ID A0A5F9CKV7_RABIT Unreviewed; 304 AA.
AC A0A5F9CKV7;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000034095.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000034095.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000034095.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000034095.1};
RG Ensembl;
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 AlphaFoldDB; A0A5F9CKV7; -.
DR Ensembl; ENSOCUT00000063067.1; ENSOCUP00000034095.1; ENSOCUG00000004610.4.
DR GeneTree; ENSGT00390000001802; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000004610; Expressed in embryo and 16 other cell types or tissues.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProt.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 99..266
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
SQ SEQUENCE 304 AA; 34420 MW; D4C4A46493910A51 CRC64;
MVSLSFMKIS SVNLNTDPNV ALTFLEKTRE KVKSSDEAVI LCKTAIGALK LNIGDLQVTK
ETIEDVEEML SNLPGVTSVH SRFYDLSSKY YQTTGNHASY YKDALRFLGC VDIKDLPVSE
QQERAFTLGL AGLLGEGVFN FGELLMHPVL ESLRNTDRQW LIDTLYAFNS GNVERFQTLK
AAWGQQPDLA ANEAQLLRKI QLLCLMEMTF TRPANHRQLT FEEIAQSAKI TVNEVELLVM
KALSVGLVKG SIDEVDKRVH MTWVQPRVLD LQQIKGMKDR LEFWCTDVKS MEMLVERQAH
DILT
//
