVQAL RKAPQQAAVG FRQTVQKLVI
     VVELLLGDIP ERKVFRQAAL RRSLGPYFQL TQAVRMGNLQ RFGEVLENFG EQFRQDHTFT
     LIIRLRHNVI KTAIRSIGLA YSRISPQDIA RKLGLDSPED AEFIVAKAIR DGVIDATLDP
     EKGYMRTKES TDIYSTREPQ LAFHQRISFC LDLHNQSVKA MRYPPKSYGK ELESAEERRE
     REQQDLELAK EMAEEDDDDF