KLDC3_MOUSE
ID KLDC3_MOUSE Reviewed; 382 AA.
AC Q8VEM9; Q3TCN9; Q3UR95; Q91XU6; Q99JH9; Q9DBG8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Kelch domain-containing protein 3 {ECO:0000305};
DE AltName: Full=Testis intracellular mediator protein {ECO:0000303|PubMed:12606021};
GN Name=Klhdc3 {ECO:0000312|MGI:MGI:2651568};
GN Synonyms=Peas {ECO:0000303|PubMed:12444059, ECO:0000303|PubMed:12606021};
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=12444059; DOI=10.1095/biolreprod.101.002550;
RA Ohinata Y., Sutou S., Kondo M., Takahashi T., Mitsui Y.;
RT "Male-enhanced antigen-1 gene flanked by two overlapping genes is expressed
RT in late spermatogenesis.";
RL Biol. Reprod. 67:1824-1831(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-123, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12606021; DOI=10.1016/s0014-5793(03)00036-x;
RA Ohinata Y., Sutou S., Mitsui Y.;
RT "A novel testis-specific RAG2-like protein, Peas: its expression in
RT pachytene spermatocyte cytoplasm and meiotic chromatin.";
RL FEBS Lett. 537:1-5(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-123.
RA Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-123.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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(KLHDC3) complex specifically recognizes proteins with a glycine
CC (Gly) at the C-terminus, leading to their ubiquitination and
CC degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg-
CC (Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3)
CC complex mediates ubiquitination and degradation of truncated SELENOV
CC and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which
CC end with a glycine (By similarity). May be involved in meiotic
CC recombination process (PubMed:12606021). {ECO:0000250|UniProtKB:Q9BQ90,
CC ECO:0000269|PubMed:12606021}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BQ90}.
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 KLHDC3. {ECO:0000250|UniProtKB:Q9BQ90}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12606021}.
CC Note=Also found in meiotic chromatin. {ECO:0000269|PubMed:12606021}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in testis, particularly in
CC pachytene spermatocytes. {ECO:0000269|PubMed:12606021}.
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DR EMBL; AB074009; BAB91441.1; -; Genomic_DNA.
DR EMBL; AB053465; BAB62016.1; -; mRNA.
DR EMBL; AJ278127; CAC34582.1; -; mRNA.
DR EMBL; AK004964; BAB23704.1; -; mRNA.
DR EMBL; AK141673; BAE24793.1; -; mRNA.
DR EMBL; AK170623; BAE41917.1; -; mRNA.
DR EMBL; BC018154; AAH18154.1; -; mRNA.
DR CCDS; CCDS28834.1; -.
DR RefSeq; NP_001157201.2; NM_001163729.2.
DR RefSeq; NP_082186.2; NM_027910.3.
DR RefSeq; XP_006525006.1; XM_006524943.3.
DR AlphaFoldDB; Q8VEM9; -.
DR SMR; Q8VEM9; -.
DR BioGRID; 214909; 1.
DR STRING; 10090.ENSMUSP00000071743; -.
DR PhosphoSitePlus; Q8VEM9; -.
DR MaxQB; Q8VEM9; -.
DR PaxDb; Q8VEM9; -.
DR PeptideAtlas; Q8VEM9; -.
DR PRIDE; Q8VEM9; -.
DR ProteomicsDB; 264947; -.
DR DNASU; 71765; -.
DR GeneID; 71765; -.
DR KEGG; mmu:71765; -.
DR UCSC; uc008ctw.2; mouse.
DR CTD; 116138; -.
DR MGI; MGI:2651568; Klhdc3.
DR eggNOG; KOG4693; Eukaryota.
DR InParanoid; Q8VEM9; -.
DR OrthoDB; 933937at2759; -.
DR PhylomeDB; Q8VEM9; -.
DR TreeFam; TF354289; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71765; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Klhdc3; mouse.
DR PRO; PR:Q8VEM9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VEM9; protein.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; 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; ISO:MGI.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011498; Kelch_2.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR SUPFAM; SSF117281; SSF117281; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Kelch repeat; Meiosis; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..382
FT /note="Kelch domain-containing protein 3"
FT /id="PRO_0000228996"
FT REPEAT 25..77
FT /note="Kelch 1"
FT REPEAT 88..138
FT /note="Kelch 2"
FT REPEAT 139..189
FT /note="Kelch 3"
FT REPEAT 191..249
FT /note="Kelch 4"
FT REPEAT 251..301
FT /note="Kelch 5"
FT VARIANT 123
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:12606021,
FT ECO:0000269|PubMed:16141072, ECO:0000269|Ref.3"
FT CONFLICT 2
FT /note="L -> I (in Ref. 4; BAE41917)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="A -> T (in Ref. 2; BAB62016)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="T -> A (in Ref. 4; BAB23704)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> H (in Ref. 4; BAE24793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43082 MW; 275296C5F7919B03 CRC64;
MLRWTVHLEG GPRRVNHAAV AVGHRVYSFG GYCSGEDYET LRQIDVHIFN AVSLRWTKLP
PVRPAVRGQA PVVPYMRYGH STVLIDDTVF LWGGRNDTEG ACNVLYAFDV NTHKWSTPRV
SGTVPGARDG HSACVLGKIM YIFGGYEQLA DCFSNDIHKL DTSTMTWTLV CTKGNPARWR
DFHSATMLGN HMYVFGGRAD RFGPFHSNNE IYCNRIRVFD TRTEAWLDCP HTPVLPEGRR
SHSAFGYNGE LYIFGGYNAR LNRHFHDLWK FNPGSFTWKK IEPKGKGPCP RRRQCCCIVG
DKIVLFGGTS PSPEEGLGDE FDLIDHSDLH ILDFSPSLKT LCKLAVIQYS LDQSCLPHDI
RWELNAMTTN SNISRPIVSS HG