USH1G_HUMAN
ID USH1G_HUMAN Reviewed; 461 AA.
AC Q495M9; Q8N251;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=pre-mRNA splicing regulator USH1G {ECO:0000305};
DE AltName: Full=Scaffold protein containing ankyrin repeats and SAM domain;
DE AltName: Full=Usher syndrome type-1G protein;
GN Name=USH1G; Synonyms=SANS;
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].
RC TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH PDZD7.
RX PubMed=19028668; DOI=10.1093/hmg/ddn395;
RA Schneider E., Marker T., Daser A., Frey-Mahn G., Beyer V., Farcas R.,
RA Schneider-Ratzke B., Kohlschmidt N., Grossmann B., Bauss K., Napiontek U.,
RA Keilmann A., Bartsch O., Zechner U., Wolfrum U., Haaf T.;
RT "Homozygous disruption of PDZD7 by reciprocal translocation in a
RT consanguineous family: a new member of the Usher syndrome protein
RT interactome causing congenital hearing impairment.";
RL Hum. Mol. Genet. 18:655-666(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MYO7A;
RP USH1C AND USH1G.
RX PubMed=21709241; DOI=10.1073/pnas.1104161108;
RA Grati M., Kachar B.;
RT "Myosin VIIa and sans localization at stereocilia upper tip-link density
RT implicates these Usher syndrome proteins in mechanotransduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011).
RN [5]
RP FUNCTION, INTERACTION WITH MAGI2, PHOSPHORYLATION AT SER-422, AND
RP MUTAGENESIS OF SER-422.
RX PubMed=24608321; DOI=10.1093/hmg/ddu104;
RA Bauss K., Knapp B., Jores P., Roepman R., Kremer H., Wijk E.V., Maerker T.,
RA Wolfrum U.;
RT "Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-
RT mediated endocytosis.";
RL Hum. Mol. Genet. 23:3923-3942(2014).
RN [6]
RP INTERACTION WITH IFT20; IFT52 AND IFT57, AND CHARACTERIZATION OF VARIANT
RP USH1G PRO-48 AND VARIANT VAL-104.
RX PubMed=31637240; DOI=10.3389/fcell.2019.00216;
RA Sorusch N., Yildirim A., Knapp B., Janson J., Fleck W., Scharf C.,
RA Wolfrum U.;
RT "SANS (USH1G) Molecularly Links the Human Usher Syndrome Protein Network to
RT the Intraflagellar Transport Module by Direct Binding to IFT-B Proteins.";
RL Front. Cell Dev. Biol. 7:216-216(2019).
RN [7]
RP FUNCTION, INTERACTION WITH SF3B1; PRPF6; PRPF31; SON AND U4/U6.U5 TRI-SNRNP
RP COMPLEX, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT VAL-104.
RX PubMed=34023904; DOI=10.1093/nar/gkab386;
RA Yildirim A., Mozaffari-Jovin S., Wallisch A.K., Schaefer J., Ludwig S.E.J.,
RA Urlaub H., Luehrmann R., Wolfrum U.;
RT "SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear
RT transfer of tri-snRNP complexes.";
RL Nucleic Acids Res. 49:5845-5866(2021).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 388-461 IN COMPLEX WITH USH1C,
RP INTERACTION WITH USH1C, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
RP VARIANT USH1G VAL-458.
RX PubMed=20142502; DOI=10.1073/pnas.0911385107;
RA Yan J., Pan L., Chen X., Wu L., Zhang M.;
RT "The structure of the harmonin/sans complex reveals an unexpected
RT interaction mode of the two Usher syndrome proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4040-4045(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 295-390 IN COMPLEX WITH MYO7A,
RP STRUCTURE BY NMR OF 370-380, INTERACTION WITH MYO7A, AND MUTAGENESIS OF
RP PHE-307; PHE-317 AND TRP-374.
RX PubMed=21311020; DOI=10.1126/science.1198848;
RA Wu L., Pan L., Wei Z., Zhang M.;
RT "Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo.";
RL Science 331:757-760(2011).
RN [10]
RP VARIANT USH1G PRO-48, INTERACTION WITH USH1C, TISSUE SPECIFICITY, AND
RP POSSIBLE FUNCTION.
RX PubMed=12588794; DOI=10.1093/hmg/ddg051;
RA Weil D., El-Amraoui A., Masmoudi S., Mustapha M., Kikkawa Y., Laine S.,
RA Delmaghani S., Adato A., Nadifi S., Zina Z.B., Hamel C., Gal A., Ayadi H.,
RA Yonekawa H., Petit C.;
RT "Usher syndrome type I G (USH1G) is caused by mutations in the gene
RT encoding SANS, a protein that associates with the USH1C protein,
RT harmonin.";
RL Hum. Mol. Genet. 12:463-471(2003).
RN [11]
RP VARIANT USH1G VAL-458.
RX PubMed=16283141; DOI=10.1007/s00109-005-0719-4;
RA Kalay E., de Brouwer A.P.M., Caylan R., Nabuurs S.B., Wollnik B.,
RA Karaguzel A., Heister J.G.A.M., Erdol H., Cremers F.P.M., Cremers C.W.R.J.,
RA Brunner H.G., Kremer H.;
RT "A novel D458V mutation in the SANS PDZ binding motif causes atypical Usher
RT syndrome.";
RL J. Mol. Med. 83:1025-1032(2005).
RN [12]
RP INVOLVEMENT IN NON-SYNDROMIC SENSORINEURAL HEARING LOSS, AND VARIANT
RP VAL-104.
RX PubMed=25255398; DOI=10.1097/aud.0000000000000095;
RA Oonk A.M., van Huet R.A., Leijendeckers J.M., Oostrik J., Venselaar H.,
RA van Wijk E., Beynon A., Kunst H.P., Hoyng C.B., Kremer H., Schraders M.,
RA Pennings R.J.;
RT "Nonsyndromic hearing loss caused by USH1G mutations: widening the USH1G
RT disease spectrum.";
RL Ear Hear. 36:205-211(2015).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing by regulating the release
CC and transfer of U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-
CC snRNP) complexes from their assembly site in Cajal bodies to nuclear
CC speckles, thereby contributing to the assembly of the pre-catalytic
CC spliceosome on target pre-mRNAs (PubMed:34023904). May also participate
CC in recycling of snRNPs back to Cajal bodies during splicing
CC (PubMed:34023904). Plays a role in regulating MAGI2-mediated
CC endocytosis (PubMed:24608321). Anchoring/scaffolding protein that is a
CC part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A
CC that mediates mechanotransduction in cochlear hair cells. Required for
CC normal development and maintenance of cochlear hair cell bundles.
CC Required for normal hearing. {ECO:0000269|PubMed:21709241,
CC ECO:0000269|PubMed:24608321, ECO:0000269|PubMed:34023904}.
CC -!- SUBUNIT: Part of a complex composed of USH1C, USH1G and MYO7A
CC (PubMed:21709241, PubMed:21311020). Interacts with USH1C (via the first
CC PDZ domain) (PubMed:20142502, PubMed:12588794). Interacts with PDZD7
CC (PubMed:19028668). Interacts with CDH23 and PCDH15; these interactions
CC may recruit USH1G to the plasma membrane (By similarity). Interacts
CC with intraflagellar transport proteins IFT20, IFT52 AND IFT57
CC (PubMed:31637240). Interacts with splicing factors SF3B1, PRPF6, PRPF31
CC and SON (PubMed:34023904). Interacts with the U4/U6.U5 tri-small
CC nuclear ribonucleoprotein (tri-snRNP) complex in the presence of pre-
CC mRNAs (PubMed:34023904). Interacts (via SAM domain) with MAGI2 (via PDZ
CC 6 domain); the interaction is triggered by phosphorylation of USH1G by
CC CK2 and negatively regulates MAGI2-mediated endocytosis
CC (PubMed:24608321). {ECO:0000250|UniProtKB:Q80T11,
CC ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:19028668,
CC ECO:0000269|PubMed:20142502, ECO:0000269|PubMed:21311020,
CC ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:24608321,
CC ECO:0000269|PubMed:31637240, ECO:0000269|PubMed:34023904}.
CC -!- INTERACTION:
CC Q495M9; X5D778: ANKRD11; NbExp=3; IntAct=EBI-8601749, EBI-17183751;
CC Q495M9; Q13895: BYSL; NbExp=3; IntAct=EBI-8601749, EBI-358049;
CC Q495M9; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-8601749, EBI-8643161;
CC Q495M9; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-8601749, EBI-11530605;
CC Q495M9; Q9HC52: CBX8; NbExp=3; IntAct=EBI-8601749, EBI-712912;
CC Q495M9; Q9UER7: DAXX; NbExp=3; IntAct=EBI-8601749, EBI-77321;
CC Q495M9; P26196: DDX6; NbExp=3; IntAct=EBI-8601749, EBI-351257;
CC Q495M9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-8601749, EBI-744099;
CC Q495M9; Q96MY7: FAM161B; NbExp=4; IntAct=EBI-8601749, EBI-7225287;
CC Q495M9; P22607: FGFR3; NbExp=3; IntAct=EBI-8601749, EBI-348399;
CC Q495M9; P55040: GEM; NbExp=3; IntAct=EBI-8601749, EBI-744104;
CC Q495M9; P09067: HOXB5; NbExp=3; IntAct=EBI-8601749, EBI-3893317;
CC Q495M9; P01112: HRAS; NbExp=3; IntAct=EBI-8601749, EBI-350145;
CC Q495M9; O43464: HTRA2; NbExp=3; IntAct=EBI-8601749, EBI-517086;
CC Q495M9; P42858: HTT; NbExp=3; IntAct=EBI-8601749, EBI-466029;
CC Q495M9; Q9C086: INO80B; NbExp=3; IntAct=EBI-8601749, EBI-715611;
CC Q495M9; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-8601749, EBI-14069005;
CC Q495M9; P25791-3: LMO2; NbExp=3; IntAct=EBI-8601749, EBI-11959475;
CC Q495M9; I6L9F6: NEFL; NbExp=3; IntAct=EBI-8601749, EBI-10178578;
CC Q495M9; P54646: PRKAA2; NbExp=3; IntAct=EBI-8601749, EBI-1383852;
CC Q495M9; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-8601749, EBI-1567797;
CC Q495M9; P41219: PRPH; NbExp=3; IntAct=EBI-8601749, EBI-752074;
CC Q495M9; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-8601749, EBI-748391;
CC Q495M9; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-8601749, EBI-11955057;
CC Q495M9; Q9Y6N9: USH1C; NbExp=13; IntAct=EBI-8601749, EBI-954308;
CC Q495M9; Q495M9: USH1G; NbExp=2; IntAct=EBI-8601749, EBI-8601749;
CC Q495M9; Q9Y649; NbExp=3; IntAct=EBI-8601749, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell
CC membrane {ECO:0000250|UniProtKB:Q80T11}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q80T11}.
CC Nucleus speckle {ECO:0000269|PubMed:34023904}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:34023904}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q80T11}.
CC Photoreceptor inner segment {ECO:0000250|UniProtKB:Q80T11}.
CC Note=Detected at the tip of cochlear hair cell stereocilia. Recruited
CC to the cell membrane via interaction with CDH23 or PCDH15 (By
CC similarity). In photoreceptor cilia, detected predominantly at the
CC cilium base (By similarity). Expressed in the pericentriolar region of
CC the centrosome (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q80T11}.
CC -!- TISSUE SPECIFICITY: Expressed in vestibule of the inner ear, eye and
CC small intestine. {ECO:0000269|PubMed:12588794}.
CC -!- DISEASE: Usher syndrome 1G (USH1G) [MIM:606943]: USH is a genetically
CC heterogeneous condition characterized by the association of retinitis
CC pigmentosa with 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 USH1 is characterized by profound congenital sensorineural deafness,
CC absent vestibular function and prepubertal onset of progressive
CC retinitis pigmentosa leading to blindness.
CC {ECO:0000269|PubMed:12588794, ECO:0000269|PubMed:16283141,
CC ECO:0000269|PubMed:20142502, ECO:0000269|PubMed:31637240}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=The first cases with non-syndromic sensorineural hearing
CC loss based on mutations in USH1G. The hearing loss has an onset during
CC early childhood, is progressive, and has a downsloping audiogram
CC configuration. Ophthalmic and vestibular abnormalities are absent.
CC {ECO:0000269|PubMed:25255398}.
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DR EMBL; AK091243; BAC03619.1; -; mRNA.
DR EMBL; BC101096; AAI01097.1; -; mRNA.
DR EMBL; BC101097; AAI01098.1; -; mRNA.
DR EMBL; BC101098; AAI01099.1; -; mRNA.
DR EMBL; BC101099; AAI01100.1; -; mRNA.
DR CCDS; CCDS32725.1; -.
DR RefSeq; NP_001269418.1; NM_001282489.2.
DR RefSeq; NP_775748.2; NM_173477.4.
DR PDB; 2L7T; NMR; -; A=370-380.
DR PDB; 3K1R; X-ray; 2.30 A; B=388-461.
DR PDB; 3PVL; X-ray; 2.80 A; B=295-390.
DR PDBsum; 2L7T; -.
DR PDBsum; 3K1R; -.
DR PDBsum; 3PVL; -.
DR AlphaFoldDB; Q495M9; -.
DR SMR; Q495M9; -.
DR BioGRID; 125876; 22.
DR CORUM; Q495M9; -.
DR DIP; DIP-41617N; -.
DR ELM; Q495M9; -.
DR IntAct; Q495M9; 28.
DR MINT; Q495M9; -.
DR STRING; 9606.ENSP00000480279; -.
DR iPTMnet; Q495M9; -.
DR PhosphoSitePlus; Q495M9; -.
DR BioMuta; USH1G; -.
DR DMDM; 81175048; -.
DR MassIVE; Q495M9; -.
DR PaxDb; Q495M9; -.
DR PeptideAtlas; Q495M9; -.
DR PRIDE; Q495M9; -.
DR ProteomicsDB; 61966; -.
DR Antibodypedia; 19482; 52 antibodies from 17 providers.
DR DNASU; 124590; -.
DR Ensembl; ENST00000614341.5; ENSP00000480279.1; ENSG00000182040.9.
DR GeneID; 124590; -.
DR KEGG; hsa:124590; -.
DR MANE-Select; ENST00000614341.5; ENSP00000480279.1; NM_173477.5; NP_775748.2.
DR UCSC; uc032fra.2; human.
DR CTD; 124590; -.
DR DisGeNET; 124590; -.
DR GeneCards; USH1G; -.
DR GeneReviews; USH1G; -.
DR HGNC; HGNC:16356; USH1G.
DR HPA; ENSG00000182040; Tissue enhanced (esophagus).
DR MalaCards; USH1G; -.
DR MIM; 276900; phenotype.
DR MIM; 606943; phenotype.
DR MIM; 607696; gene.
DR neXtProt; NX_Q495M9; -.
DR OpenTargets; ENSG00000182040; -.
DR Orphanet; 231169; Usher syndrome type 1.
DR PharmGKB; PA38126; -.
DR VEuPathDB; HostDB:ENSG00000182040; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000017548; -.
DR HOGENOM; CLU_028071_0_0_1; -.
DR InParanoid; Q495M9; -.
DR OMA; HSSTCPH; -.
DR OrthoDB; 1344159at2759; -.
DR PhylomeDB; Q495M9; -.
DR TreeFam; TF324946; -.
DR PathwayCommons; Q495M9; -.
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; Q495M9; -.
DR SIGNOR; Q495M9; -.
DR BioGRID-ORCS; 124590; 96 hits in 1067 CRISPR screens.
DR EvolutionaryTrace; Q495M9; -.
DR GeneWiki; USH1G; -.
DR GenomeRNAi; 124590; -.
DR Pharos; Q495M9; Tbio.
DR PRO; PR:Q495M9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q495M9; protein.
DR Bgee; ENSG00000182040; Expressed in lower esophagus mucosa and 54 other tissues.
DR ExpressionAtlas; Q495M9; baseline and differential.
DR Genevisible; Q495M9; HS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0050957; P:equilibrioception; IMP:HGNC-UCL.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC-UCL.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
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 CDD; cd09586; SAM_USH1G; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037602; USH1G_SAM.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Deafness; Disease variant; Hearing; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Retinitis pigmentosa;
KW Usher syndrome.
FT CHAIN 1..461
FT /note="pre-mRNA splicing regulator USH1G"
FT /id="PRO_0000067077"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 64..93
FT /note="ANK 2"
FT REPEAT 97..126
FT /note="ANK 3"
FT DOMAIN 385..447
FT /note="SAM"
FT REGION 208..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 422
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:24608321"
FT VARIANT 48
FT /note="L -> P (in USH1G; reduced interaction with IFT52 and
FT IFT57; dbSNP:rs104894651)"
FT /evidence="ECO:0000269|PubMed:12588794,
FT ECO:0000269|PubMed:31637240"
FT /id="VAR_023739"
FT VARIANT 104
FT /note="M -> V (probable disease-associated variant found in
FT patients with non-syndromic sensorineural hearing loss;
FT reduced interaction with IFT52 and IFT57; failure to rescue
FT the USH1C splicing defect seen in USH1G-depleted cells;
FT dbSNP:rs149529031)"
FT /evidence="ECO:0000269|PubMed:25255398,
FT ECO:0000269|PubMed:31637240"
FT /id="VAR_072369"
FT VARIANT 458
FT /note="D -> V (in USH1G; atypical form with mild retinitis
FT pigmentosa and normal vestibular function; also found in
FT patients with autosomal recessive non-syndromic deafness;
FT strongly reduced affinity for USH1C; dbSNP:rs397517925)"
FT /evidence="ECO:0000269|PubMed:16283141,
FT ECO:0000269|PubMed:20142502"
FT /id="VAR_060468"
FT MUTAGEN 307
FT /note="F->E: Reduced affinity for MYO7A."
FT /evidence="ECO:0000269|PubMed:21311020"
FT MUTAGEN 317
FT /note="F->E: Reduced affinity for MYO7A."
FT /evidence="ECO:0000269|PubMed:21311020"
FT MUTAGEN 374
FT /note="W->Q: Strongly reduced affinity for MYO7A."
FT /evidence="ECO:0000269|PubMed:21311020"
FT MUTAGEN 422
FT /note="S->A: Abolishes interaction with MAGI2."
FT /evidence="ECO:0000269|PubMed:24608321"
FT MUTAGEN 422
FT /note="S->E: Phosphomimetic mutant; does not affect
FT interaction with MAGI2."
FT /evidence="ECO:0000269|PubMed:24608321"
FT CONFLICT 300
FT /note="D -> N (in Ref. 1; BAC03619)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="E -> G (in Ref. 1; BAC03619)"
FT /evidence="ECO:0000305"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3PVL"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3PVL"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3PVL"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2L7T"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:3K1R"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3K1R"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3K1R"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:3K1R"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:3K1R"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:3K1R"
FT HELIX 433..451
FT /evidence="ECO:0007829|PDB:3K1R"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:3K1R"
SQ SEQUENCE 461 AA; 51489 MW; B0ABB9F5711A5095 CRC64;
MNDQYHRAAR DGYLELLKEA TRKELNAPDE DGMTPTLWAA YHGNLESLRL IVSRGGDPDK
CDIWGNTPLH LAASNGHLHC LSFLVSFGAN IWCLDNDYHT PLDMAAMKGH MECVRYLDSI
AAKQSSLNPK LVGKLKDKAF REAERRIREC AKLQRRHHER MERRYRRELA ERSDTLSFSS
LTSSTLSRRL QHLALGSHLP YSQATLHGTA RGKTKMQKKL ERRKQGGEGT FKVSEDGRKS
ARSLSGLQLG SDVMFVRQGT YANPKEWGRA PLRDMFLSDE DSVSRATLAA EPAHSEVSTD
SGHDSLFTRP GLGTMVFRRN YLSSGLHGLG REDGGLDGVG APRGRLQSSP SLDDDSLGSA
NSLQDRSCGE ELPWDELDLG LDEDLEPETS PLETFLASLH MEDFAALLRQ EKIDLEALML
CSDLDLRSIS VPLGPRKKIL GAVRRRRQAM ERPPALEDTE L
