ID Q6IQ72_DANRE Unreviewed; 440 AA.
AC Q6IQ72; A0A8M1MZW2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE SubName: Full=Proteasome (Prosome, macropain) 26S subunit, ATPase, 1b {ECO:0000313|EMBL:AAH71538.1};
DE SubName: Full=Proteasome 26S subunit, ATPase 1b {ECO:0000313|Ensembl:ENSDARP00000063949, ECO:0000313|RefSeq:NP_001002091.1};
GN Name=psmc1b {ECO:0000313|EMBL:AAH71538.1,
GN ECO:0000313|Ensembl:ENSDARP00000063949,
GN ECO:0000313|RefSeq:NP_001002091.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040625-69};
GN Synonyms=wu:fj14c10 {ECO:0000313|RefSeq:NP_001002091.1}, zgc:86923
GN {ECO:0000313|RefSeq:NP_001002091.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH71538.1};
RN [1] {ECO:0000313|EMBL:AAH71538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH71538.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001002091.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16109975;
RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL Genome Res. 15:1307-1314(2005).
RN [3] {ECO:0000313|RefSeq:NP_001002091.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16412219;
RA Link V., Shevchenko A., Heisenberg C.P.;
RT "Proteomics of early zebrafish embryos.";
RL BMC Dev. Biol. 6:1-1(2006).
RN [4] {ECO:0000313|RefSeq:NP_001002091.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22805612;
RA Yang D., Liu Q., Yang M., Wu H., Wang Q., Xiao J., Zhang Y.;
RT "RNA-seq liver transcriptome analysis reveals an activated MHC-I pathway
RT and an inhibited MHC-II pathway at the early stage of vaccine immunization
RT in zebrafish.";
RL BMC Genomics 13:319-319(2012).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000063949}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000063949};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [6] {ECO:0000313|Ensembl:ENSDARP00000063949, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000063949};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [7] {ECO:0000313|RefSeq:NP_001002091.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [8] {ECO:0000313|RefSeq:NP_001002091.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; AL935145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071538; AAH71538.1; -; mRNA.
DR RefSeq; NP_001002091.1; NM_001002091.1.
DR STRING; 7955.ENSDARP00000063949; -.
DR PaxDb; 7955-ENSDARP00000063949; -.
DR Ensembl; ENSDART00000063950.7; ENSDARP00000063949.5; ENSDARG00000043561.8.
DR GeneID; 415181; -.
DR KEGG; dre:415181; -.
DR AGR; ZFIN:ZDB-GENE-040625-69; -.
DR CTD; 415181; -.
DR ZFIN; ZDB-GENE-040625-69; psmc1b.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR OMA; YCPLHIT; -.
DR OrthoDB; 1707207at2759; -.
DR TreeFam; TF106226; -.
DR Reactome; R-DRE-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-DRE-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-DRE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-DRE-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DRE-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DRE-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DRE-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DRE-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DRE-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DRE-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR Reactome; R-DRE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DRE-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-DRE-4641257; Degradation of AXIN.
DR Reactome; R-DRE-4641258; Degradation of DVL.
DR Reactome; R-DRE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-DRE-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-DRE-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-DRE-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR Reactome; R-DRE-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DRE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-DRE-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DRE-5689603; UCH proteinases.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DRE-68949; Orc1 removal from chromatin.
DR Reactome; R-DRE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DRE-69481; G2/M Checkpoints.
DR Reactome; R-DRE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DRE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DRE-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-DRE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-DRE-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-DRE-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DRE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DRE-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000000437; Chromosome 20.
DR Bgee; ENSDARG00000043561; Expressed in presomitic mesoderm and 29 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:AAH71538.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q6IQ72};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 218..357
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 49211 MW; 9578B262D2A29097 CRC64;
MGQSQSGGHG PGGGKKDDKD KKKKYEPPIP TRVGKRKRKS KGPDAASKLP LVTPHTQCRL
KLLKQDRIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGAPGT GKTLLAKAVA
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
KRRIFQIHTS RMTVAEDVSL DDLILAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
KSKENVLYKK QEGTPEGLYL
//
