KIF7_HUMAN
ID KIF7_HUMAN Reviewed; 1343 AA.
AC Q2M1P5; Q3SXY0; Q6UXE9; Q8IW72;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Kinesin-like protein KIF7;
GN Name=KIF7; ORFNames=UNQ340/PRO539;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1343.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-1343, AND VARIANTS ILE-958
RP AND ARG-1005.
RC TISSUE=Heart, Lung, and Ovary;
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 [4]
RP IDENTIFICATION.
RX PubMed=15547730;
RA Katoh Y., Katoh M.;
RT "Characterization of KIF7 gene in silico.";
RL Int. J. Oncol. 25:1881-1886(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GLI1; GLI2; GLI3; SMO AND SUFU.
RX PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
RA Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
RA Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
RA Peterson A.S.;
RT "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh
RT signal transduction during development.";
RL Curr. Biol. 19:1320-1326(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, INTERACTION WITH NPHP1, TISSUE SPECIFICITY, AND VARIANT JBTS12
RP 1329-ARG--SER-1332 DEL.
RX PubMed=21633164; DOI=10.1172/jci43639;
RA Dafinger C., Liebau M.C., Elsayed S.M., Hellenbroich Y., Boltshauser E.,
RA Korenke G.C., Fabretti F., Janecke A.R., Ebermann I., Nurnberg G.,
RA Nurnberg P., Zentgraf H., Koerber F., Addicks K., Elsobky E., Benzing T.,
RA Schermer B., Bolz H.J.;
RT "Mutations in KIF7 link Joubert syndrome with Sonic Hedgehog signaling and
RT microtubule dynamics.";
RL J. Clin. Invest. 121:2662-2667(2011).
RN [10]
RP INVOLVEMENT IN CILIOPATHIES, INVOLVEMENT IN HLS2, VARIANTS BBS GLY-641;
RP ARG-994 AND TRP-1068, VARIANT ACLS GLN-702, VARIANTS LEU-632; PRO-759;
RP ARG-834 AND GLN-1115, CHARACTERIZATION OF VARIANTS BBS GLY-641; ARG-994 AND
RP TRP-1068, CHARACTERIZATION OF VARIANT ACLS GLN-702, AND CHARACTERIZATION OF
RP VARIANTS PRO-759 AND ARG-834.
RX PubMed=21552264; DOI=10.1038/ng.826;
RA Putoux A., Thomas S., Coene K.L., Davis E.E., Alanay Y., Ogur G., Uz E.,
RA Buzas D., Gomes C., Patrier S., Bennett C.L., Elkhartoufi N., Frison M.H.,
RA Rigonnot L., Joye N., Pruvost S., Utine G.E., Boduroglu K., Nitschke P.,
RA Fertitta L., Thauvin-Robinet C., Munnich A., Cormier-Daire V., Hennekam R.,
RA Colin E., Akarsu N.A., Bole-Feysot C., Cagnard N., Schmitt A., Goudin N.,
RA Lyonnet S., Encha-Razavi F., Siffroi J.P., Winey M., Katsanis N.,
RA Gonzales M., Vekemans M., Beales P.L., Attie-Bitach T.;
RT "KIF7 mutations cause fetal hydrolethalus and acrocallosal syndromes.";
RL Nat. Genet. 43:601-606(2011).
RN [11]
RP INVOLVEMENT IN ACLS.
RX PubMed=23125460; DOI=10.1136/jmedgenet-2012-101016;
RA Putoux A., Nampoothiri S., Laurent N., Cormier-Daire V., Beales P.L.,
RA Schinzel A., Bartholdi D., Alby C., Thomas S., Elkhartoufi N., Ichkou A.,
RA Litzler J., Munnich A., Encha-Razavi F., Kannan R., Faivre L., Boddaert N.,
RA Rauch A., Vekemans M., Attie-Bitach T.;
RT "Novel KIF7 mutations extend the phenotypic spectrum of acrocallosal
RT syndrome.";
RL J. Med. Genet. 49:713-720(2012).
RN [12]
RP INVOLVEMENT IN AGBK, AND VARIANT AGBK SER-1060.
RX PubMed=22587682; DOI=10.1186/1750-1172-7-27;
RA Ali B.R., Silhavy J.L., Akawi N.A., Gleeson J.G., Al-Gazali L.;
RT "A mutation in KIF7 is responsible for the autosomal recessive syndrome of
RT macrocephaly, multiple epiphyseal dysplasia and distinctive facial
RT appearance.";
RL Orphanet J. Rare Dis. 7:27-27(2012).
RN [13]
RP INVOLVEMENT IN ACLS, AND VARIANTS ACLS GLN-154; MET-828; LYS-987 AND
RP TRP-1122.
RX PubMed=26174511; DOI=10.1002/ajmg.a.37249;
RA Tunovic S., Baranano K.W., Barkovich J.A., Strober J.B., Jamal L.,
RA Slavotinek A.M.;
RT "Novel KIF7 missense substitutions in two patients presenting with multiple
RT malformations and features of acrocallosal syndrome.";
RL Am. J. Med. Genet. A 167A:2767-2776(2015).
CC -!- FUNCTION: Essential for hedgehog signaling regulation: acts as both a
CC negative and positive regulator of sonic hedgehog (Shh) and Indian
CC hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-
CC dependent and -independent mechanisms (PubMed:21633164). Involved in
CC the regulation of microtubular dynamics. Required for proper
CC organization of the ciliary tip and control of ciliary localization of
CC SUFU-GLI2 complexes (By similarity). Required for localization of GLI3
CC to cilia in response to Shh. Negatively regulates Shh signaling by
CC preventing inappropriate activation of the transcriptional activator
CC GLI2 in the absence of ligand. Positively regulates Shh signaling by
CC preventing the processing of the transcription factor GLI3 into its
CC repressor form. In keratinocytes, promotes the dissociation of SUFU-
CC GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation
CC (By similarity). Involved in the regulation of epidermal
CC differentiation and chondrocyte development (By similarity).
CC {ECO:0000250|UniProtKB:B7ZNG0, ECO:0000269|PubMed:21633164}.
CC -!- SUBUNIT: Can form homodimers and interacts with microtubules (By
CC similarity). Interacts with GLI1, GLI2, GLI3, SMO and SUFU
CC (PubMed:19592253). Interacts with NPHP1 (PubMed:21633164). Interacts
CC with SMO and DLG5 (via PDZ4 or guanylate kinase-like domain) (By
CC similarity). {ECO:0000250|UniProtKB:B7ZNG0,
CC ECO:0000269|PubMed:19592253, ECO:0000269|PubMed:21633164}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:19592253}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:B7ZNG0}. Note=Localizes to the cilium tip.
CC -!- TISSUE SPECIFICITY: Embryonic stem cells, melanotic melanoma and Jurkat
CC T-cells. Expressed in heart, lung, liver, kidney, testis, retina,
CC placenta, pancreas, colon, small intestin, prostate and thymus.
CC {ECO:0000269|PubMed:21633164}.
CC -!- PTM: Polyubiquitinated by UBR3. {ECO:0000250|UniProtKB:B7ZNG0}.
CC -!- DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of
CC disorders, collectively termed ciliopathies. The ciliopathy range of
CC diseases includes Meckel-Gruber syndrome, Bardet-Biedl syndrome,
CC Joubert syndrome, and hydrolethalus syndrome among others. Single-locus
CC allelism is insufficient to explain the variable penetrance and
CC expressivity of such disorders, leading to the suggestion that
CC variations across multiple sites of the ciliary proteome influence the
CC clinical outcome. Primary ciliopathy loci can be modulated by
CC pathogenic lesions in other ciliary genes to either exacerbate overall
CC severity or induce specific endophenotypes. KIF7 may be causally
CC associated with diverse ciliopathies, and also acts as a modifier gene
CC across the ciliopathy spectrum.
CC -!- DISEASE: Bardet-Biedl syndrome (BBS) [MIM:209900]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:21552264}. Note=The gene represented in this entry
CC may act as a disease modifier. Heterozygous missense mutations in KIF7
CC may genetically interact with other BBS genes and contribute to disease
CC manifestation and severity.
CC -!- DISEASE: Hydrolethalus syndrome 2 (HLS2) [MIM:614120]: An embryonic
CC lethal disorder characterized by hydrocephaly or anencephaly, postaxial
CC polydactyly of the upper limbs, and pre- or postaxial polydactyly of
CC the lower limbs. Duplication of the hallux is a common finding.
CC {ECO:0000269|PubMed:21552264}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Acrocallosal syndrome (ACLS) [MIM:200990]: An autosomal
CC recessive syndrome characterized by hypogenesis or agenesis of the
CC corpus callosum. Clinical features include postaxial polydactyly,
CC hallux duplication, macrocephaly, craniofacial abnormalities, severe
CC developmental delay and intellectual disability.
CC {ECO:0000269|PubMed:21552264, ECO:0000269|PubMed:23125460,
CC ECO:0000269|PubMed:26174511}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Joubert syndrome 12 (JBTS12) [MIM:200990]: A disorder
CC presenting with cerebellar ataxia, oculomotor apraxia, hypotonia,
CC neonatal breathing abnormalities and psychomotor delay.
CC Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy and renal
CC disease. {ECO:0000269|PubMed:21633164}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Al-Gazali-Bakalinova syndrome (AGBK) [MIM:607131]: An
CC autosomal recessive syndrome consisting of macrocephaly, multiple
CC epiphyseal dysplasia and distinctive facial appearance.
CC {ECO:0000269|PubMed:22587682}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF27 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI04045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI12272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI12274.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ88750.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC079075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY358384; AAQ88750.1; ALT_INIT; mRNA.
DR EMBL; BC040878; AAH40878.1; -; mRNA.
DR EMBL; BC104044; AAI04045.1; ALT_INIT; mRNA.
DR EMBL; BC112271; AAI12272.1; ALT_INIT; mRNA.
DR EMBL; BC112273; AAI12274.1; ALT_INIT; mRNA.
DR CCDS; CCDS32325.2; -.
DR RefSeq; NP_940927.2; NM_198525.2.
DR PDB; 2XT3; X-ray; 1.88 A; A=8-347.
DR PDB; 4A14; X-ray; 1.60 A; A=8-347.
DR PDB; 6MLQ; EM; 4.20 A; C=1-398.
DR PDB; 6MLR; EM; 4.20 A; C=1-398.
DR PDBsum; 2XT3; -.
DR PDBsum; 4A14; -.
DR PDBsum; 6MLQ; -.
DR PDBsum; 6MLR; -.
DR AlphaFoldDB; Q2M1P5; -.
DR SMR; Q2M1P5; -.
DR BioGRID; 131912; 135.
DR IntAct; Q2M1P5; 72.
DR MINT; Q2M1P5; -.
DR STRING; 9606.ENSP00000377934; -.
DR ChEMBL; CHEMBL2021751; -.
DR iPTMnet; Q2M1P5; -.
DR PhosphoSitePlus; Q2M1P5; -.
DR BioMuta; KIF7; -.
DR DMDM; 172045866; -.
DR EPD; Q2M1P5; -.
DR jPOST; Q2M1P5; -.
DR MassIVE; Q2M1P5; -.
DR MaxQB; Q2M1P5; -.
DR PaxDb; Q2M1P5; -.
DR PeptideAtlas; Q2M1P5; -.
DR PRIDE; Q2M1P5; -.
DR ProteomicsDB; 61341; -.
DR Antibodypedia; 51762; 110 antibodies from 21 providers.
DR DNASU; 374654; -.
DR Ensembl; ENST00000394412.8; ENSP00000377934.3; ENSG00000166813.16.
DR GeneID; 374654; -.
DR KEGG; hsa:374654; -.
DR MANE-Select; ENST00000394412.8; ENSP00000377934.3; NM_198525.3; NP_940927.2.
DR UCSC; uc002bof.3; human.
DR CTD; 374654; -.
DR DisGeNET; 374654; -.
DR GeneCards; KIF7; -.
DR GeneReviews; KIF7; -.
DR HGNC; HGNC:30497; KIF7.
DR HPA; ENSG00000166813; Low tissue specificity.
DR MalaCards; KIF7; -.
DR MIM; 200990; phenotype.
DR MIM; 209900; phenotype.
DR MIM; 607131; phenotype.
DR MIM; 611254; gene.
DR MIM; 614120; phenotype.
DR neXtProt; NX_Q2M1P5; -.
DR OpenTargets; ENSG00000166813; -.
DR Orphanet; 36; Acrocallosal syndrome.
DR Orphanet; 2189; Hydrolethalus.
DR Orphanet; 166024; Multiple epiphyseal dysplasia, Al-Gazali type.
DR Orphanet; 2754; Orofaciodigital syndrome type 6.
DR PharmGKB; PA134871338; -.
DR VEuPathDB; HostDB:ENSG00000166813; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000159749; -.
DR HOGENOM; CLU_005591_0_0_1; -.
DR InParanoid; Q2M1P5; -.
DR OMA; HPCLARK; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q2M1P5; -.
DR TreeFam; TF325946; -.
DR PathwayCommons; Q2M1P5; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR SignaLink; Q2M1P5; -.
DR SIGNOR; Q2M1P5; -.
DR BioGRID-ORCS; 374654; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; KIF7; human.
DR GenomeRNAi; 374654; -.
DR Pharos; Q2M1P5; Tbio.
DR PRO; PR:Q2M1P5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q2M1P5; protein.
DR Bgee; ENSG00000166813; Expressed in ascending aorta and 111 other tissues.
DR ExpressionAtlas; Q2M1P5; baseline and differential.
DR Genevisible; Q2M1P5; HS.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Bardet-Biedl syndrome; Cell projection;
KW Ciliopathy; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Intellectual disability; Joubert syndrome; Motor protein;
KW Nucleotide-binding; Obesity; Phosphoprotein; Reference proteome; Repressor;
KW Ubl conjugation.
FT CHAIN 1..1343
FT /note="Kinesin-like protein KIF7"
FT /id="PRO_0000307146"
FT DOMAIN 15..349
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 356..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..1206
FT /note="Interaction with SMO"
FT /evidence="ECO:0000250|UniProtKB:B7ZNG0"
FT REGION 358..479
FT /note="Interaction with DLG5"
FT /evidence="ECO:0000250|UniProtKB:B7ZNG0"
FT REGION 451..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..775
FT /note="Sufficient for interaction with NPHP1"
FT /evidence="ECO:0000269|PubMed:21633164"
FT REGION 611..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..542
FT /evidence="ECO:0000255"
FT COILED 698..1057
FT /evidence="ECO:0000255"
FT COILED 1109..1211
FT /evidence="ECO:0000255"
FT COMPBIAS 356..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B7ZNG0"
FT VARIANT 52
FT /note="D -> N (in dbSNP:rs8179065)"
FT /id="VAR_061287"
FT VARIANT 154
FT /note="R -> Q (in ACLS; atypical phenotype; unknown
FT pathological significance; dbSNP:rs180758272)"
FT /evidence="ECO:0000269|PubMed:26174511"
FT /id="VAR_077692"
FT VARIANT 632
FT /note="P -> L (in dbSNP:rs115857753)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066450"
FT VARIANT 641
FT /note="R -> G (in BBS; the patient also carries homozygous
FT mutation R-390 in BBS1; may affect splicing; hypomorphic
FT variant in vitro; dbSNP:rs137905815)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066451"
FT VARIANT 702
FT /note="R -> Q (in ACLS; may affect splicing; hypomorphic
FT mutation in vitro; dbSNP:rs149078926)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066452"
FT VARIANT 759
FT /note="L -> P (found as heterozygous variant in a patient
FT with Bardet-Biedl syndrome; hypomorphic variant in vitro)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066453"
FT VARIANT 828
FT /note="V -> M (in ACLS; atypical phenotype; unknown
FT pathological significance; dbSNP:rs143915145)"
FT /evidence="ECO:0000269|PubMed:26174511"
FT /id="VAR_077693"
FT VARIANT 834
FT /note="Q -> R (rare variant found in a patient with Bardet-
FT Biedl syndrome also carrying a frameshift mutation in BBS10
FT and variant P-293 in BBS7; dbSNP:rs138354681)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066454"
FT VARIANT 958
FT /note="S -> I (in dbSNP:rs3803530)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035363"
FT VARIANT 987
FT /note="E -> K (in ACLS; atypical phenotype; unknown
FT pathological significance; dbSNP:rs146626238)"
FT /evidence="ECO:0000269|PubMed:26174511"
FT /id="VAR_077694"
FT VARIANT 994
FT /note="Q -> R (in BBS; the patient is a compound
FT heterozygote for a truncating mutation and mutation R-390
FT in BBS1; hypomorphic variant in vitro; dbSNP:rs138410949)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066455"
FT VARIANT 1005
FT /note="G -> R (in dbSNP:rs12900805)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035364"
FT VARIANT 1060
FT /note="N -> S (in AGBK; dbSNP:rs886039282)"
FT /evidence="ECO:0000269|PubMed:22587682"
FT /id="VAR_071185"
FT VARIANT 1068
FT /note="R -> W (in BBS; the patient is a compound
FT heterozygote for two frameshift mutations in BBS9;
FT hypomorphic variant in vitro; dbSNP:rs147191956)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066456"
FT VARIANT 1115
FT /note="H -> Q (in dbSNP:rs142032413)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066457"
FT VARIANT 1122
FT /note="S -> W (in ACLS; atypical phenotype; unknown
FT pathological significance; dbSNP:rs202195179)"
FT /evidence="ECO:0000269|PubMed:26174511"
FT /id="VAR_077695"
FT VARIANT 1329..1332
FT /note="Missing (in JBTS12; found in a patient with Joubert
FT syndrome that also carries mutations L-358 and T-833 in
FT TMEM67)"
FT /evidence="ECO:0000269|PubMed:21633164"
FT /id="VAR_066458"
FT CONFLICT 548
FT /note="P -> L (in Ref. 2; AAQ88750)"
FT /evidence="ECO:0000305"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4A14"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 217..228
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:4A14"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:4A14"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4A14"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:4A14"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:4A14"
SQ SEQUENCE 1343 AA; 150587 MW; 5217A6F36C156587 CRC64;
MGLEAQRLPG AEEAPVRVAL RVRPLLPKEL LHGHQSCLQV EPGLGRVTLG RDRHFGFHVV
LAEDAGQEAV YQACVQPLLE AFFEGFNATV FAYGQTGSGK TYTMGEASVA SLLEDEQGIV
PRAMAEAFKL IDENDLLDCL VHVSYLEVYK EEFRDLLEVG TASRDIQLRE DERGNVVLCG
VKEVDVEGLD EVLSLLEMGN AARHTGATHL NHLSSRSHTV FTVTLEQRGR APSRLPRPAP
GQLLVSKFHF VDLAGSERVL KTGSTGERLK ESIQINSSLL ALGNVISALG DPQRRGSHIP
YRDSKITRIL KDSLGGNAKT VMIACVSPSS SDFDETLNTL NYASRAQNIR NRATVNWRPE
AERPPEETAS GARGPPRHRS ETRIIHRGRR APGPATASAA AAMRLGAECA RYRACTDAAY
SLLRELQAEP GLPGAAARKV RDWLCAVEGE RSALSSASGP DSGIESASVE DQAAQGAGGR
KEDEGAQQLL TLQNQVARLE EENRDFLAAL EDAMEQYKLQ SDRLREQQEE MVELRLRLEL
VRPGWGGPRL LNGLPPGSFV PRPHTAPLGG AHAHVLGMVP PACLPGDEVG SEQRGEQVTN
GREAGAELLT EVNRLGSGSS AASEEEEEEE EPPRRTLHLR RNRISNCSQR AGARPGSLPE
RKGPELCLEE LDAAIPGSRA VGGSKARVQA RQVPPATASE WRLAQAQQKI RELAINIRMK
EELIGELVRT GKAAQALNRQ HSQRIRELEQ EAEQVRAELS EGQRQLRELE GKELQDAGER
SRLQEFRRRV AAAQSQVQVL KEKKQATERL VSLSAQSEKR LQELERNVQL MRQQQGQLQR
RLREETEQKR RLEAEMSKRQ HRVKELELKH EQQQKILKIK TEEIAAFQRK RRSGSNGSVV
SLEQQQKIEE QKKWLDQEME KVLQQRRALE ELGEELHKRE AILAKKEALM QEKTGLESKR
LRSSQALNED IVRVSSRLEH LEKELSEKSG QLRQGSAQSQ QQIRGEIDSL RQEKDSLLKQ
RLEIDGKLRQ GSLLSPEEER TLFQLDEAIE ALDAAIEYKN EAITCRQRVL RASASLLSQC
EMNLMAKLSY LSSSETRALL CKYFDKVVTL REEQHQQQIA FSELEMQLEE QQRLVYWLEV
ALERQRLEMD RQLTLQQKEH EQNMQLLLQQ SRDHLGEGLA DSRRQYEARI QALEKELGRY
MWINQELKQK LGGVNAVGHS RGGEKRSLCS EGRQAPGNED ELHLAPELLW LSPLTEGAPR
TREETRDLVH APLPLTWKRS SLCGEEQGSP EELRQREAAE PLVGRVLPVG EAGLPWNFGP
LSKPRRELRR ASPGMIDVRK NPL
