KLHL7_HUMAN
ID KLHL7_HUMAN Reviewed; 586 AA.
AC Q8IXQ5; A4D144; B7Z5I9; G5E9G3; Q7Z765; Q96MV2; Q9BQF8; Q9UDQ9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Kelch-like protein 7;
GN Name=KLHL7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Zhang W., He L., Wan T., Zhu X., Cao X.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Pancreas, and Skin;
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).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16918702; DOI=10.1111/j.1365-3083.2006.01821.x;
RA Bredholt G., Storstein A., Haugen M., Krossnes B.K., Husebye E.,
RA Knappskog P., Vedeler C.A.;
RT "Detection of autoantibodies to the BTB-kelch protein KLHL7 in cancer
RT sera.";
RL Scand. J. Immunol. 64:325-335(2006).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE BCR(KLHL7) COMPLEX, HOMODIMERIZATION, AND
RP CHARACTERIZATION OF VARIANTS RP42 THR-153 AND VAL-153.
RX PubMed=21828050; DOI=10.1074/jbc.m111.245126;
RA Kigoshi Y., Tsuruta F., Chiba T.;
RT "Ubiquitin ligase activity of Cul3-KLHL7 protein is attenuated by autosomal
RT dominant retinitis pigmentosa causative mutation.";
RL J. Biol. Chem. 286:33613-33621(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 283-586.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the KELCH domain of human KLHL7.";
RL Submitted (AUG-2009) to the PDB data bank.
RN [12]
RP VARIANTS RP42 ASN-150; THR-153 AND VAL-153, VARIANTS ASN-255; TYR-423 AND
RP GLN-472, AND VARIANT ARG-18 (ISOFORM 2).
RX PubMed=19520207; DOI=10.1016/j.ajhg.2009.05.007;
RA Friedman J.S., Ray J.W., Waseem N., Johnson K., Brooks M.J., Hugosson T.,
RA Breuer D., Branham K.E., Krauth D.S., Bowne S.J., Sullivan L.S.,
RA Ponjavic V., Graense L., Khanna R., Trager E.H., Gieser L.M.,
RA Hughbanks-Wheaton D., Cojocaru R.I., Ghiasvand N.M., Chakarova C.F.,
RA Abrahamson M., Goering H.H.H., Webster A.R., Birch D.G., Abecasis G.R.,
RA Fann Y., Bhattacharya S.S., Daiger S.P., Heckenlively J.R., Andreasson S.,
RA Swaroop A.;
RT "Mutations in a BTB-Kelch protein, KLHL7, cause autosomal-dominant
RT retinitis pigmentosa.";
RL Am. J. Hum. Genet. 84:792-800(2009).
RN [13]
RP VARIANT RP42 VAL-153.
RX PubMed=20547956; DOI=10.1001/archophthalmol.2010.98;
RA Hugosson T., Friedman J.S., Ponjavic V., Abrahamson M., Swaroop A.,
RA Andreasson S.;
RT "Phenotype associated with mutation in the recently identified autosomal
RT dominant retinitis pigmentosa KLHL7 gene.";
RL Arch. Ophthalmol. 128:772-778(2010).
RN [14]
RP VARIANTS RP42 ASN-150; THR-153 AND VAL-153.
RX PubMed=22084217; DOI=10.1001/archophthalmol.2011.307;
RA Wen Y., Locke K.G., Klein M., Bowne S.J., Sullivan L.S., Ray J.W.,
RA Daiger S.P., Birch D.G., Hughbanks-Wheaton D.K.;
RT "Phenotypic characterization of 3 families with autosomal dominant
RT retinitis pigmentosa due to mutations in KLHL7.";
RL Arch. Ophthalmol. 129:1475-1482(2011).
RN [15]
RP VARIANTS PERCHING GLN-372; CYS-420 AND SER-421, CHARACTERIZATION OF
RP VARIANTS PERCHING GLN-372; CYS-420 AND SER-421, INVOLVEMENT IN PERCHING,
RP AND SUBCELLULAR LOCATION.
RX PubMed=27392078; DOI=10.1016/j.ajhg.2016.05.026;
RA Angius A., Uva P., Buers I., Oppo M., Puddu A., Onano S., Persico I.,
RA Loi A., Marcia L., Hoehne W., Cuccuru G., Fotia G., Deiana M., Marongiu M.,
RA Atalay H.T., Inan S., El Assy O., Smit L.M., Okur I., Boduroglu K.,
RA Utine G.E., Kilic E., Zampino G., Crisponi G., Crisponi L., Rutsch F.;
RT "Bi-allelic mutations in KLHL7 cause a Crisponi/CISS1-like phenotype
RT associated with early-onset retinitis pigmentosa.";
RL Am. J. Hum. Genet. 99:236-245(2016).
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.
CC {ECO:0000269|PubMed:21828050}.
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.
CC {ECO:0000269|PubMed:21828050}.
CC -!- INTERACTION:
CC Q8IXQ5; Q13618: CUL3; NbExp=9; IntAct=EBI-6153160, EBI-456129;
CC Q8IXQ5; Q8IXQ5: KLHL7; NbExp=7; IntAct=EBI-6153160, EBI-6153160;
CC Q8IXQ5-4; P40337-2: VHL; NbExp=3; IntAct=EBI-25895859, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16918702}. Cytoplasm
CC {ECO:0000269|PubMed:27392078}. Note=Colocalizes with CUL3 in punctate
CC structures at the perinuclear region of the cytoplasm.
CC {ECO:0000269|PubMed:27392078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IXQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXQ5-2; Sequence=VSP_038416;
CC Name=3;
CC IsoId=Q8IXQ5-3; Sequence=VSP_038417, VSP_038418;
CC Name=4;
CC IsoId=Q8IXQ5-4; Sequence=VSP_038416, VSP_038417, VSP_038418;
CC Name=5;
CC IsoId=Q8IXQ5-5; Sequence=VSP_046974;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in adult and
CC fetal heart, CNS and adult testis. {ECO:0000269|PubMed:16918702}.
CC -!- DISEASE: Perching syndrome (PERCHING) [MIM:617055]: An autosomal
CC recessive multisystem disorder characterized by global developmental
CC delay, dysmorphic facial features, feeding and respiratory difficulties
CC with poor overall growth, axial hypotonia, and joint contractures. The
CC features are variable, even within families, and may also include
CC retinitis pigmentosa, cardiac or genitourinary anomalies, and abnormal
CC sweating. {ECO:0000269|PubMed:27392078}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa 42 (RP42) [MIM:612943]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:19520207,
CC ECO:0000269|PubMed:20547956, ECO:0000269|PubMed:21828050,
CC ECO:0000269|PubMed:22084217}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF111113; AAF27196.1; -; mRNA.
DR EMBL; AL136597; CAB66532.1; -; mRNA.
DR EMBL; AK056390; BAB71175.1; -; mRNA.
DR EMBL; AK299006; BAH12925.1; -; mRNA.
DR EMBL; EF560731; ABQ59041.1; -; mRNA.
DR EMBL; AC005082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006039; AAO21916.1; -; Genomic_DNA.
DR EMBL; AC073992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24261.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93770.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93773.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93774.1; -; Genomic_DNA.
DR EMBL; BC009555; AAH09555.1; -; mRNA.
DR EMBL; BC039585; AAH39585.1; -; mRNA.
DR CCDS; CCDS34609.1; -. [Q8IXQ5-1]
DR CCDS; CCDS5378.2; -. [Q8IXQ5-5]
DR CCDS; CCDS55095.1; -. [Q8IXQ5-3]
DR RefSeq; NP_001026880.2; NM_001031710.2. [Q8IXQ5-1]
DR RefSeq; NP_001165899.1; NM_001172428.1. [Q8IXQ5-3]
DR RefSeq; NP_061334.4; NM_018846.4. [Q8IXQ5-5]
DR RefSeq; XP_016867928.1; XM_017012439.1. [Q8IXQ5-2]
DR PDB; 3II7; X-ray; 1.63 A; A=283-586.
DR PDBsum; 3II7; -.
DR AlphaFoldDB; Q8IXQ5; -.
DR SMR; Q8IXQ5; -.
DR BioGRID; 121021; 46.
DR CORUM; Q8IXQ5; -.
DR IntAct; Q8IXQ5; 28.
DR STRING; 9606.ENSP00000343273; -.
DR iPTMnet; Q8IXQ5; -.
DR PhosphoSitePlus; Q8IXQ5; -.
DR BioMuta; KLHL7; -.
DR DMDM; 116242609; -.
DR EPD; Q8IXQ5; -.
DR jPOST; Q8IXQ5; -.
DR MassIVE; Q8IXQ5; -.
DR MaxQB; Q8IXQ5; -.
DR PaxDb; Q8IXQ5; -.
DR PeptideAtlas; Q8IXQ5; -.
DR PRIDE; Q8IXQ5; -.
DR ProteomicsDB; 33929; -.
DR ProteomicsDB; 71041; -. [Q8IXQ5-1]
DR ProteomicsDB; 71042; -. [Q8IXQ5-2]
DR ProteomicsDB; 71043; -. [Q8IXQ5-3]
DR ProteomicsDB; 71044; -. [Q8IXQ5-4]
DR Antibodypedia; 25599; 104 antibodies from 19 providers.
DR DNASU; 55975; -.
DR Ensembl; ENST00000322275.9; ENSP00000323270.5; ENSG00000122550.18. [Q8IXQ5-3]
DR Ensembl; ENST00000339077.10; ENSP00000343273.4; ENSG00000122550.18. [Q8IXQ5-1]
DR Ensembl; ENST00000409689.5; ENSP00000386263.1; ENSG00000122550.18. [Q8IXQ5-5]
DR Ensembl; ENST00000410047.1; ENSP00000386999.1; ENSG00000122550.18. [Q8IXQ5-4]
DR GeneID; 55975; -.
DR KEGG; hsa:55975; -.
DR MANE-Select; ENST00000339077.10; ENSP00000343273.4; NM_001031710.3; NP_001026880.2.
DR UCSC; uc003svq.4; human. [Q8IXQ5-1]
DR CTD; 55975; -.
DR DisGeNET; 55975; -.
DR GeneCards; KLHL7; -.
DR GeneReviews; KLHL7; -.
DR HGNC; HGNC:15646; KLHL7.
DR HPA; ENSG00000122550; Tissue enhanced (heart).
DR MalaCards; KLHL7; -.
DR MIM; 611119; gene.
DR MIM; 612943; phenotype.
DR MIM; 617055; phenotype.
DR neXtProt; NX_Q8IXQ5; -.
DR OpenTargets; ENSG00000122550; -.
DR Orphanet; 157820; Cold-induced sweating syndrome.
DR Orphanet; 603689; KLHL7-related Bohring-Opitz-like syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA38392; -.
DR VEuPathDB; HostDB:ENSG00000122550; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155602; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q8IXQ5; -.
DR OMA; WRAASPM; -.
DR OrthoDB; 293214at2759; -.
DR PhylomeDB; Q8IXQ5; -.
DR TreeFam; TF351653; -.
DR PathwayCommons; Q8IXQ5; -.
DR SignaLink; Q8IXQ5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55975; 27 hits in 1123 CRISPR screens.
DR ChiTaRS; KLHL7; human.
DR EvolutionaryTrace; Q8IXQ5; -.
DR GeneWiki; KLHL7; -.
DR GenomeRNAi; 55975; -.
DR Pharos; Q8IXQ5; Tbio.
DR PRO; PR:Q8IXQ5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8IXQ5; protein.
DR Bgee; ENSG00000122550; Expressed in oocyte and 191 other tissues.
DR ExpressionAtlas; Q8IXQ5; baseline and differential.
DR Genevisible; Q8IXQ5; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW Kelch repeat; Nucleus; Reference proteome; Repeat; Retinitis pigmentosa;
KW Ubl conjugation pathway.
FT CHAIN 1..586
FT /note="Kelch-like protein 7"
FT /id="PRO_0000228988"
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 VAR_SEQ 1..48
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046974"
FT VAR_SEQ 1..40
FT /note="MAASGVEKSSKKKTEKKLAAREEAKLLAGFMGVMNNMRKQ -> MLGGTDCR
FT TFLTSHINLK (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_038416"
FT VAR_SEQ 149..166
FT /note="ISVLAECLDCPELKATAD -> EAEKVDQSLPECGMLFTV (in isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_038417"
FT VAR_SEQ 167..586
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_038418"
FT VARIANT 150
FT /note="S -> N (in RP42; dbSNP:rs137853112)"
FT /evidence="ECO:0000269|PubMed:19520207,
FT ECO:0000269|PubMed:22084217"
FT /id="VAR_060672"
FT VARIANT 153
FT /note="A -> T (in RP42; impairs interaction with CUL3 and
FT ubiquitin ligase activity of the BCR(KLHL7) complex;
FT dbSNP:rs137853114)"
FT /evidence="ECO:0000269|PubMed:19520207,
FT ECO:0000269|PubMed:21828050, ECO:0000269|PubMed:22084217"
FT /id="VAR_060673"
FT VARIANT 153
FT /note="A -> V (in RP42; impairs interaction with CUL3 and
FT ubiquitin ligase activity of the BCR(KLHL7) complex;
FT dbSNP:rs137853113)"
FT /evidence="ECO:0000269|PubMed:19520207,
FT ECO:0000269|PubMed:20547956, ECO:0000269|PubMed:21828050,
FT ECO:0000269|PubMed:22084217"
FT /id="VAR_060674"
FT VARIANT 255
FT /note="D -> N (in a patient with retinitis pigmentosa;
FT uncertain pathological significance; dbSNP:rs1227070758)"
FT /evidence="ECO:0000269|PubMed:19520207"
FT /id="VAR_060675"
FT VARIANT 372
FT /note="R -> Q (in PERCHING; subcellular localization in
FT punctate structures at the perinuclear region of cytoplasm
FT is similar to wild-type and colocalized with CUL3;
FT dbSNP:rs879255558)"
FT /evidence="ECO:0000269|PubMed:27392078"
FT /id="VAR_077161"
FT VARIANT 420
FT /note="R -> C (in PERCHING; subcellular localization in
FT punctate structures at the perinuclear region of cytoplasm
FT is similar to wild-type and colocalized with CUL3;
FT dbSNP:rs780705654)"
FT /evidence="ECO:0000269|PubMed:27392078"
FT /id="VAR_077162"
FT VARIANT 421
FT /note="C -> S (in PERCHING; subcellular localization in
FT punctate structures at the perinuclear region of cytoplasm
FT is similar to wild-type and colocalized with CUL3;
FT dbSNP:rs879255556)"
FT /evidence="ECO:0000269|PubMed:27392078"
FT /id="VAR_077163"
FT VARIANT 423
FT /note="H -> Y"
FT /evidence="ECO:0000269|PubMed:19520207"
FT /id="VAR_060676"
FT VARIANT 472
FT /note="K -> Q (in a patient with retinitis pigmentosa;
FT uncertain pathological significance)"
FT /evidence="ECO:0000269|PubMed:19520207"
FT /id="VAR_060677"
FT CONFLICT 85
FT /note="V -> L (in Ref. 8; AAH39585)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="K -> R (in Ref. 3; BAB71175)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="E -> D (in Ref. 3; BAH12925)"
FT /evidence="ECO:0000305"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 503..506
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:3II7"
FT TURN 550..553
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:3II7"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:3II7"
FT VARIANT Q8IXQ5-2:18
FT /note="K -> R (in dbSNP:rs17147682)"
FT /evidence="ECO:0000305"
FT /id="VAR_082842"
SQ SEQUENCE 586 AA; 65992 MW; FA4ED8F1567AC7A8 CRC64;
MAASGVEKSS KKKTEKKLAA REEAKLLAGF MGVMNNMRKQ KTLCDVILMV QERKIPAHRV
VLAAASHFFN LMFTTNMLES KSFEVELKDA EPDIIEQLVE FAYTARISVN SNNVQSLLDA
ANQYQIEPVK KMCVDFLKEQ VDASNCLGIS VLAECLDCPE LKATADDFIH QHFTEVYKTD
EFLQLDVKRV THLLNQDTLT VRAEDQVYDA AVRWLKYDEP NRQPFMVDIL AKVRFPLISK
NFLSKTVQAE PLIQDNPECL KMVISGMRYH LLSPEDREEL VDGTRPRRKK HDYRIALFGG
SQPQSCRYFN PKDYSWTDIR CPFEKRRDAA CVFWDNVVYI LGGSQLFPIK RMDCYNVVKD
SWYSKLGPPT PRDSLAACAA EGKIYTSGGS EVGNSALYLF ECYDTRTESW HTKPSMLTQR
CSHGMVEANG LIYVCGGSLG NNVSGRVLNS CEVYDPATET WTELCPMIEA RKNHGLVFVK
DKIFAVGGQN GLGGLDNVEY YDIKLNEWKM VSPMPWKGVT VKCAAVGSIV YVLAGFQGVG
RLGHILEYNT ETDKWVANSK VRAFPVTSCL ICVVDTCGAN EETLET
