ID   KLD10_RAT               Reviewed;         410 AA.
AC   Q5U3Y0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Kelch domain-containing protein 10 {ECO:0000305};
GN   Name=Klhdc10 {ECO:0000312|RGD:1309792};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC       ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC       degrons) pathway, which recognizes a C-degron located at the extreme C
CC       terminus of target proteins, leading to their ubiquitination and
CC       degradation. The C-degron recognized by the DesCEND pathway is usually
CC       a motif of less than ten residues and can be present in full-length
CC       proteins, truncated proteins or proteolytically cleaved forms. The
CC       CRL2(KLHDC10) complex specifically recognizes proteins with a proline-
CC       glycine (Pro-Gly) at the C-terminus, leading to their ubiquitination
CC       and degradation (By similarity). Participates in the oxidative stress-
CC       induced cell death through MAP3K5 activation. Inhibits PPP5C
CC       phosphatase activity on MAP3K5. Acts as a regulator of necroptosis (By
CC       similarity). {ECO:0000250|UniProtKB:Q6PAR0,
CC       ECO:0000250|UniProtKB:Q6PID8}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q6PID8}.
CC   -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC       named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC       CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC       KLHDC10. Interacts (via the 6 Kelch repeats) with PPP5C.
CC       {ECO:0000250|UniProtKB:Q6PID8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PID8}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6PID8}.
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DR   EMBL; BC085351; AAH85351.1; -; mRNA.
DR   RefSeq; NP_001017456.1; NM_001017456.1.
DR   AlphaFoldDB; Q5U3Y0; -.
DR   SMR; Q5U3Y0; -.
DR   STRING; 10116.ENSRNOP00000038586; -.
DR   iPTMnet; Q5U3Y0; -.
DR   PhosphoSitePlus; Q5U3Y0; -.
DR   PaxDb; Q5U3Y0; -.
DR   Ensembl; ENSRNOT00000034429; ENSRNOP00000038586; ENSRNOG00000010267.
DR   GeneID; 312199; -.
DR   KEGG; rno:312199; -.
DR   UCSC; RGD:1309792; rat.
DR   CTD; 23008; -.
DR   RGD; 1309792; Klhdc10.
DR   eggNOG; KOG0379; Eukaryota.
DR   GeneTree; ENSGT00940000155977; -.
DR   HOGENOM; CLU_030914_0_0_1; -.
DR   InParanoid; Q5U3Y0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5U3Y0; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000010267; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q5U3Y0; baseline and differential.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR   Gene3D; 2.120.10.80; -; 2.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   SMART; SM00612; Kelch; 2.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF50965; SSF50965; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Kelch repeat; Methylation; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..410
FT                   /note="Kelch domain-containing protein 10"
FT                   /id="PRO_0000319438"
FT   REPEAT          71..132
FT                   /note="Kelch 1"
FT   REPEAT          134..185
FT                   /note="Kelch 2"
FT   REPEAT          186..238
FT                   /note="Kelch 3"
FT   REPEAT          239..287
FT                   /note="Kelch 4"
FT   REPEAT          295..341
FT                   /note="Kelch 5"
FT   REPEAT          344..387
FT                   /note="Kelch 6"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..410
FT                   /note="Interaction with CUL2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PID8"
FT   MOD_RES         13
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PAR0"
SQ   SEQUENCE   410 AA;  45380 MW;  3E70898BEE23B92A CRC64;
     MSAAQGWDRN RRRGGGAAGG ASGVSGAGAA GGGRGTGQLN RFVQLSGRPH LPGHRPPPAR
     SGHRCVADNT NLYVFGGYNP DYDESGGPDN EDYPLFRELW RYHFATGVWH QMGTDGYMPR
     ELASMSLVLH GNNLLVFGGT GIPFGESNGN DVHVCNVKYK RWALLSCRGK RPSRIYGQAM
     ALINGSLYVF GGTTGYIYST DLHKLDLNTM VWTQLKPNNL SCDLPEERYR HEIAHDGQRI
     YILGGGTSWT AYSLNKIHAY NLETNAWEEI ATKPHEKIGF PAARRCHSCV QIKNDVFICG
     GYNGEVILGD IWKLNLQTFQ WVKLPATMPE PVYFHCAAVT PAGCMYIHGG VVNIHENKRT
     GSLFKIWLVV PSLLELAWEK LLAAFPNLAN LSRTQLLHLG LTQELIERLK