ID INVS_HUMAN Reviewed; 1065 AA. AC Q9Y283; A2A2Y2; Q2NKL0; Q5W0T6; Q8IVX8; Q9BRB9; Q9Y488; Q9Y498; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Inversin; DE AltName: Full=Inversion of embryo turning homolog; DE AltName: Full=Nephrocystin-2; GN Name=INVS; Synonyms=INV, NPHP2; 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 1), AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=11935322; DOI=10.1007/s00439-001-0655-5; RA Schoen P., Tsuchiya K., Lenoir D., Mochizuki T., Guichard C., Takai S., RA Maiti A.K., Nihei H., Weil J., Yokoyama T., Bouvagnet P.; RT "Identification, genomic organization, chromosomal mapping and mutation RT analysis of the human INV gene, the ortholog of a murine gene implicated in RT left-right axis development and biliary atresia."; RL Hum. Genet. 110:157-165(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=11941489; DOI=10.1007/s00439-002-0696-4; RA Morgan D., Goodship J., Essner J.J., Vogan K.J., Turnpenny L., Yost H.J., RA Tabin C.J., Strachan T.; RT "The left-right determinant inversin has highly conserved ankyrin repeat RT and IQ domains and interacts with calmodulin."; RL Hum. Genet. 110:377-384(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lymph, and Muscle; 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 [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NPHP1, AND RP VARIANTS NPHP2 ARG-482 AND SER-493. RX PubMed=12872123; DOI=10.1038/ng1217; RA Otto E.A., Schermer B., Obara T., O'Toole J.F., Hiller K.S., Mueller A.M., RA Ruf R.G., Hoefele J., Beekmann F., Landau D., Foreman J.W., Goodship J.A., RA Strachan T., Kispert A., Wolf M.T., Gagnadoux M.F., Nivet H., Antignac C., RA Walz G., Drummond I.A., Benzing T., Hildebrandt F.; RT "Mutations in INVS encoding inversin cause nephronophthisis type 2, linking RT renal cystic disease to the function of primary cilia and left-right axis RT determination."; RL Nat. Genet. 34:413-420(2003). RN [7] RP FUNCTION, AND INTERACTION WITH DVL1; PRICKLE AND VANGL. RX PubMed=15852005; DOI=10.1038/ng1552; RA Simons M., Gloy J., Ganner A., Bullerkotte A., Bashkurov M., Kroenig C., RA Schermer B., Benzing T., Cabello O.A., Jenny A., Mlodzik M., Polok B., RA Driever W., Obara T., Walz G.; RT "Inversin, the gene product mutated in nephronophthisis type II, functions RT as a molecular switch between Wnt signaling pathways."; RL Nat. Genet. 37:537-543(2005). RN [8] RP FUNCTION, AND INTERACTION WITH NPHP3. RX PubMed=18371931; DOI=10.1016/j.ajhg.2008.02.017; RA Bergmann C., Fliegauf M., Bruechle N.O., Frank V., Olbrich H., RA Kirschner J., Schermer B., Schmedding I., Kispert A., Kraenzlin B., RA Nuernberg G., Becker C., Grimm T., Girschick G., Lynch S.A., Kelehan P., RA Senderek J., Neuhaus T.J., Stallmach T., Zentgraf H., Nuernberg P., RA Gretz N., Lo C., Lienkamp S., Schaefer T., Walz G., Benzing T., Zerres K., RA Omran H.; RT "Loss of nephrocystin-3 function can cause embryonic lethality, Meckel- RT Gruber-like syndrome, situs inversus, and renal-hepatic-pancreatic RT dysplasia."; RL Am. J. Hum. Genet. 82:959-970(2008). RN [9] RP INTERACTION WITH NPHP1 AND IQCB1. RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019; RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.; RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes RT and pathways."; RL Cell 145:513-528(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP INTERACTION WITH ANKS6; NEK8 AND NPHP3, AND HYDROXYLATION AT ASN-75. RX PubMed=23793029; DOI=10.1038/ng.2681; RA Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M., van Reeuwijk J., RA Boehlke C., Schell C., Yasunaga T., Helmstadter M., Mergen M., Filhol E., RA Boldt K., Horn N., Ueffing M., Otto E.A., Eisenberger T., Elting M.W., RA van Wijk J.A., Bockenhauer D., Sebire N.J., Rittig S., Vyberg M., Ring T., RA Pohl M., Pape L., Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C., RA Grahammer F., Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J., RA Roepman R., Saunier S., Walz G., Hildebrandt F., Bergmann C., RA Lienkamp S.S.; RT "ANKS6 is a central component of a nephronophthisis module linking NEK8 to RT INVS and NPHP3."; RL Nat. Genet. 45:951-956(2013). CC -!- FUNCTION: Required for normal renal development and establishment of CC left-right axis. Probably acts as a molecular switch between different CC Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting CC cytoplasmic disheveled (DVL1) for degradation by the ubiquitin- CC proteasome. This suggests that it is required in renal development to CC oppose the repression of terminal differentiation of tubular epithelial CC cells by Wnt signaling. Involved in the organization of apical CC junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8 CC (By similarity). Does not seem to be strictly required for ciliogenesis CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:15852005, CC ECO:0000269|PubMed:18371931}. CC -!- SUBUNIT: Binds calmodulin via its IQ domains. Interacts with APC2. CC Interacts with alpha-, beta-, and gamma-catenin. Interacts with N- CC cadherin (CDH2). Interacts with microtubules (By similarity). Interacts CC with NPHP1. Interacts with DVL1, PRICKLE (PRICKLE1 or PRICKLE2) and CC Strabismus (VANGL1 or VANGL2). Interacts with IQCB1; the interaction CC likely requires additional interactors. Component of a complex CC containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may organize CC complex assembly by linking INVS and NPHP3 to NEK8 and INVS may target CC the complex to the proximal ciliary axoneme. {ECO:0000250, CC ECO:0000269|PubMed:12872123, ECO:0000269|PubMed:15852005, CC ECO:0000269|PubMed:18371931, ECO:0000269|PubMed:21565611, CC ECO:0000269|PubMed:23793029}. CC -!- INTERACTION: CC Q9Y283; Q9BPU9: B9D2; NbExp=4; IntAct=EBI-751472, EBI-6958971; CC Q9Y283; Q9Y265: RUVBL1; NbExp=2; IntAct=EBI-751472, EBI-353675; CC Q9Y283-3; Q92876: KLK6; NbExp=3; IntAct=EBI-11944909, EBI-2432309; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus CC {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:12872123}. CC Note=Associates with several components of the cytoskeleton including CC ciliary, random and polarized microtubules. During mitosis, it is CC recruited to mitotic spindle. Frequently membrane-associated, membrane CC localization is dependent upon cell-cell contacts and is redistributed CC when cell adhesion is disrupted after incubation of the cell monolayer CC with low-calcium/EGTA medium. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y283-1; Sequence=Displayed; CC Name=2; Synonyms=S2; CC IsoId=Q9Y283-2; Sequence=VSP_014497; CC Name=3; CC IsoId=Q9Y283-3; Sequence=VSP_014495, VSP_014496; CC -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in the primary CC cilia of renal tubular cells. {ECO:0000269|PubMed:11935322, CC ECO:0000269|PubMed:12872123}. CC -!- DOMAIN: The D-box 1 (destruction box 1) mediates the interaction with CC APC2, and may act as a recognition signal for degradation via the CC ubiquitin-proteasome pathway. {ECO:0000250}. CC -!- PTM: May be ubiquitinated via its interaction with APC2. {ECO:0000250}. CC -!- PTM: Hydroxylated at Asn-75, most probably by HIF1AN. CC {ECO:0000269|PubMed:23793029}. CC -!- DISEASE: Nephronophthisis 2 (NPHP2) [MIM:602088]: An autosomal CC recessive disorder resulting in end-stage renal disease. It is CC characterized by early onset and rapid progression. Phenotypic CC manifestations include enlarged kidneys, chronic tubulo-interstitial CC nephritis, anemia, hyperkalemic metabolic acidosis. Some patients also CC display situs inversus. Pathologically, it differs from later-onset CC nephronophthisis by the absence of medullary cysts and thickened CC tubular basement membranes, and by the presence of cortical microcysts. CC {ECO:0000269|PubMed:12872123}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAD02131.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH41665.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF039217; AAD02131.2; ALT_INIT; mRNA. DR EMBL; AF084367; AAC79436.1; -; mRNA. DR EMBL; AF084382; AAC79456.1; -; Genomic_DNA. DR EMBL; AF084373; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084374; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084375; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084377; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084379; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084381; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084371; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084369; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084368; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084370; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084372; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084380; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084378; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084376; AAC79456.1; JOINED; Genomic_DNA. DR EMBL; AF084382; AAC79457.1; -; Genomic_DNA. DR EMBL; AF084368; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084369; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084370; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084371; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084372; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084373; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084374; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084375; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084376; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084377; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084378; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084379; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084380; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AF084381; AAC79457.1; JOINED; Genomic_DNA. DR EMBL; AL137072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445214; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW58926.1; -; Genomic_DNA. DR EMBL; BC006370; AAH06370.1; -; mRNA. DR EMBL; BC041665; AAH41665.1; ALT_SEQ; mRNA. DR EMBL; BC111761; AAI11762.1; -; mRNA. DR CCDS; CCDS6746.1; -. [Q9Y283-1] DR RefSeq; NP_055240.2; NM_014425.4. [Q9Y283-1] DR AlphaFoldDB; Q9Y283; -. DR SMR; Q9Y283; -. DR BioGRID; 118021; 17. DR CORUM; Q9Y283; -. DR IntAct; Q9Y283; 15. DR MINT; Q9Y283; -. DR STRING; 9606.ENSP00000262457; -. DR GlyGen; Q9Y283; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9Y283; -. DR PhosphoSitePlus; Q9Y283; -. DR BioMuta; INVS; -. DR DMDM; 68565551; -. DR EPD; Q9Y283; -. DR jPOST; Q9Y283; -. DR MassIVE; Q9Y283; -. DR MaxQB; Q9Y283; -. DR PaxDb; 9606-ENSP00000262457; -. DR PeptideAtlas; Q9Y283; -. DR ProteomicsDB; 85690; -. [Q9Y283-1] DR ProteomicsDB; 85691; -. [Q9Y283-2] DR Pumba; Q9Y283; -. DR Antibodypedia; 29080; 128 antibodies from 19 providers. DR DNASU; 27130; -. DR Ensembl; ENST00000262456.6; ENSP00000262456.2; ENSG00000119509.13. [Q9Y283-2] DR Ensembl; ENST00000262457.7; ENSP00000262457.2; ENSG00000119509.13. [Q9Y283-1] DR Ensembl; ENST00000374921.3; ENSP00000364056.3; ENSG00000119509.13. [Q9Y283-3] DR GeneID; 27130; -. DR KEGG; hsa:27130; -. DR MANE-Select; ENST00000262457.7; ENSP00000262457.2; NM_014425.5; NP_055240.2. DR UCSC; uc004bao.3; human. [Q9Y283-1] DR AGR; HGNC:17870; -. DR CTD; 27130; -. DR DisGeNET; 27130; -. DR GeneCards; INVS; -. DR GeneReviews; INVS; -. DR HGNC; HGNC:17870; INVS. DR HPA; ENSG00000119509; Low tissue specificity. DR MalaCards; INVS; -. DR MIM; 243305; gene. DR MIM; 602088; phenotype. DR neXtProt; NX_Q9Y283; -. DR OpenTargets; ENSG00000119509; -. DR Orphanet; 93591; Infantile nephronophthisis. DR Orphanet; 3156; Senior-Loken syndrome. DR PharmGKB; PA38472; -. DR VEuPathDB; HostDB:ENSG00000119509; -. DR eggNOG; KOG0504; Eukaryota. DR GeneTree; ENSGT00940000157688; -. DR HOGENOM; CLU_010082_0_0_1; -. DR InParanoid; Q9Y283; -. DR OMA; DGHWKPS; -. DR OrthoDB; 5474520at2759; -. DR PhylomeDB; Q9Y283; -. DR TreeFam; TF312824; -. DR PathwayCommons; Q9Y283; -. DR SignaLink; Q9Y283; -. DR SIGNOR; Q9Y283; -. DR BioGRID-ORCS; 27130; 13 hits in 1161 CRISPR screens. DR ChiTaRS; INVS; human. DR GeneWiki; INVS; -. DR GenomeRNAi; 27130; -. DR Pharos; Q9Y283; Tbio. DR PRO; PR:Q9Y283; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9Y283; Protein. DR Bgee; ENSG00000119509; Expressed in calcaneal tendon and 137 other cell types or tissues. DR ExpressionAtlas; Q9Y283; baseline and differential. DR GO; GO:0097543; C:ciliary inversin compartment; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:1904108; P:protein localization to ciliary inversin compartment; IBA:GO_Central. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR PANTHER; PTHR24178:SF2; INVERSIN; 1. DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1. DR Pfam; PF00023; Ank; 3. DR Pfam; PF12796; Ank_2; 4. DR Pfam; PF00612; IQ; 2. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 15. DR SMART; SM00015; IQ; 2. DR SUPFAM; SSF48403; Ankyrin repeat; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 11. DR PROSITE; PS50096; IQ; 2. DR Genevisible; Q9Y283; HS. PE 1: Evidence at protein level; KW Alternative splicing; ANK repeat; Calmodulin-binding; Cell projection; KW Ciliopathy; Cilium; Cytoplasm; Cytoskeleton; Developmental protein; KW Disease variant; Hydroxylation; Membrane; Microtubule; Nephronophthisis; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1..1065 FT /note="Inversin" FT /id="PRO_0000067016" FT REPEAT 13..42 FT /note="ANK 1" FT REPEAT 47..76 FT /note="ANK 2" FT REPEAT 80..110 FT /note="ANK 3" FT REPEAT 113..144 FT /note="ANK 4" FT REPEAT 148..177 FT /note="ANK 5" FT REPEAT 181..213 FT /note="ANK 6" FT REPEAT 220..250 FT /note="ANK 7" FT REPEAT 254..283 FT /note="ANK 8" FT REPEAT 288..317 FT /note="ANK 9" FT REPEAT 321..350 FT /note="ANK 10" FT REPEAT 356..385 FT /note="ANK 11" FT REPEAT 389..418 FT /note="ANK 12" FT REPEAT 422..451 FT /note="ANK 13" FT REPEAT 455..484 FT /note="ANK 14" FT REPEAT 488..517 FT /note="ANK 15" FT REPEAT 523..553 FT /note="ANK 16" FT DOMAIN 555..584 FT /note="IQ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 916..945 FT /note="IQ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 589..833 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 847..886 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 976..999 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 490..498 FT /note="D-box 1" FT MOTIF 909..917 FT /note="D-box 2" FT COMPBIAS 589..614 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 623..644 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..687 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 719..739 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 752..799 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..999 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 75 FT /note="3-hydroxyasparagine" FT /evidence="ECO:0000269|PubMed:23793029" FT MOD_RES 661 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 92..101 FT /note="GNYRFMKLLL -> ALRTISTGRI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014495" FT VAR_SEQ 102..1065 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014496" FT VAR_SEQ 727..896 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11941489" FT /id="VSP_014497" FT VARIANT 242 FT /note="S -> L (in dbSNP:rs2491097)" FT /id="VAR_044119" FT VARIANT 482 FT /note="P -> R (in NPHP2)" FT /evidence="ECO:0000269|PubMed:12872123" FT /id="VAR_022822" FT VARIANT 493 FT /note="L -> S (in NPHP2; impairs ability to target DVL1 for FT degradation; dbSNP:rs121964995)" FT /evidence="ECO:0000269|PubMed:12872123" FT /id="VAR_022823" FT VARIANT 888 FT /note="S -> R (in dbSNP:rs1052867)" FT /id="VAR_044120" FT CONFLICT 487 FT /note="K -> Q (in Ref. 5; AAI11762)" FT /evidence="ECO:0000305" FT CONFLICT 764 FT /note="A -> G (in Ref. 2; AAC79436/AAC79456)" FT /evidence="ECO:0000305" SQ SEQUENCE 1065 AA; 117826 MW; DACDF33C1B8573AC CRC64; MNKSENLLFA GSSLASQVHA AAVNGDKGAL QRLIVGNSAL KDKEDQFGRT PLMYCVLADR LDCADALLKA GADVNKTDHS QRTALHLAAQ KGNYRFMKLL LTRRANWMQK DLEEMTPLHL TTRHRSPKCL ALLLKFMAPG EVDTQDKNKQ TALHWSAYYN NPEHVKLLIK HDSNIGIPDV EGKIPLHWAA NHKDPSAVHT VRCILDAAPT ESLLNWQDYE GRTPLHFAVA DGNVTVVDVL TSYESCNITS YDNLFRTPLH WAALLGHAQI VHLLLERNKS GTIPSDSQGA TPLHYAAQSN FAETVKVFLK HPSVKDDSDL EGRTSFMWAA GKGSDDVLRT MLSLKSDIDI NMADKYGGTA LHAAALSGHV STVKLLLENN AQVDATDVMK HTPLFRACEM GHKDVIQTLI KGGARVDLVD QDGHSLLHWA ALGGNADVCQ ILIENKINPN VQDYAGRTPL QCAAYGGYIN CMAVLMENNA DPNIQDKEGR TALHWSCNNG YLDAIKLLLD FAAFPNQMEN NEERYTPLDY ALLGERHEVI QFMLEHGALS IAAIQDIAAF KIQAVYKGYK VRKAFRDRKN LLMKHEQLRK DAAAKKREEE NKRKEAEQQK GRRSPDSCRP QALPCLPSTQ DVPSRQSRAP SKQPPAGNVA QGPEPRDSRG SPGGSLGGAL QKEQHVSSDL QGTNSRRPNE TAREHSKGQS ACVHFRPNEG SDGSRHPGVP SVEKSRGETA GDERCAKGKG FVKQPSCIRV AGPDEKGEDS RRAAASLPPH DSHWKPSRRH DTEPKAKCAP QKRRTQELRG GRCSPAGSSR PGSARGEAVH AGQNPPHHRT PRNKVTQAKL TGGLYSHLPQ STEELRSGAR RLETSTLSED FQVSKETDPA PGPLSGQSVN IDLLPVELRL QIIQRERRRK ELFRKKNKAA AVIQRAWRSY QLRKHLSHLR HMKQLGAGDV DRWRQESTAL LLQVWRKELE LKFPQTTAVS KAPKSPSKGT SGTKSTKHSV LKQIYGCSHE GKIHHPTRSV KASSVLRLNS VSNLQCIHLL ENSGRSKNFS YNLQSATQPK NKTKP //