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Harmonin (Antigen NY-CO-38/NY-CO-37) (Autoimmune enteropathy-related antigen AIE-75) (Protein PDZ-73) (Renal carcinoma antigen NY-REN-3) (Usher syndrome type-1C protein)

 USH1C_HUMAN             Reviewed;         552 AA.
Q9Y6N9; A8K423; Q7RTU8; Q96B29; Q9UM04; Q9UM17; Q9UPC3;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
25-OCT-2017, entry version 163.
RecName: Full=Harmonin;
AltName: Full=Antigen NY-CO-38/NY-CO-37;
AltName: Full=Autoimmune enteropathy-related antigen AIE-75;
AltName: Full=Protein PDZ-73;
AltName: Full=Renal carcinoma antigen NY-REN-3;
AltName: Full=Usher syndrome type-1C protein;
Name=USH1C; Synonyms=AIE75;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND VARIANT ASP-519.
TISSUE=Colon cancer;
PubMed=9610721;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by
autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Duodenum;
PubMed=10500064; DOI=10.1016/S0016-5085(99)70340-9;
Kobayashi I., Imamura K., Kubota M., Ishikawa S., Yamada M.,
Tonoki H., Okano M., Storch W.B., Moriuchi T., Sakiyama Y.,
Kobayashi K.;
"Identification of an autoimmune enteropathy-related 75-kilodalton
antigen.";
Gastroenterology 117:823-830(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASP-519.
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
ASP-519.
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[8]
INVOLVEMENT IN USH1C, AND ALTERNATIVE SPLICING (ISOFORM 5).
PubMed=10973247; DOI=10.1038/79171;
Verpy E., Leibovici M., Zwaenepoel I., Liu X.-Z., Gal A., Salem N.,
Mansour A., Blanchard S., Kobayashi I., Keats B.J.B., Slim R.,
Petit C.;
"A defect in harmonin, a PDZ domain-containing protein expressed in
the inner ear sensory hair cells, underlies Usher syndrome type 1C.";
Nat. Genet. 26:51-55(2000).
[9]
INTERACTION WITH USHBP1, AND DOMAIN.
PubMed=11311560; DOI=10.1016/S0378-1119(01)00378-X;
Ishikawa S., Kobayashi I., Hamada J., Tada M., Hirai A., Furuuchi K.,
Takahashi Y., Ba Y., Moriuchi T.;
"Interaction of MCC2, a novel homologue of MCC tumor suppressor, with
PDZ-domain protein AIE-75.";
Gene 267:101-110(2001).
[10]
INVOLVEMENT IN DFNB18A.
PubMed=12107438; DOI=10.1007/s00439-002-0732-4;
Ahmed Z.M., Smith T.N., Riazuddin S., Makishima T., Ghosh M.,
Bokhari S., Menon P.S., Deshmukh D., Griffith A.J., Riazuddin S.,
Friedman T.B., Wilcox E.R.;
"Nonsyndromic recessive deafness DFNB18 and Usher syndrome type IC are
allelic mutations of USHIC.";
Hum. Genet. 110:527-531(2002).
[11]
INTERACTION WITH USH1G, AND TISSUE SPECIFICITY.
PubMed=12588794; DOI=10.1093/hmg/ddg051;
Weil D., El-Amraoui A., Masmoudi S., Mustapha M., Kikkawa Y.,
Laine S., Delmaghani S., Adato A., Nadifi S., Zina Z.B., Hamel C.,
Gal A., Ayadi H., Yonekawa H., Petit C.;
"Usher syndrome type I G (USH1G) is caused by mutations in the gene
encoding SANS, a protein that associates with the USH1C protein,
harmonin.";
Hum. Mol. Genet. 12:463-471(2003).
[12]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[13]
INTERACTION WITH SLC4A7 AND USH2A, AND DOMAIN.
PubMed=16301216; DOI=10.1093/hmg/ddi417;
Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K.,
te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H.,
Wolfrum U.;
"Scaffold protein harmonin (USH1C) provides molecular links between
Usher syndrome type 1 and type 2.";
Hum. Mol. Genet. 14:3933-3943(2005).
[14]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MYO7A AND
USH1G.
PubMed=21709241; DOI=10.1073/pnas.1104161108;
Grati M., Kachar B.;
"Myosin VIIa and sans localization at stereocilia upper tip-link
density implicates these Usher syndrome proteins in
mechanotransduction.";
Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011).
[15]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF THE IMAC COMPLEX,
INTERACTION WITH CDHR2; CDHR5 AND MYO7B, AND DOMAIN.
PubMed=24725409; DOI=10.1016/j.cell.2014.01.067;
Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E.,
Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A.,
Kachar B., Tyska M.J.;
"Intestinal brush border assembly driven by protocadherin-based
intermicrovillar adhesion.";
Cell 157:433-446(2014).
[16]
FUNCTION, IDENTIFICATION OF THE IMAC COMPLEX, INTERACTION WITH ANKS4B
AND MYO7B, DOMAIN, AND REGION.
PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022;
Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr.,
Tyska M.J.;
"ANKS4B is essential for intermicrovillar adhesion complex
formation.";
Dev. Cell 36:190-200(2016).
[17]
STRUCTURE BY NMR OF 197-301.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second PDZ domain of harmonin protein.";
Submitted (NOV-2005) to the PDB data bank.
[18]
STRUCTURE BY NMR OF 1-80 AND 208-299 IN COMPLEX WITH CDH23,
SUBCELLULAR LOCATION, AND INTERACTION WITH CDH23.
PubMed=19297620; DOI=10.1073/pnas.0901819106;
Pan L., Yan J., Wu L., Zhang M.;
"Assembling stable hair cell tip link complex via multidentate
interactions between harmonin and cadherin 23.";
Proc. Natl. Acad. Sci. U.S.A. 106:5575-5580(2009).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-192 IN COMPLEX WITH USH1G,
INTERACTION WITH USH1G, MUTAGENESIS OF ARG-103, DOMAIN, AND
SUBCELLULAR LOCATION.
PubMed=20142502; DOI=10.1073/pnas.0911385107;
Yan J., Pan L., Chen X., Wu L., Zhang M.;
"The structure of the harmonin/sans complex reveals an unexpected
interaction mode of the two Usher syndrome proteins.";
Proc. Natl. Acad. Sci. U.S.A. 107:4040-4045(2010).
[20]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-194 IN COMPLEX WITH
ANKS4B, INTERACTION WITH CDHR2 AND MYO7B, REGION, AND DOMAIN.
PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
Li J., He Y., Lu Q., Zhang M.;
"Mechanistic basis of organization of the Harmonin/USH1C-mediated
brush border microvilli tip-link complex.";
Dev. Cell 36:179-189(2016).
-!- FUNCTION: Anchoring/scaffolding protein that is a part of the
functional network formed by USH1C, USH1G, CDH23 and MYO7A that
mediates mechanotransduction in cochlear hair cells. Required for
normal development and maintenance of cochlear hair cell bundles
(By similarity). As part of the intermicrovillar adhesion
complex/IMAC plays a role in brush border differentiation,
controlling microvilli organization and length. Probably plays a
central regulatory role in the assembly of the complex, recruiting
CDHR2, CDHR5 and MYO7B to the microvilli tips (PubMed:24725409,
PubMed:26812018). {ECO:0000250|UniProtKB:Q9ES64,
ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:26812018}.
-!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
complex/intermicrovillar tip-link complex composed of ANKS4B,
MYO7B, USH1C, CDHR2 and CDHR5 (Probable). Part of a complex
composed of USH1C, USH1G and MYO7A (PubMed:21709241). Interacts
with F-actin (By similarity). Interacts with USH2A
(PubMed:16301216). Interacts with SLC4A7 (PubMed:16301216).
Interacts (via PDZ1 domain) with the C-terminus of USHBP1
(PubMed:11311560). Interacts (via N-terminus and PDZ 2 domain)
with CDH23 (PubMed:19297620). Interacts with USH1G
(PubMed:12588794, PubMed:20142502). Interacts with MYO7B
(PubMed:24725409, PubMed:26812017). Interacts with CDHR2 and
CDHR5; may mediate their interaction with MYO7B at the microvilli
tip (PubMed:24725409, PubMed:26812017). Interacts (via PDZ 1
domain) with ANKS4B (PubMed:26812018, PubMed:26812017).
{ECO:0000250|UniProtKB:Q9ES64, ECO:0000269|PubMed:11311560,
ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:16301216,
ECO:0000269|PubMed:19297620, ECO:0000269|PubMed:20142502,
ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:24725409,
ECO:0000269|PubMed:26812017, ECO:0000269|PubMed:26812018,
ECO:0000305|PubMed:24725409, ECO:0000305|PubMed:26812018}.
-!- INTERACTION:
Q9BYE9:CDHR2; NbExp=2; IntAct=EBI-9541226, EBI-493793;
Q9HBB8:CDHR5; NbExp=2; IntAct=EBI-9541226, EBI-9540696;
Q9UBT7:CTNNAL1; NbExp=3; IntAct=EBI-954308, EBI-514206;
Q8WXG9-1:GPR98; NbExp=3; IntAct=EBI-11523636, EBI-11621707;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-954308, EBI-2548751;
P63000:RAC1; NbExp=3; IntAct=EBI-954308, EBI-413628;
Q495M9:USH1G; NbExp=5; IntAct=EBI-954308, EBI-8601749;
O75445-1:USH2A; NbExp=3; IntAct=EBI-11523636, EBI-11621644;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20142502}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19297620, ECO:0000269|PubMed:21709241}. Cell
projection, microvillus {ECO:0000269|PubMed:24725409}.
Note=Colocalizes with F-actin (By similarity). Detected at the tip
of cochlear hair cell stereocilia (By similarity). Enriched in
microvilli of the intestinal brush border (PubMed:24725409).
{ECO:0000250|UniProtKB:Q9ES64, ECO:0000269|PubMed:24725409}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9Y6N9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6N9-2; Sequence=VSP_003789;
Name=3;
IsoId=Q9Y6N9-3; Sequence=VSP_003790;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q9Y6N9-4; Sequence=VSP_007422;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9Y6N9-5; Sequence=VSP_043520, VSP_043521;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in small intestine, colon, kidney,
eye and weakly in pancreas. Expressed also in vestibule of the
inner ear. {ECO:0000269|PubMed:12588794}.
-!- DOMAIN: The PDZ 1 domain mediates interaction with ANKS4B, USHBP1,
USH1G, SLC4A7. {ECO:0000269|PubMed:16301216,
ECO:0000269|PubMed:20142502, ECO:0000269|PubMed:24725409,
ECO:0000269|PubMed:26812017, ECO:0000269|PubMed:26812018}.
-!- DOMAIN: The N-terminal region constitutes an independently folded
domain that has structural similarity with the CCM2 C-terminus,
despite very low sequence similarity.
{ECO:0000269|PubMed:20142502}.
-!- DISEASE: Usher syndrome 1C (USH1C) [MIM:276904]: USH is a
genetically heterogeneous condition characterized by the
association of retinitis pigmentosa with sensorineural deafness.
Age at onset and differences in auditory and vestibular function
distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2
(USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by
profound congenital sensorineural deafness, absent vestibular
function and prepubertal onset of progressive retinitis pigmentosa
leading to blindness. {ECO:0000269|PubMed:10973247}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Deafness, autosomal recessive, 18A (DFNB18A)
[MIM:602092]: A form of non-syndromic sensorineural hearing loss.
Sensorineural deafness results from damage to the neural receptors
of the inner ear, the nerve pathways to the brain, or the area of
the brain that receives sound information.
{ECO:0000269|PubMed:12107438}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAC18049.1; Type=Frameshift; Positions=552; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mutations of the USH1C gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/ush1cmut.htm";
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EMBL; AF039700; AAC18049.1; ALT_FRAME; mRNA.
EMBL; AF039699; AAC18048.1; -; mRNA.
EMBL; AB006955; BAA81739.1; -; mRNA.
EMBL; AB018687; BAA81740.1; -; mRNA.
EMBL; AK290788; BAF83477.1; -; mRNA.
EMBL; AC124799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016057; AAH16057.1; -; mRNA.
EMBL; CH471064; EAW68432.1; -; Genomic_DNA.
EMBL; BK000147; DAA00086.1; -; mRNA.
CCDS; CCDS31438.1; -. [Q9Y6N9-1]
CCDS; CCDS73265.1; -. [Q9Y6N9-4]
CCDS; CCDS7825.1; -. [Q9Y6N9-5]
RefSeq; NP_001284693.1; NM_001297764.1. [Q9Y6N9-4]
RefSeq; NP_005700.2; NM_005709.3. [Q9Y6N9-1]
RefSeq; NP_710142.1; NM_153676.3. [Q9Y6N9-5]
UniGene; Hs.502072; -.
PDB; 1X5N; NMR; -; A=201-301.
PDB; 2KBQ; NMR; -; A=1-80.
PDB; 2KBR; NMR; -; A=1-80.
PDB; 2KBS; NMR; -; A=208-299.
PDB; 2LSR; NMR; -; A=1-80.
PDB; 3K1R; X-ray; 2.30 A; A=1-192.
PDB; 5F3X; X-ray; 2.65 A; A/C=1-194.
PDB; 5XBF; X-ray; 1.80 A; B=428-552.
PDBsum; 1X5N; -.
PDBsum; 2KBQ; -.
PDBsum; 2KBR; -.
PDBsum; 2KBS; -.
PDBsum; 2LSR; -.
PDBsum; 3K1R; -.
PDBsum; 5F3X; -.
PDBsum; 5XBF; -.
ProteinModelPortal; Q9Y6N9; -.
SMR; Q9Y6N9; -.
BioGrid; 115392; 21.
CORUM; Q9Y6N9; -.
DIP; DIP-41473N; -.
ELM; Q9Y6N9; -.
IntAct; Q9Y6N9; 28.
MINT; MINT-196953; -.
STRING; 9606.ENSP00000005226; -.
iPTMnet; Q9Y6N9; -.
PhosphoSitePlus; Q9Y6N9; -.
BioMuta; USH1C; -.
DMDM; 160113087; -.
PaxDb; Q9Y6N9; -.
PeptideAtlas; Q9Y6N9; -.
PRIDE; Q9Y6N9; -.
DNASU; 10083; -.
Ensembl; ENST00000005226; ENSP00000005226; ENSG00000006611. [Q9Y6N9-5]
Ensembl; ENST00000318024; ENSP00000317018; ENSG00000006611. [Q9Y6N9-1]
Ensembl; ENST00000526313; ENSP00000432236; ENSG00000006611. [Q9Y6N9-3]
Ensembl; ENST00000527020; ENSP00000436934; ENSG00000006611. [Q9Y6N9-4]
Ensembl; ENST00000527720; ENSP00000432944; ENSG00000006611. [Q9Y6N9-2]
GeneID; 10083; -.
KEGG; hsa:10083; -.
UCSC; uc001mne.4; human. [Q9Y6N9-1]
CTD; 10083; -.
DisGeNET; 10083; -.
EuPathDB; HostDB:ENSG00000006611.15; -.
GeneCards; USH1C; -.
GeneReviews; USH1C; -.
H-InvDB; HIX0009478; -.
HGNC; HGNC:12597; USH1C.
HPA; CAB013690; -.
HPA; HPA027398; -.
HPA; HPA027492; -.
HPA; HPA028033; -.
MalaCards; USH1C; -.
MIM; 276900; phenotype.
MIM; 276904; phenotype.
MIM; 602092; phenotype.
MIM; 605242; gene.
neXtProt; NX_Q9Y6N9; -.
OpenTargets; ENSG00000006611; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 231169; Usher syndrome type 1.
PharmGKB; PA37226; -.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00530000063178; -.
HOGENOM; HOG000126890; -.
HOVERGEN; HBG057181; -.
InParanoid; Q9Y6N9; -.
KO; K21877; -.
OMA; KRLAMES; -.
OrthoDB; EOG091G073L; -.
PhylomeDB; Q9Y6N9; -.
TreeFam; TF325033; -.
ChiTaRS; USH1C; human.
EvolutionaryTrace; Q9Y6N9; -.
GeneWiki; USH1C; -.
GenomeRNAi; 10083; -.
PRO; PR:Q9Y6N9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000006611; -.
CleanEx; HS_USH1C; -.
ExpressionAtlas; Q9Y6N9; baseline and differential.
Genevisible; Q9Y6N9; HS.
GO; GO:0045177; C:apical part of cell; IDA:HGNC.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0001917; C:photoreceptor inner segment; ISS:BHF-UCL.
GO; GO:0001750; C:photoreceptor outer segment; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0032420; C:stereocilium; ISS:BHF-UCL.
GO; GO:0045202; C:synapse; ISS:BHF-UCL.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0030507; F:spectrin binding; IDA:MGI.
GO; GO:0051017; P:actin filament bundle assembly; ISS:BHF-UCL.
GO; GO:0042491; P:auditory receptor cell differentiation; ISS:BHF-UCL.
GO; GO:1904970; P:brush border assembly; IMP:UniProtKB.
GO; GO:0043623; P:cellular protein complex assembly; IDA:UniProtKB.
GO; GO:0050957; P:equilibrioception; IMP:HGNC.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:HGNC.
GO; GO:0042472; P:inner ear morphogenesis; ISS:BHF-UCL.
GO; GO:0060122; P:inner ear receptor stereocilium organization; ISS:BHF-UCL.
GO; GO:0030046; P:parallel actin filament bundle assembly; ISS:BHF-UCL.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC.
GO; GO:1904106; P:protein localization to microvillus; IMP:UniProtKB.
GO; GO:0032532; P:regulation of microvillus length; ISS:UniProtKB.
GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC.
GO; GO:0007605; P:sensory perception of sound; IMP:HGNC.
InterPro; IPR030237; Harmonin.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR23116:SF36; PTHR23116:SF36; 2.
Pfam; PF00595; PDZ; 3.
SMART; SM00228; PDZ; 3.
SUPFAM; SSF50156; SSF50156; 3.
PROSITE; PS50106; PDZ; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Differentiation;
Hearing; Non-syndromic deafness; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Retinitis pigmentosa; Usher syndrome.
CHAIN 1 552 Harmonin.
/FTId=PRO_0000065727.
DOMAIN 87 169 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 211 293 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 452 537 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 1 86 N-terminal domain.
{ECO:0000269|PubMed:20142502}.
REGION 194 552 Mediates interaction with MYO7B.
{ECO:0000269|PubMed:26812017,
ECO:0000269|PubMed:26812018}.
COILED 310 377 {ECO:0000255}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES64}.
VAR_SEQ 1 31 Missing (in isoform 2).
{ECO:0000303|PubMed:10500064}.
/FTId=VSP_003789.
VAR_SEQ 274 292 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007422.
VAR_SEQ 404 552 Missing (in isoform 3).
{ECO:0000303|PubMed:9610721}.
/FTId=VSP_003790.
VAR_SEQ 404 427 YDQGVEPELEPADDLDGGTEEQGE -> SFGWFYRYDGKFP
TIRKKGKDKKKAKYGSLQDLRKNKKELEFEQKLYKEKEEML
EKEKQLKINRLAQEVSETEREDLEESEKIQYWVERLCQTRL
EQISSADNEISEMTTGPPPPPPSVSPLAPPLRRFAGGLHLH
TTDLDDIPLDMFYYPPKTPSALPVMPHPPPSNPPHKVPAPP
VLPLSGHVSASSSPWVQRTPPPIPIPPPPSVPTQDLTPTRP
LPSALEEALSNHPFRTGDTGNPVEDWEAKNHSGKPTNSPVP
EQSFPPTPKTFCPSPQPPRGPGVSTISKPVMVHQEPNFIYR
PAVKSEVLPQEMLKRMVVYQTAFR (in isoform 5).
{ECO:0000305}.
/FTId=VSP_043520.
VAR_SEQ 550 552 TFF -> ASLPSSVAESPQPVRKLLEDRAAVHRHGFLLQLE
PTDLLLKSKRGNQIHR (in isoform 5).
{ECO:0000305}.
/FTId=VSP_043521.
VARIANT 519 519 E -> D (in dbSNP:rs1064074).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9610721}.
/FTId=VAR_012320.
MUTAGEN 103 103 R->H: Strongly reduced affinity for
USH1G. {ECO:0000269|PubMed:20142502}.
CONFLICT 103 103 R -> S (in Ref. 2; BAA81739).
{ECO:0000305}.
CONFLICT 280 280 S -> N (in Ref. 1; AAC18049/AAC18048).
{ECO:0000305}.
CONFLICT 305 305 A -> T (in Ref. 2; BAA81739).
{ECO:0000305}.
HELIX 2 16 {ECO:0000244|PDB:3K1R}.
HELIX 20 36 {ECO:0000244|PDB:3K1R}.
HELIX 39 46 {ECO:0000244|PDB:3K1R}.
TURN 47 49 {ECO:0000244|PDB:3K1R}.
HELIX 53 56 {ECO:0000244|PDB:3K1R}.
HELIX 57 62 {ECO:0000244|PDB:3K1R}.
HELIX 63 65 {ECO:0000244|PDB:3K1R}.
HELIX 68 70 {ECO:0000244|PDB:3K1R}.
HELIX 71 77 {ECO:0000244|PDB:3K1R}.
STRAND 86 91 {ECO:0000244|PDB:3K1R}.
STRAND 100 105 {ECO:0000244|PDB:3K1R}.
HELIX 106 108 {ECO:0000244|PDB:3K1R}.
STRAND 110 117 {ECO:0000244|PDB:3K1R}.
HELIX 122 125 {ECO:0000244|PDB:3K1R}.
STRAND 132 137 {ECO:0000244|PDB:3K1R}.
HELIX 147 154 {ECO:0000244|PDB:3K1R}.
STRAND 156 166 {ECO:0000244|PDB:3K1R}.
STRAND 169 172 {ECO:0000244|PDB:3K1R}.
STRAND 181 184 {ECO:0000244|PDB:3K1R}.
HELIX 185 191 {ECO:0000244|PDB:3K1R}.
STRAND 208 214 {ECO:0000244|PDB:1X5N}.
STRAND 217 220 {ECO:0000244|PDB:2KBS}.
STRAND 224 228 {ECO:0000244|PDB:1X5N}.
STRAND 231 233 {ECO:0000244|PDB:1X5N}.
STRAND 235 241 {ECO:0000244|PDB:1X5N}.
TURN 246 251 {ECO:0000244|PDB:1X5N}.
STRAND 257 261 {ECO:0000244|PDB:1X5N}.
HELIX 273 280 {ECO:0000244|PDB:1X5N}.
STRAND 282 288 {ECO:0000244|PDB:1X5N}.
TURN 292 294 {ECO:0000244|PDB:1X5N}.
HELIX 295 298 {ECO:0000244|PDB:1X5N}.
SEQUENCE 552 AA; 62211 MW; 7E75CEE873C57F41 CRC64;
MDRKVAREFR HKVDFLIEND AEKDYLYDVL RMYHQTMDVA VLVGDLKLVI NEPSRLPLFD
AIRPLIPLKH QVEYDQLTPR RSRKLKEVRL DRLHPEGLGL SVRGGLEFGC GLFISHLIKG
GQADSVGLQV GDEIVRINGY SISSCTHEEV INLIRTKKTV SIKVRHIGLI PVKSSPDEPL
TWQYVDQFVS ESGGVRGSLG SPGNRENKEK KVFISLVGSR GLGCSISSGP IQKPGIFISH
VKPGSLSAEV GLEIGDQIVE VNGVDFSNLD HKEAVNVLKS SRSLTISIVA AAGRELFMTD
RERLAEARQR ELQRQELLMQ KRLAMESNKI LQEQQEMERQ RRKEIAQKAA EENERYRKEM
EQIVEEEEKF KKQWEEDWGS KEQLLLPKTI TAEVHPVPLR KPKYDQGVEP ELEPADDLDG
GTEEQGEQDF RKYEEGFDPY SMFTPEQIMG KDVRLLRIKK EGSLDLALEG GVDSPIGKVV
VSAVYERGAA ERHGGIVKGD EIMAINGKIV TDYTLAEAEA ALQKAWNQGG DWIDLVVAVC
PPKEYDDELT FF


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