KLDC1_MOUSE
ID KLDC1_MOUSE Reviewed; 406 AA.
AC Q80YG3; Q0VDQ7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Kelch domain-containing protein 1 {ECO:0000305};
GN Name=Klhdc1 {ECO:0000303|Ref.1, ECO:0000312|MGI:MGI:2672853};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N;
RA Ng D.C.H., Chin K.-T., Zhou H.-J., Jin D.-Y.;
RT "Characterization of human and mouse kelch domain containing protein 1.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 Cul5-RING (CRL5) 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 CRL5(KLHDC1) complex mediates ubiquitination and degradation of
CC truncated SELENOS selenoprotein produced by failed UGA/Sec decoding,
CC which ends with a glycine. {ECO:0000250|UniProtKB:Q8N7A1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8N7A1}.
CC -!- SUBUNIT: Component of a CRL5 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL5, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC KLHDC1. {ECO:0000250|UniProtKB:Q8N7A1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8N7A1}.
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DR EMBL; AY238938; AAO88963.1; -; mRNA.
DR EMBL; AK144621; BAE25974.1; -; mRNA.
DR EMBL; BC119568; AAI19569.1; -; mRNA.
DR CCDS; CCDS25949.1; -.
DR RefSeq; NP_839984.1; NM_178253.5.
DR AlphaFoldDB; Q80YG3; -.
DR SMR; Q80YG3; -.
DR STRING; 10090.ENSMUSP00000068046; -.
DR PhosphoSitePlus; Q80YG3; -.
DR PaxDb; Q80YG3; -.
DR PRIDE; Q80YG3; -.
DR ProteomicsDB; 264945; -.
DR Antibodypedia; 10289; 91 antibodies from 17 providers.
DR DNASU; 271005; -.
DR Ensembl; ENSMUST00000063445; ENSMUSP00000068046; ENSMUSG00000051890.
DR GeneID; 271005; -.
DR KEGG; mmu:271005; -.
DR UCSC; uc007nrx.1; mouse.
DR CTD; 122773; -.
DR MGI; MGI:2672853; Klhdc1.
DR VEuPathDB; HostDB:ENSMUSG00000051890; -.
DR eggNOG; KOG0379; Eukaryota.
DR GeneTree; ENSGT00940000157509; -.
DR InParanoid; Q80YG3; -.
DR OMA; SCGACVH; -.
DR OrthoDB; 933937at2759; -.
DR PhylomeDB; Q80YG3; -.
DR TreeFam; TF314081; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 271005; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Klhdc1; mouse.
DR PRO; PR:Q80YG3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80YG3; protein.
DR Bgee; ENSMUSG00000051890; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q80YG3; baseline and differential.
DR Genevisible; Q80YG3; MM.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
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; IPR011498; Kelch_2.
DR Pfam; PF07646; Kelch_2; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Kelch repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..406
FT /note="Kelch domain-containing protein 1"
FT /id="PRO_0000228992"
FT REPEAT 24..76
FT /note="Kelch 1"
FT REPEAT 80..134
FT /note="Kelch 2"
FT REPEAT 135..181
FT /note="Kelch 3"
FT REPEAT 208..258
FT /note="Kelch 4"
FT REPEAT 260..307
FT /note="Kelch 5"
FT REPEAT 311..361
FT /note="Kelch 6"
SQ SEQUENCE 406 AA; 46830 MW; B1EB523A5C3D6CBF CRC64;
MADPQAFCVA EERSGHCAVV DGHFLYVWGG YVSIEDNEVY LPNDEMWTYD IDSGLWKMHL
MEGELPPSMS GSCGACIHGR LYVFGGYDDK GYSNRLYFVN LRTRDGTYTW EKITKFDGQP
PTPRDKLSCW VYKDRLIYFG GYGYRRHSEL QECFDVHDAS WEEQIFWGWH NDVHVFDTKT
RTWSQPEIKG GVPPQPRAAH SCAVLGNKGY VFGGRVLQTR MNDLHYLNLD TWVWSGRISV
NGESPKHRSW HTLTAITDDK LFLFGGLNAD NIPLSDGWIH NITTNCWKQL RHLPYTRPRL
WHTACLGKEN EIMVFGGSKD NLLFLDTGHC NDLLIFQTQP YSLLRSCLDC IGKNAIILKS
QISLLPPKLL QQVLKKITFW TAANYRKEQR IRKEETENNQ PRVSSC
