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Database: UniProt
Entry: F6VLC5_XENTR
LinkDB: F6VLC5_XENTR
Original site: F6VLC5_XENTR 
ID   F6VLC5_XENTR            Unreviewed;       378 AA.
AC   F6VLC5; A0A6I8QBD9; Q6GLI4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 13 {ECO:0000256|ARBA:ARBA00015732};
DE   AltName: Full=26S proteasome regulatory subunit RPN9 {ECO:0000256|ARBA:ARBA00029749};
DE   AltName: Full=26S proteasome regulatory subunit S11 {ECO:0000256|ARBA:ARBA00032323};
DE   AltName: Full=26S proteasome regulatory subunit p40.5 {ECO:0000256|ARBA:ARBA00031303};
GN   Name=psmd13 {ECO:0000313|EMBL:AAH74506.1,
GN   ECO:0000313|Ensembl:ENSXETP00000069828,
GN   ECO:0000313|RefSeq:NP_001005429.1,
GN   ECO:0000313|Xenbase:XB-GENE-1005572};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH74506.1};
RN   [1] {ECO:0000313|RefSeq:NP_001005429.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH74506.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH74506.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSXETP00000069828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000069828};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [4] {ECO:0000313|Ensembl:ENSXETP00000069828}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [5] {ECO:0000313|RefSeq:NP_001005429.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. {ECO:0000256|ARBA:ARBA00002362}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits including PSMD13, a base containing 6 ATPases
CC       and few additional components. {ECO:0000256|ARBA:ARBA00011441}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC       {ECO:0000256|ARBA:ARBA00006207}.
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DR   EMBL; BC074506; AAH74506.1; -; mRNA.
DR   RefSeq; NP_001005429.1; NM_001005429.1.
DR   DNASU; 447992; -.
DR   Ensembl; ENSXETT00000087148; ENSXETP00000069828; ENSXETG00000008827.
DR   GeneID; 447992; -.
DR   KEGG; xtr:447992; -.
DR   AGR; Xenbase:XB-GENE-1005572; -.
DR   CTD; 5719; -.
DR   Xenbase; XB-GENE-1005572; psmd13.
DR   eggNOG; KOG2908; Eukaryota.
DR   HOGENOM; CLU_042989_0_0_1; -.
DR   OMA; TWVQPRI; -.
DR   OrthoDB; 101547at2759; -.
DR   Reactome; R-XTR-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-XTR-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-XTR-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-XTR-5632684; Hedgehog 'on' state.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Reactome; R-XTR-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-XTR-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-XTR-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-XTR-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Bgee; ENSXETG00000008827; Expressed in neurula embryo and 18 other cell types or tissues.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035298; PSMD13.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10539; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 13; 1.
DR   PANTHER; PTHR10539:SF0; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 13; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Proteasome {ECO:0000313|EMBL:AAH74506.1,
KW   ECO:0000313|RefSeq:NP_001005429.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143}.
FT   DOMAIN          170..340
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
SQ   SEQUENCE   378 AA;  42985 MW;  90C5B694497A33FE CRC64;
     MRDVTGFLQQ QQSQSSAPET AAVWHRLEEL HNKKLWHQLT LELLEFVQDP ECSKGDGLIK
     LYENFISDFE HRINPLSLVE IILHVVRQMT DPSVALNFLE KTREKVKSSD EAVILCRTAI
     GALKLNIGEL QATKETIEAV EEMLGGLAGV TSVHSRFYDL SSKYYQTIGN HASYYKDALR
     FLGCTDHKEL SVSEQQDRAF TLGLAGLLGD GVYNFGELLM HPILESLRNS DRQWLIDTLY
     AFNSGNVETF RGLKTAWGQQ PDLAANEPLL LKKIQLLCLM EMTFTRPANH RQLTFEEIAK
     SAQVTVNDVE LLVMKALSVG LLRGSIDEVD KRVHITWVQP RVLDLQQIKG MKDRLEHWCT
     DVKSMEMLVE HQAHDILT
//
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