KLH42_MOUSE
ID KLH42_MOUSE Reviewed; 493 AA.
AC Q8BFQ9; Q6ZPT4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kelch-like protein 42;
DE AltName: Full=Cullin-3-binding protein 9;
DE Short=Ctb9;
DE AltName: Full=Kelch domain-containing protein 5;
GN Name=Klhl42; Synonyms=Kiaa1340, Klhdc5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-493.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex required for mitotic progression and
CC cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the
CC ubiquitination and subsequent degradation of KATNA1. Involved in
CC microtubule dynamics throughout mitosis (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at
CC least composed of CUL3 and KLHL42. Interacts (via the BTB domain) with
CC CUL3. Interacts (via the kelch domains) with KATNA1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Note=Predominantly in mitotic cells. Localized
CC diffusely in the cytoplasm during the interphase. During metaphase is
CC localized throughout the cell and more widely dispersed than the
CC microtubules. In anaphase cells is localized between the two sets of
CC separated chromosomes as well as at the spindle poles (By similarity).
CC During telophase is localized arround the nuclei of the two daughter
CC cells. Not detected at the midbody region during cytokinesis.
CC {ECO:0000250}.
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DR EMBL; AK048908; BAC33488.1; -; mRNA.
DR EMBL; AK083047; BAC38745.1; -; mRNA.
DR EMBL; AK129335; BAC98145.1; -; mRNA.
DR CCDS; CCDS39716.1; -.
DR RefSeq; NP_001074706.1; NM_001081237.1.
DR AlphaFoldDB; Q8BFQ9; -.
DR STRING; 10090.ENSMUSP00000042558; -.
DR PhosphoSitePlus; Q8BFQ9; -.
DR EPD; Q8BFQ9; -.
DR MaxQB; Q8BFQ9; -.
DR PaxDb; Q8BFQ9; -.
DR PRIDE; Q8BFQ9; -.
DR ProteomicsDB; 263656; -.
DR Antibodypedia; 12736; 128 antibodies from 26 providers.
DR Ensembl; ENSMUST00000036003; ENSMUSP00000042558; ENSMUSG00000040102.
DR GeneID; 232539; -.
DR KEGG; mmu:232539; -.
DR UCSC; uc009esu.1; mouse.
DR CTD; 57542; -.
DR MGI; MGI:2444786; Klhl42.
DR VEuPathDB; HostDB:ENSMUSG00000040102; -.
DR eggNOG; KOG1072; Eukaryota.
DR GeneTree; ENSGT00940000160124; -.
DR HOGENOM; CLU_021248_1_0_1; -.
DR InParanoid; Q8BFQ9; -.
DR OMA; LKYMSCH; -.
DR OrthoDB; 909276at2759; -.
DR PhylomeDB; Q8BFQ9; -.
DR TreeFam; TF328485; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 232539; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8BFQ9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BFQ9; protein.
DR Bgee; ENSMUSG00000040102; Expressed in dorsal pancreas and 210 other tissues.
DR ExpressionAtlas; Q8BFQ9; baseline and differential.
DR Genevisible; Q8BFQ9; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR CDD; cd18478; BACK_KLHL42_KLHDC5; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR044727; KLHL42_BACK.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF01344; Kelch_1; 2.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kelch repeat; Mitosis;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..493
FT /note="Kelch-like protein 42"
FT /id="PRO_0000119129"
FT DOMAIN 5..77
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 183..241
FT /note="Kelch 1"
FT REPEAT 242..289
FT /note="Kelch 2"
FT REPEAT 291..332
FT /note="Kelch 3"
FT REPEAT 334..379
FT /note="Kelch 4"
FT REPEAT 381..436
FT /note="Kelch 5"
FT REPEAT 438..487
FT /note="Kelch 6"
SQ SEQUENCE 493 AA; 55599 MW; FAF9F431BC07FDC6 CRC64;
MSAEEMVQIR LEDRCYPVSK SKLIEQSDYF RALYRSGMRE AVRPEVGPEV QQLRGLSAPG
LRLVLDFINA GGAREGWGLS EDELAEASVL SEMVEAASFL QVTALLRLLL SHVRLGNCLE
LYRLAQVYGL PDLQDACLRF MVLRFHQVLC QPQFPLLLSP PQAPGDCSLK QRLREARMRG
TPVLVALGDF LGGPLAPHPY QGEPPSMLRY EETTERWFPL ANNLPPDLVN VRGYGSAILD
NYLFIVGGYR ITSQEISAAH SYNPITNEWL QVASMNQKRS NFKLVAVNSK LYAIGGQAVS
NVECYNPEQD AWNFVAPLPN PLAEFSACEC KGKIYVIGGY TTRDRNMNIL QYCPSADLWT
LFETCDVHIR KQQMVSVEET IYIVGGCLHE LGPNRRSSQS EDMLTVQSYN TVTRQWLYLK
ENTSKSGLNL TCALHNDGIY IMSRDVTLST SLEHRVFLKY NIFADSWEAF RRFPAFGHNL
LISSLYLPNK AET
