KLHL7_MOUSE
ID KLHL7_MOUSE Reviewed; 586 AA.
AC Q8BUL5; Q9CZP4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kelch-like protein 7;
GN Name=Klhl7;
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=Thymus;
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).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating
CC ubiquitination and subsequent degradation of substrate proteins.
CC Probably mediates 'Lys-48'-linked ubiquitination (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Component of the BCR(KLHL7) E3 ubiquitin ligase
CC complex, at least composed of CUL3 and KLHL7 and RBX1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXQ5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IXQ5}. Note=Colocalizes with CUL3 in punctate
CC structures at the perinuclear region of the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8IXQ5}.
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DR EMBL; AK012326; BAB28163.1; -; mRNA.
DR EMBL; AK083358; BAC38883.1; -; mRNA.
DR CCDS; CCDS19114.1; -.
DR RefSeq; NP_080724.2; NM_026448.3.
DR AlphaFoldDB; Q8BUL5; -.
DR SMR; Q8BUL5; -.
DR BioGRID; 206516; 32.
DR IntAct; Q8BUL5; 1.
DR STRING; 10090.ENSMUSP00000030841; -.
DR iPTMnet; Q8BUL5; -.
DR PhosphoSitePlus; Q8BUL5; -.
DR EPD; Q8BUL5; -.
DR jPOST; Q8BUL5; -.
DR MaxQB; Q8BUL5; -.
DR PaxDb; Q8BUL5; -.
DR PeptideAtlas; Q8BUL5; -.
DR PRIDE; Q8BUL5; -.
DR ProteomicsDB; 263633; -.
DR Antibodypedia; 25599; 104 antibodies from 19 providers.
DR Ensembl; ENSMUST00000030841; ENSMUSP00000030841; ENSMUSG00000028986.
DR GeneID; 52323; -.
DR KEGG; mmu:52323; -.
DR UCSC; uc008wqy.2; mouse.
DR CTD; 55975; -.
DR MGI; MGI:1196453; Klhl7.
DR VEuPathDB; HostDB:ENSMUSG00000028986; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155602; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q8BUL5; -.
DR OMA; WRAASPM; -.
DR OrthoDB; 293214at2759; -.
DR PhylomeDB; Q8BUL5; -.
DR TreeFam; TF351653; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 52323; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Klhl7; mouse.
DR PRO; PR:Q8BUL5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BUL5; protein.
DR Bgee; ENSMUSG00000028986; Expressed in cortical plate and 250 other tissues.
DR ExpressionAtlas; Q8BUL5; baseline and differential.
DR Genevisible; Q8BUL5; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030599; KLHL7.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF435; PTHR24412:SF435; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Kelch repeat; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..586
FT /note="Kelch-like protein 7"
FT /id="PRO_0000228989"
FT DOMAIN 44..111
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 146..248
FT /note="BACK"
FT REPEAT 294..336
FT /note="Kelch 1"
FT REPEAT 337..382
FT /note="Kelch 2"
FT REPEAT 383..430
FT /note="Kelch 3"
FT REPEAT 431..481
FT /note="Kelch 4"
FT REPEAT 483..528
FT /note="Kelch 5"
FT REPEAT 530..575
FT /note="Kelch 6"
FT CONFLICT 529
FT /note="V -> D (in Ref. 1; BAB28163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 65938 MW; 1E676E01FA143653 CRC64;
MATSGVEKSS KKKTEKKLAA REEAKLLAGF MGVMNNMRKQ RTLCDVILTV QERKIPAHRV
VLAAASHFFN LMFTTNMLES KSFEVELKDA EPDIIEQLVE FAYTARISVN SNNVQSLLDA
ANQYQIEPVK KMCVDFLKEQ VDASNCLGIS VLAECLDCPE LKATADDFIH QHFTEVYKTD
EFLQLDVKRV THLLSQDTLT VRAEDQVYDA AVRWLKYDEP NRQPFMVDIL AKVRFPLISK
NFLSKTVQAE PLIQDNPECL KMVISGMRYH LLSPEDREEL AGGTRPRRKK HDYRIALFGG
SQPQSCRYFN PKDYSWTDIR CPFEKRRDAA CVFWDNVVYI LGGSQLFPIK RMDCYNVVKD
SWYSKLGPPT PRDSLAACAA EGKIYTSGGS EVGNSALYLF ECYDTRTESW HTKPSMLTQR
CSHGMVEANG LIYVCGGSLG NNVSGRVLSS CEVYDPATET WTELCSMIEP RKNHGLVFVK
DKIFAVGGQN GLGGLDNVEY YDIKLNEWKM VSPMPWRGVT VKCAAVGSVI YVLAGFQGVG
RLGHILEYNT ETDKWIANSK VRAFPVTSCL ICVVDTCGAN EETLET
