ID   KLD10_BOVIN             Reviewed;         442 AA.
AC   Q0IIC2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Kelch domain-containing protein 10;
GN   Name=KLHDC10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC122712; AAI22713.1; -; mRNA.
DR   RefSeq; NP_001068695.1; NM_001075227.1.
DR   AlphaFoldDB; Q0IIC2; -.
DR   SMR; Q0IIC2; -.
DR   STRING; 9913.ENSBTAP00000000718; -.
DR   PaxDb; Q0IIC2; -.
DR   PRIDE; Q0IIC2; -.
DR   Ensembl; ENSBTAT00000000718; ENSBTAP00000000718; ENSBTAG00000000548.
DR   GeneID; 505844; -.
DR   KEGG; bta:505844; -.
DR   CTD; 23008; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000548; -.
DR   VGNC; VGNC:30634; KLHDC10.
DR   eggNOG; KOG0379; Eukaryota.
DR   GeneTree; ENSGT00940000155977; -.
DR   HOGENOM; CLU_030914_0_0_1; -.
DR   InParanoid; Q0IIC2; -.
DR   OMA; HCDMPEE; -.
DR   OrthoDB; 564212at2759; -.
DR   TreeFam; TF314081; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000000548; Expressed in spermatid and 106 other tissues.
DR   ExpressionAtlas; Q0IIC2; 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:0005654; C:nucleoplasm; IEA:Ensembl.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Kelch repeat; Methylation; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..442
FT                   /note="Kelch domain-containing protein 10"
FT                   /id="PRO_0000319435"
FT   REPEAT          103..164
FT                   /note="Kelch 1"
FT   REPEAT          166..217
FT                   /note="Kelch 2"
FT   REPEAT          218..270
FT                   /note="Kelch 3"
FT   REPEAT          271..319
FT                   /note="Kelch 4"
FT   REPEAT          327..373
FT                   /note="Kelch 5"
FT   REPEAT          376..419
FT                   /note="Kelch 6"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..442
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   442 AA;  49111 MW;  98BC3FFF786949B9 CRC64;
     MSAAQGWDRN RRRGGGAAGG GGGGSGAGGG SGGNGGRGTG QLNRFVQLSG RPHLPGKKKI
     RWDPVRRRFI QSCPIIRIPN RFLRGHRPPP ARSGHRCVAD NTNLYVFGGY NPDYDESGGP
     DNEDYPLFRE LWRYHFATGV WHQMGTDGYM PRELASMSLV LHGNNLLVFG GTGIPFGESN
     GNDVHVCNVK YKRWALLSCR GKKPSRIYGQ AMAIINGSLY VFGGTTGYIY STDLHKLDLN
     TREWTQLKPN NLSCDLPEER YRHEIAHDGQ RIYILGGGTS WTAYSLNKIH AYNLETNAWE
     EIATKPHEKI GFPAARRCHS CVQIKNDVFI CGGYNGEVIL GDIWKLNLQT FQWVKLPATM
     PEPVYFHCAA VTPAGCMYIH GGVVNIHENK RTGSLFKIWL VVPSLLELAW EKLLAAFPNL
     ANLSRTQLLH LGLTQGLIER LK