WHRN_HUMAN
ID WHRN_HUMAN Reviewed; 907 AA.
AC Q9P202; A0A0C4DFT9; A5PKU1; A5PKZ9; Q5TAU9; Q5TAV0; Q5TAV1; Q5TAV2; Q96MZ9;
AC Q9H9F4; Q9UFZ3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Whirlin {ECO:0000305};
DE AltName: Full=Autosomal recessive deafness type 31 protein {ECO:0000305};
GN Name=WHRN {ECO:0000312|HGNC:HGNC:16361};
GN Synonyms=DFNB31 {ECO:0000303|PubMed:11973626}, KIAA1526;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANTS
RP THR-613 AND ALA-783.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-613
RP AND ALA-783.
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 [7]
RP INVOLVEMENT IN DFNB31.
RX PubMed=11973626; DOI=10.1038/sj.ejhg.5200780;
RA Mustapha M., Chouery E., Chardenoux S., Naboulsi M., Paronnaud J.,
RA Lemainque A., Megarbane A., Loiselet J., Weil D., Lathrop M., Petit C.;
RT "DFNB31, a recessive form of sensorineural hearing loss, maps to chromosome
RT 9q32-34.";
RL Eur. J. Hum. Genet. 10:210-212(2002).
RN [8]
RP INVOLVEMENT IN DFNB31, AND ALTERNATIVE SPLICING.
RX PubMed=12833159; DOI=10.1038/ng1208;
RA Mburu P., Mustapha M., Varela A., Weil D., El-Amraoui A., Holme R.H.,
RA Rump A., Hardisty R.E., Blanchard S., Coimbra R.S., Perfettini I.,
RA Parkinson N., Mallon A.-M., Glenister P., Rogers M.J., Paige A.J., Moir L.,
RA Clay J., Rosenthal A., Liu X.Z., Blanco G., Steel K.P., Petit C.,
RA Brown S.D.;
RT "Defects in whirlin, a PDZ domain molecule involved in stereocilia
RT elongation, cause deafness in the whirler mouse and families with DFNB31.";
RL Nat. Genet. 34:421-428(2003).
RN [9]
RP INVOLVEMENT IN DFNB31.
RX PubMed=15841483; DOI=10.1002/humu.9333;
RA Tlili A., Charfedine I., Lahmar I., Benzina Z., Mohamed B.A., Weil D.,
RA Idriss N., Drira M., Masmoudi S., Ayadi H.;
RT "Identification of a novel frameshift mutation in the DFNB31/WHRN gene in a
RT Tunisian consanguineous family with hereditary non-syndromic recessive
RT hearing loss.";
RL Hum. Mutat. 25:503-503(2005).
RN [10]
RP INTERACTION WITH USH2A AND ADGRV1.
RX PubMed=16434480; DOI=10.1093/hmg/ddi490;
RA van Wijk E., van der Zwaag B., Peters T., Zimmermann U., Te Brinke H.,
RA Kersten F.F.J., Maerker T., Aller E., Hoefsloot L.H., Cremers C.W.R.J.,
RA Cremers F.P.M., Wolfrum U., Knipper M., Roepman R., Kremer H.;
RT "The DFNB31 gene product whirlin connects to the Usher protein network in
RT the cochlea and retina by direct association with USH2A and VLGR1.";
RL Hum. Mol. Genet. 15:751-765(2006).
RN [11]
RP INVOLVEMENT IN USH2D.
RX PubMed=17171570; DOI=10.1007/s00439-006-0304-0;
RA Ebermann I., Scholl H.P.N., Charbel Issa P., Becirovic E., Lamprecht J.,
RA Jurklies B., Millan J.M., Aller E., Mitter D., Bolz H.;
RT "A novel gene for Usher syndrome type 2: mutations in the long isoform of
RT whirlin are associated with retinitis pigmentosa and sensorineural hearing
RT loss.";
RL Hum. Genet. 121:203-211(2007).
RN [12]
RP INTERACTION WITH MPP1, AND SUBCELLULAR LOCATION.
RX PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT "MPP1 links the Usher protein network and the Crumbs protein complex in the
RT retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [13]
RP INTERACTION WITH CIB2.
RX PubMed=23023331; DOI=10.1038/ng.2426;
RA Riazuddin S., Belyantseva I.A., Giese A.P., Lee K., Indzhykulian A.A.,
RA Nandamuri S.P., Yousaf R., Sinha G.P., Lee S., Terrell D., Hegde R.S.,
RA Ali R.A., Anwar S., Andrade-Elizondo P.B., Sirmaci A., Parise L.V.,
RA Basit S., Wali A., Ayub M., Ansar M., Ahmad W., Khan S.N., Akram J.,
RA Tekin M., Riazuddin S., Cook T., Buschbeck E.K., Frolenkov G.I., Leal S.M.,
RA Friedman T.B., Ahmed Z.M.;
RT "Alterations of the CIB2 calcium- and integrin-binding protein cause Usher
RT syndrome type 1J and nonsyndromic deafness DFNB48.";
RL Nat. Genet. 44:1265-1271(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, 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 [15]
RP STRUCTURE BY NMR OF 136-378 AND 815-904.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domains of human KIAA1526 protein.";
RL Submitted (DEC-2003) to the PDB data bank.
CC -!- FUNCTION: Involved in hearing and vision as member of the USH2 complex.
CC Necessary for elongation and maintenance of inner and outer hair cell
CC stereocilia in the organ of Corti in the inner ear. Involved in the
CC maintenance of the hair bundle ankle region, which connects stereocilia
CC in cochlear hair cells of the inner ear. In retina photoreceptors,
CC required for the maintenance of periciliary membrane complex that seems
CC to play a role in regulating intracellular protein transport.
CC {ECO:0000250|UniProtKB:Q80VW5}.
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts (via C-terminal
CC PDZ domain) with MYO15A; this interaction is necessary for localization
CC of WHRN to stereocilia tips (By similarity). Interacts (via C-terminal
CC PDZ domain) with MPP1/p55 (PubMed:17584769). Interacts with
CC LRRC4C/NGL1. Interacts with MYO7A. Interacts with RPGR. Interacts with
CC EPS8 (By similarity). Interacts with CASK (By similarity). Interacts
CC with CIB2 (PubMed:23023331). Component of USH2 complex, composed of
CC ADGRV1, PDZD7, USH2A and WHRN. Interacts (via PDZ domains) with PDZD7;
CC the interaction is direct. Interacts (via N-terminal PDZ domain) with
CC USH2A (via cytoplasmic region) (PubMed:16434480). Interacts with
CC ADGRV1/MASS1 (via cytoplasmic region) (PubMed:16434480).
CC {ECO:0000250|UniProtKB:Q80VW5, ECO:0000250|UniProtKB:Q810W9,
CC ECO:0000269|PubMed:16434480, ECO:0000269|PubMed:17584769,
CC ECO:0000269|PubMed:23023331}.
CC -!- INTERACTION:
CC Q9P202; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-310886, EBI-10181188;
CC Q9P202; P35226: BMI1; NbExp=3; IntAct=EBI-310886, EBI-2341576;
CC Q9P202; Q9UMD9: COL17A1; NbExp=3; IntAct=EBI-310886, EBI-2528742;
CC Q9P202; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-310886, EBI-742054;
CC Q9P202; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-310886, EBI-743105;
CC Q9P202; Q08379: GOLGA2; NbExp=3; IntAct=EBI-310886, EBI-618309;
CC Q9P202; P81274: GPSM2; NbExp=3; IntAct=EBI-310886, EBI-618655;
CC Q9P202; Q14145: KEAP1; NbExp=3; IntAct=EBI-310886, EBI-751001;
CC Q9P202; P49023-2: PXN; NbExp=3; IntAct=EBI-310886, EBI-11954250;
CC Q9P202; Q8NBT2: SPC24; NbExp=3; IntAct=EBI-310886, EBI-999900;
CC Q9P202; Q4KMQ1-2: TPRN; NbExp=7; IntAct=EBI-310886, EBI-11978969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80VW5}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:Q80VW5}. Cell
CC projection, growth cone {ECO:0000250|UniProtKB:Q80VW5}. Photoreceptor
CC inner segment {ECO:0000250|UniProtKB:Q80VW5}. Synapse
CC {ECO:0000250|UniProtKB:Q810W9}. Note=Detected at the level of
CC stereocilia in inner and outer hair cells of the cochlea and vestibule.
CC Localizes to both tip and ankle-link stereocilia regions. Colocalizes
CC with the growing ends of actin filaments. Colocalizes with MPP1 in the
CC retina, at the outer limiting membrane (OLM), outer plexifirm layer
CC (OPL), basal bodies and at the connecting cilium (CC). In
CC photoreceptors, localizes at a plasma membrane microdomain in the
CC apical inner segment that surrounds the connecting cilia called
CC periciliary membrane complex. {ECO:0000250|UniProtKB:Q80VW5,
CC ECO:0000250|UniProtKB:Q810W9, ECO:0000269|PubMed:17584769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P202-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P202-2; Sequence=VSP_012218, VSP_012219;
CC Name=3;
CC IsoId=Q9P202-3; Sequence=VSP_012216;
CC Name=4;
CC IsoId=Q9P202-4; Sequence=VSP_012217, VSP_012220;
CC -!- DISEASE: Deafness, autosomal recessive, 31 (DFNB31) [MIM:607084]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:11973626,
CC ECO:0000269|PubMed:12833159, ECO:0000269|PubMed:15841483}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Usher syndrome 2D (USH2D) [MIM:611383]: USH is a genetically
CC heterogeneous condition characterized by the association of retinitis
CC pigmentosa and sensorineural deafness. Age at onset and differences in
CC auditory and vestibular function distinguish Usher syndrome type 1
CC (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3).
CC USH2 is characterized by congenital mild hearing impairment with normal
CC vestibular responses. {ECO:0000269|PubMed:17171570}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene page;
CC URL="https://hereditaryhearingloss.org/recessive-genes";
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DR EMBL; AB040959; BAA96050.1; ALT_INIT; mRNA.
DR EMBL; AK022854; BAB14275.1; -; mRNA.
DR EMBL; AK056190; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL110228; CAB53685.2; -; mRNA.
DR EMBL; AL138895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87422.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87423.1; -; Genomic_DNA.
DR EMBL; BC142614; AAI42615.1; -; mRNA.
DR EMBL; BC142684; AAI42685.1; -; mRNA.
DR CCDS; CCDS43870.1; -. [Q9P202-3]
DR CCDS; CCDS6806.1; -. [Q9P202-1]
DR CCDS; CCDS87678.1; -. [Q9P202-4]
DR PIR; T14765; T14765.
DR RefSeq; NP_001077354.2; NM_001083885.2. [Q9P202-3]
DR RefSeq; NP_001166896.1; NM_001173425.1.
DR RefSeq; NP_001333819.1; NM_001346890.1. [Q9P202-4]
DR RefSeq; NP_056219.3; NM_015404.3. [Q9P202-1]
DR PDB; 1UEZ; NMR; -; A=137-224.
DR PDB; 1UF1; NMR; -; A=263-378.
DR PDB; 1UFX; NMR; -; A=815-904.
DR PDB; 6KZ1; X-ray; 1.69 A; A=814-907.
DR PDBsum; 1UEZ; -.
DR PDBsum; 1UF1; -.
DR PDBsum; 1UFX; -.
DR PDBsum; 6KZ1; -.
DR AlphaFoldDB; Q9P202; -.
DR BMRB; Q9P202; -.
DR SMR; Q9P202; -.
DR BioGRID; 117381; 22.
DR ComplexPortal; CPX-2821; USH2 complex.
DR CORUM; Q9P202; -.
DR IntAct; Q9P202; 16.
DR MINT; Q9P202; -.
DR STRING; 9606.ENSP00000354623; -.
DR iPTMnet; Q9P202; -.
DR PhosphoSitePlus; Q9P202; -.
DR SwissPalm; Q9P202; -.
DR BioMuta; WHRN; -.
DR DMDM; 296453079; -.
DR EPD; Q9P202; -.
DR jPOST; Q9P202; -.
DR MassIVE; Q9P202; -.
DR PaxDb; Q9P202; -.
DR PeptideAtlas; Q9P202; -.
DR PRIDE; Q9P202; -.
DR ProteomicsDB; 83692; -. [Q9P202-1]
DR ProteomicsDB; 83693; -. [Q9P202-2]
DR ProteomicsDB; 83694; -. [Q9P202-3]
DR ProteomicsDB; 83695; -. [Q9P202-4]
DR Antibodypedia; 29951; 155 antibodies from 23 providers.
DR DNASU; 25861; -.
DR Ensembl; ENST00000265134.10; ENSP00000265134.6; ENSG00000095397.16. [Q9P202-3]
DR Ensembl; ENST00000362057.4; ENSP00000354623.3; ENSG00000095397.16. [Q9P202-1]
DR Ensembl; ENST00000374057.3; ENSP00000363170.3; ENSG00000095397.16. [Q9P202-2]
DR GeneID; 25861; -.
DR KEGG; hsa:25861; -.
DR MANE-Select; ENST00000362057.4; ENSP00000354623.3; NM_015404.4; NP_056219.3.
DR UCSC; uc004biy.5; human. [Q9P202-1]
DR CTD; 25861; -.
DR DisGeNET; 25861; -.
DR GeneCards; WHRN; -.
DR GeneReviews; WHRN; -.
DR HGNC; HGNC:16361; WHRN.
DR HPA; ENSG00000095397; Tissue enhanced (adrenal).
DR MalaCards; WHRN; -.
DR MIM; 607084; phenotype.
DR MIM; 607928; gene.
DR MIM; 611383; phenotype.
DR neXtProt; NX_Q9P202; -.
DR OpenTargets; ENSG00000095397; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 231178; Usher syndrome type 2.
DR PharmGKB; PA27297; -.
DR VEuPathDB; HostDB:ENSG00000095397; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183002; -.
DR HOGENOM; CLU_069153_0_0_1; -.
DR InParanoid; Q9P202; -.
DR OMA; VANQHFI; -.
DR OrthoDB; 168224at2759; -.
DR PhylomeDB; Q9P202; -.
DR TreeFam; TF325033; -.
DR PathwayCommons; Q9P202; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q9P202; -.
DR BioGRID-ORCS; 25861; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; WHRN; human.
DR EvolutionaryTrace; Q9P202; -.
DR GeneWiki; DFNB31; -.
DR GenomeRNAi; 25861; -.
DR Pharos; Q9P202; Tbio.
DR PRO; PR:Q9P202; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9P202; protein.
DR Bgee; ENSG00000095397; Expressed in right adrenal gland cortex and 153 other tissues.
DR ExpressionAtlas; Q9P202; baseline and differential.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:1990075; C:periciliary membrane compartment; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002141; C:stereocilia ankle link; ISS:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:1990696; C:USH2 complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IBA:GO_Central.
DR GO; GO:0021694; P:cerebellar Purkinje cell layer formation; IEA:Ensembl.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; IC:ComplexPortal.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:1990227; P:paranodal junction maintenance; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IMP:HGNC-UCL.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:HGNC-UCL.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR033028; Whirlin.
DR PANTHER; PTHR23116:SF37; PTHR23116:SF37; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; Deafness;
KW Hearing; Non-syndromic deafness; Phosphoprotein; Reference proteome;
KW Repeat; Retinitis pigmentosa; Synapse; Usher syndrome.
FT CHAIN 1..907
FT /note="Whirlin"
FT /id="PRO_0000065968"
FT DOMAIN 140..223
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 279..361
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 816..899
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..383
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012216"
FT VAR_SEQ 1..351
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012217"
FT VAR_SEQ 281..345
FT /note="NLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAEGSGLKVGDQILEVNGR
FT SFLNILHDEAVRL -> SGVGKGGQPLRHRILPPNPEQQSCLEAARRGWFCPGSVFPQV
FT CTEGWCFFFAFLFDLCSVCYNTG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012218"
FT VAR_SEQ 346..907
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012219"
FT VAR_SEQ 352..389
FT /note="LILTVKDVGRLPHARTTVDETKWIASSRIRETMANSAG -> MHGSLEALLF
FT LPQVTLSLAHAHLICSNAQLEMCVFPHR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012220"
FT VARIANT 364
FT /note="H -> R (in dbSNP:rs10817610)"
FT /id="VAR_036684"
FT VARIANT 423
FT /note="R -> P (in dbSNP:rs35003670)"
FT /id="VAR_036685"
FT VARIANT 440
FT /note="A -> T (in dbSNP:rs4978584)"
FT /id="VAR_020593"
FT VARIANT 443
FT /note="A -> S (in dbSNP:rs11539662)"
FT /id="VAR_057029"
FT VARIANT 562
FT /note="P -> A (in dbSNP:rs12339210)"
FT /id="VAR_036686"
FT VARIANT 613
FT /note="M -> T (in dbSNP:rs942519)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_036687"
FT VARIANT 752
FT /note="Q -> H (in dbSNP:rs6478078)"
FT /id="VAR_036688"
FT VARIANT 783
FT /note="V -> A (in dbSNP:rs2274159)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020594"
FT VARIANT 796
FT /note="N -> K (in dbSNP:rs2274158)"
FT /id="VAR_020595"
FT VARIANT 813
FT /note="T -> M (in dbSNP:rs143728180)"
FT /id="VAR_020596"
FT CONFLICT 225
FT /note="P -> S (in Ref. 2; AK056190)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="G -> V (in Ref. 2; BAB14275)"
FT /evidence="ECO:0000305"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1UEZ"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1UEZ"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1UEZ"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1UEZ"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:1UEZ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1UEZ"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1UEZ"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1UEZ"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1UEZ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1UF1"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1UF1"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1UF1"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:1UF1"
FT STRAND 814..820
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 842..846
FT /evidence="ECO:0007829|PDB:6KZ1"
FT HELIX 851..855
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:6KZ1"
FT HELIX 877..889
FT /evidence="ECO:0007829|PDB:6KZ1"
FT STRAND 894..903
FT /evidence="ECO:0007829|PDB:6KZ1"
SQ SEQUENCE 907 AA; 96558 MW; 78ABE7A305132B89 CRC64;
MNAPLDGLSV SSSSTGSLGS AAGAGGGGGA GLRLLSANVR QLHQALTALL SEAEREQFTH
CLNAYHARRN VFDLVRTLRV LLDSPVKRRL LPMLRLVIPR SDQLLFDQYT AEGLYLPATT
PYRQPAWGGP DSAGPGEVRL VSLRRAKAHE GLGFSIRGGS EHGVGIYVSL VEPGSLAEKE
GLRVGDQILR VNDKSLARVT HAEAVKALKG SKKLVLSVYS AGRIPGGYVT NHIYTWVDPQ
GRSISPPSGL PQPHGGALRQ QEGDRRSTLH LLQGGDEKKV NLVLGDGRSL GLTIRGGAEY
GLGIYITGVD PGSEAEGSGL KVGDQILEVN GRSFLNILHD EAVRLLKSSR HLILTVKDVG
RLPHARTTVD ETKWIASSRI RETMANSAGF LGDLTTEGIN KPGFYKGPAG SQVTLSSLGN
QTRVLLEEQA RHLLNEQEHA TMAYYLDEYR GGSVSVEALV MALFKLLNTH AKFSLLSEVR
GTISPQDLER FDHLVLRREI ESMKARQPPG PGAGDTYSMV SYSDTGSSTG SHGTSTTVSS
ARNTLDLEET GEAVQGNINA LPDVSVDDVR STSQGLSSFK PLPRPPPLAQ GNDLPLGQPR
KLGREDLQPP SSMPSCSGTV FSAPQNRSPP AGTAPTPGTS SAQDLPSSPI YASVSPANPS
SKRPLDAHLA LVNQHPIGPF PRVQSPPHLK SPSAEATVAG GCLLPPSPSG HPDQTGTNQH
FVMVEVHRPD SEPDVNEVRA LPQTRTASTL SQLSDSGQTL SEDSGVDAGE AEASAPGRGR
QSVSTKSRSS KELPRNERPT DGANKPPGLL EPTSTLVRVK KSAATLGIAI EGGANTRQPL
PRIVTIQRGG SAHNCGQLKV GHVILEVNGL TLRGKEHREA ARIIAEAFKT KDRDYIDFLV
TEFNVML
