ID PRS4_DICDI Reviewed; 439 AA.
AC Q55BV5; Q9TX40;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=26S proteasome regulatory subunit 4 homolog;
DE AltName: Full=Tat-binding protein alpha;
DE Short=DdTBPalpha;
GN Name=psmC1; ORFNames=DDB_G0270784;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=7862164; DOI=10.1128/mcb.15.3.1725;
RA Cao J.-G., Firtel R.A.;
RT "Growth and developmental functions of a human immunodeficiency virus Tat-
RT binding protein/26S protease subunit homolog from Dictyostelium
RT discoideum.";
RL Mol. Cell. Biol. 15:1725-1736(1995).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). Plays an important role in regulating both
CC growth and multicellular development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated with highest levels
CC during growth and early development. {ECO:0000269|PubMed:7862164}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72742.1; -; Genomic_DNA.
DR RefSeq; XP_646726.1; XM_641634.1.
DR AlphaFoldDB; Q55BV5; -.
DR SMR; Q55BV5; -.
DR STRING; 44689.Q55BV5; -.
DR PaxDb; 44689-DDB0232964; -.
DR EnsemblProtists; EAL72742; EAL72742; DDB_G0270784.
DR GeneID; 8617698; -.
DR KEGG; ddi:DDB_G0270784; -.
DR dictyBase; DDB_G0270784; psmC1.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; Q55BV5; -.
DR OMA; QDDTDPM; -.
DR PhylomeDB; Q55BV5; -.
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-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-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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q55BV5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..439
FT /note="26S proteasome regulatory subunit 4 homolog"
FT /id="PRO_0000328368"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 96
FT /note="K -> H (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="I -> V (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="M -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="E -> K (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..247
FT /note="TSATFL -> YLYTFK (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="L -> K (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="K -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="F -> Y (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..290
FT /note="AVG -> SVF (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..326
FT /note="VKV -> CKC (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="L -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="EI -> KL (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="E -> K (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="S -> C (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49192 MW; 4A5DC57BCF7505B7 CRC64;
MGNNQSQGQG DKGEKKDQPK YQPPPPPTQF GKKKKRRGAE TSTKLPVITP HSKCKLKQLK
LERIKDYLLM EQEFLQNYDL NQPKVDENSK EQADEKIIEE LRGDPLTVGN LEEIIDDNHA
IVSSTVGPEH YVRIMSFVDK SKLYLGATVL LNNKTLSVVG VIDGEVDPMV NVMKVEKAPT
ESYSDIGGLE AQVQEMKEAI ELPLTHPELY EEIGIKPPKG VILYGEPGTG KTLLAKAVAN
QTSATFLRVV GSELIQKYLG DGPKLVRELF RVADECAPSI VFIDEIDAVG TKRYDSQSGG
EREIQRTMLE LLNQLDGFDA RTDVKVIMAT NRIETLDPAL IRPGRIDRKI EFPLPDIKTK
RKIFEIHTAK MNLSEDVNLE EFVMSKDDLS GADIKAICTE SGLLALRERR MRVTHTDFKK
AKEKVLYRKT AGAPEGLYM
//
