ID   PSMD3_ANOGA             Reviewed;         496 AA.
AC   O61470; Q7PW59;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 125.
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=Dox-A2; ORFNames=AGAP009082;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G3;
RX   PubMed=9988317; DOI=10.4269/ajtmh.1999.60.22;
RA   Romans P., Black W.C. IV, Sakai R.K., Gwadz R.W.;
RT   "Linkage of a gene causing malaria refractoriness to Diphenol oxidase-A2 on
RT   chromosome 3 of Anopheles gambiae.";
RL   Am. J. Trop. Med. Hyg. 60:22-29(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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:9988317}.
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DR   EMBL; AF042732; AAC18058.1; -; Genomic_DNA.
DR   EMBL; AAAB01008984; EAA14736.2; -; Genomic_DNA.
DR   RefSeq; XP_319831.2; XM_319831.2.
DR   AlphaFoldDB; O61470; -.
DR   SMR; O61470; -.
DR   STRING; 7165.AGAP009082-PA; -.
DR   PaxDb; O61470; -.
DR   GeneID; 1280037; -.
DR   KEGG; aga:AgaP_AGAP009082; -.
DR   CTD; 1280037; -.
DR   VEuPathDB; VectorBase:AGAP009082; -.
DR   eggNOG; KOG2581; Eukaryota.
DR   HOGENOM; CLU_019858_1_2_1; -.
DR   InParanoid; O61470; -.
DR   OMA; ENFGPQF; -.
DR   OrthoDB; 836599at2759; -.
DR   PhylomeDB; O61470; -.
DR   Proteomes; UP000007062; Chromosome 3R.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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..496
FT                   /note="Probable 26S proteasome non-ATPase regulatory
FT                   subunit 3"
FT                   /id="PRO_0000173819"
FT   DOMAIN          249..428
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          458..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        423
FT                   /note="S -> T (in Ref. 1; AAC18058)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  56276 MW;  E15D5F90C69B98E4 CRC64;
     MVSQTAAAAA PADPIVDVEM ESAEDAEAAK KDAELLAVQE IRDHARQIDK AVVSKEPRFI
     LRVLRSLPTT RRKLALVVVR SLAVQLYPAG PERDGIMAYI EDYPAGAQEP ELPRPRAAIK
     SPVPEVDAYF HLLLLVRLLD KNDLPKATKC SQDLMAKVVG QNRRSLDLIA AKSYFYHSRV
     AELNNDLESI RSFLHSRLRT ATLRNDFEGQ AVLINCLLRN YLHYSLYDQA DKLVNKSVFP
     ETASNNECAR FLYYLGRIKA AKLEYSVAHK QLVQALRKAP QQAAVGFRQT VQKLVIVVEL
     LLGDIPERKV FRQAALRRSL GPYFQLTQAV RMGNLQRFGE VLVNFGEQFR QDHTFTLIIR
     LRHNVIKTAI RSIGLAYSRI SPQDIARKLG LDSPEDAEFI VAKAIRDGVI EATLDPEKGY
     MRSKESTDIY STREPQLAFH QRISFCLDLH NQSVKAMRYP PKSYGKELES AEERREREQQ
     DLELAKEMAE EDDDGF