CUL5_PONAB
ID CUL5_PONAB Reviewed; 780 AA.
AC Q5RB36;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Cullin-5 {ECO:0000305};
DE Short=CUL-5 {ECO:0000305};
GN Name=CUL5 {ECO:0000250|UniProtKB:Q93034};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-
CC SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. As a scaffold protein may contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC functional specificity of the E3 ubiquitin-protein ligase complex
CC depends on the variable substrate recognition component. ECS(SOCS1)
CC seems to direct ubiquitination of JAK2. ECS(KLHDC1) complex is part of
CC the DesCEND (destruction via C-end degrons) pathway and mediates
CC ubiquitination and degradation of truncated SELENOS selenoprotein
CC produced by failed UGA/Sec decoding, which ends with a glycine. May
CC form a cell surface vasopressin receptor.
CC {ECO:0000250|UniProtKB:Q93034}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q93034}.
CC -!- SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein)
CC E3 ubiquitin-protein ligase complexes formed of CUL5, Elongin BC (ELOB
CC and ELOC), RBX2 and a variable SOCS box domain-containing protein as
CC substrate-specific recognition component. Component of the probable
CC ECS(LRRC41) complex with the substrate recognition component LRRC41.
CC Component of the probable ECS(SOCS1) complex with the substrate
CC recognition component SOCS1. Component of the probable ECS(WSB1)
CC complex with the substrate recognition subunit WSB1. Component of the
CC probable ECS(SOCS3) complex with the substrate recognition component
CC SOCS3. Component of the probable ECS(SPSB1) complex with the substrate
CC recognition component SPSB1. Component of the probable ECS(SPSB2)
CC complex with the substrate recognition component SPSB2. Component of
CC the probable ECS(SPSB4) complex with the substrate recognition
CC component SPSB4. Component of the probable ECS(RAB40C) complex with the
CC substrate recognition subunit RAB40C. Component of the probable
CC ECS(KLHDC1) complex with the substrate recognition component KLHDC1.
CC May also form complexes containing CUL5, elongin BC complex (ELOB and
CC ELOC), RBX1 and ELOA. May also form complexes containing CUL5, Elongin
CC BC (ELOB and ELOC), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41,
CC SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, ASB6,
CC ASB7 and ASB12. Interacts (when neddylated) with ARIH2; leading to
CC activate the E3 ligase activity of ARIH1. Interacts with NOS2 in the
CC presence of SPSB1 or SPSB2 or SPSB4. Interacts with ERCC6; the
CC interaction is induced by DNA damaging agents or inhibitors of RNA
CC polymerase II elongation. Interacts with ELOA (via BC-box). Interacts
CC (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and
CC DCUN1D5; these interactions promote the cullin neddylation.
CC {ECO:0000250|UniProtKB:Q93034}.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF and
CC prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN).
CC {ECO:0000250|UniProtKB:Q93034}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; CR858821; CAH91024.1; -; mRNA.
DR RefSeq; NP_001125591.1; NM_001132119.1.
DR AlphaFoldDB; Q5RB36; -.
DR SMR; Q5RB36; -.
DR STRING; 9601.ENSPPYP00000004398; -.
DR GeneID; 100172507; -.
DR KEGG; pon:100172507; -.
DR CTD; 8065; -.
DR eggNOG; KOG2285; Eukaryota.
DR InParanoid; Q5RB36; -.
DR OrthoDB; 1040292at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..780
FT /note="Cullin-5"
FT /id="PRO_0000119799"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93034"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q93034"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 780 AA; 90954 MW; 258D3C2ABA76E246 CRC64;
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG
KQGSNKKSNV EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV
RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE
EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ
DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAI YCDMLLRKTP
LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL
REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS
EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY EPQVNSPKDF
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA
