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   27-MAR-2024, entry version 177.
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=12; 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.
DR   PDB; 3II7; X-ray; 1.63 A; A=283-586.
DR   PDBsum; 3II7; -.
DR   AlphaFoldDB; Q8IXQ5; -.
DR   SMR; Q8IXQ5; -.
DR   BioGRID; 121021; 52.
DR   ComplexPortal; CPX-8084; CRL3 E3 ubiquitin ligase complex, KLHL7 variant.
DR   CORUM; Q8IXQ5; -.
DR   IntAct; Q8IXQ5; 32.
DR   MINT; Q8IXQ5; -.
DR   STRING; 9606.ENSP00000343273; -.
DR   GlyGen; Q8IXQ5; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000343273; -.
DR   PeptideAtlas; 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   Pumba; Q8IXQ5; -.
DR   Antibodypedia; 25599; 121 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   AGR; HGNC:15646; -.
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; 603684; KLHL7-related Bohring-Opitz-like and Crisponi/Cold-induced sweating-like overlap syndrome.
DR   Orphanet; 603689; KLHL7-related Bohring-Opitz-like syndrome.
DR   Orphanet; 603694; KLHL7-related Crisponi/cold-induced sweating-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; 5472491at2759; -.
DR   PhylomeDB; Q8IXQ5; -.
DR   TreeFam; TF351653; -.
DR   PathwayCommons; Q8IXQ5; -.
DR   SignaLink; Q8IXQ5; -.
DR   SIGNOR; Q8IXQ5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 55975; 29 hits in 1203 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 193 other cell types or tissues.
DR   ExpressionAtlas; Q8IXQ5; baseline and differential.
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   CDD; cd18447; BACK_KLHL7; 1.
DR   CDD; cd18237; BTB_POZ_KLHL7; 1.
DR   Gene3D; 1.25.40.420; -; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR030599; BTB/POZ_KLHL7.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR047060; KLHL7_BACK.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR   PANTHER; PTHR24412:SF435; KELCH-LIKE PROTEIN 7; 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; Kelch motif; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   Genevisible; Q8IXQ5; HS.
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 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 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
//