PSMD6_DICDI
ID PSMD6_DICDI Reviewed; 382 AA.
AC Q55C75;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 6;
DE AltName: Full=26S proteasome regulatory subunit RPN7;
DE AltName: Full=26S proteasome regulatory subunit S10;
GN Name=psmD6; ORFNames=DDB_G0270188;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 107-118 AND 361-372, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S10 family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72444.1; -; Genomic_DNA.
DR RefSeq; XP_646606.1; XM_641514.2.
DR AlphaFoldDB; Q55C75; -.
DR SMR; Q55C75; -.
DR STRING; 44689.DDB0232985; -.
DR PaxDb; Q55C75; -.
DR EnsemblProtists; EAL72444; EAL72444; DDB_G0270188.
DR GeneID; 8617578; -.
DR KEGG; ddi:DDB_G0270188; -.
DR dictyBase; DDB_G0270188; psmD6.
DR eggNOG; KOG0687; Eukaryota.
DR HOGENOM; CLU_031814_0_0_1; -.
DR InParanoid; Q55C75; -.
DR OMA; SLYNCHY; -.
DR PhylomeDB; Q55C75; -.
DR Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q55C75; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; ISS:dictyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035268; PSMD6.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR PANTHER; PTHR14145:SF1; PTHR14145:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Proteasome; Reference proteome.
FT CHAIN 1..382
FT /note="26S proteasome non-ATPase regulatory subunit 6"
FT /id="PRO_0000327457"
FT DOMAIN 186..354
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 382 AA; 44222 MW; 6096E6CF57E536E4 CRC64;
MDESIKKLPD LAIADLIFTV KLEGKTGTES YNKLIKEIET HKMLPLYKIL VEQLKWTEDQ
GLVSKLKAEN ESELKALDNK ITDSVENFGE SEIREAYLAK SDFYCRIGDK DTAVEMYRQT
FEKTVPLGQK LDIVFTLIRM GIFWMDHDIV TRNLEKAQSL VEEGGDWDRK NRLKTYEAVY
KMSIRQFKEA SDLYLETVAS FTSTEFIDYS RFIQYLIFTS LLHLDRVSLK QKVIDSPDVL
SVINDTPKLQ DLLQSFYNGD YANFFGALAH FSDSIKGDRY LAEHSRFFTR EMRILAYNQF
LESYSSVKLE SMSNQFGVSY DFIDRELSRF VAAGRLNCKI DKVSGVIETT RSDAKNHLYK
TTLQQGDNLL NRVQKLSRVI NV
