CIB2_HUMAN
ID CIB2_HUMAN Reviewed; 187 AA.
AC O75838; B4DDF0; H0YM71; Q05BT6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Calcium and integrin-binding family member 2;
DE AltName: Full=Kinase-interacting protein 2;
DE Short=KIP 2;
GN Name=CIB2; Synonyms=KIP2;
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).
RC TISSUE=Fetal brain;
RX PubMed=9931475; DOI=10.1016/s0167-4781(98)00253-x;
RA Seki N., Hattori A., Hayashi A., Kozuma S., Ohira M., Hori T., Saito T.;
RT "Structure, expression profile and chromosomal location of an isolog of
RT DNA-PKcs interacting protein (KIP) gene.";
RL Biochim. Biophys. Acta 1444:143-147(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Skin;
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 INTERACTION WITH ITGA2B AND ITGA7, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
RX PubMed=22779914; DOI=10.1139/o2012-021;
RA Huang H., Bogstie J.N., Vogel H.J.;
RT "Biophysical and structural studies of the human calcium- and integrin-
RT binding protein family: understanding their functional similarities and
RT differences.";
RL Biochem. Cell Biol. 90:646-656(2012).
RN [7]
RP VARIANTS DFNB48 SER-91; TRP-99 AND THR-123, VARIANT USH1J ASP-64, FUNCTION,
RP SUBUNIT, INTERACTION WITH WHRN AND MYO7A, AND TISSUE SPECIFICITY.
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 [8]
RP VARIANT MET-75.
RX PubMed=26416264; DOI=10.1002/ajmg.a.37274;
RA Booth K.T., Azaiez H., Kahrizi K., Simpson A.C., Tollefson W.T.,
RA Sloan C.M., Meyer N.C., Babanejad M., Ardalani F., Arzhangi S.,
RA Schnieders M.J., Najmabadi H., Smith R.J.;
RT "PDZD7 and hearing loss: More than just a modifier.";
RL Am. J. Med. Genet. A 167A:2957-2965(2015).
RN [9]
RP VARIANT DFNB48 TRP-186, CHARACTERIZATION OF VARIANTS DFNB48 SER-91 AND
RP TRP-186, INTERACTION WITH WHRN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26426422; DOI=10.1371/journal.pone.0133082;
RA Patel K., Giese A.P., Grossheim J.M., Hegde R.S., Hegde R.S., Delio M.,
RA Samanich J., Riazuddin S., Frolenkov G.I., Cai J., Ahmed Z.M., Morrow B.E.;
RT "A novel c-terminal CIB2 (calcium and integrin binding protein 2) mutation
RT associated with non-syndromic hearing loss in a hispanic family.";
RL PLoS ONE 10:E0133082-E0133082(2015).
RN [10]
RP VARIANTS DFNB48 TRP-66 AND SER-91, CHARACTERIZATION OF VARIANTS DFNB48
RP TRP-66 AND SER-91, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26173970; DOI=10.1038/ejhg.2015.157;
RA Seco C.Z., Giese A.P., Shafique S., Schraders M., Oonk A.M., Grossheim M.,
RA Oostrik J., Strom T., Hegde R., van Wijk E., Frolenkov G.I., Azam M.,
RA Yntema H.G., Free R.H., Riazuddin S., Verheij J.B., Admiraal R.J.,
RA Qamar R., Ahmed Z.M., Kremer H.;
RT "Novel and recurrent CIB2 variants, associated with nonsyndromic deafness,
RT do not affect calcium buffering and localization in hair cells.";
RL Eur. J. Hum. Genet. 24:542-549(2016).
CC -!- FUNCTION: Calcium-binding protein critical for proper photoreceptor
CC cell maintenance and function. Plays a role in intracellular calcium
CC homeostasis by decreasing ATP-induced calcium release (PubMed:23023331,
CC PubMed:26173970, PubMed:26426422). May be involved in the
CC mechanotransduction process (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:23023331, ECO:0000269|PubMed:26173970,
CC ECO:0000269|PubMed:26426422}.
CC -!- SUBUNIT: Homodimer (PubMed:23023331). Interacts with WHRN and MYO7A
CC (PubMed:23023331, PubMed:26426422). Interacts with ITGA2B (via C-
CC terminus cytoplasmic tail region) and ITGA7 (via C-terminus cytoplasmic
CC tail region); the interactions are stabilized/increased in a calcium
CC and magnesium-dependent manner (PubMed:22779914).
CC {ECO:0000269|PubMed:22779914, ECO:0000269|PubMed:23023331,
CC ECO:0000269|PubMed:26426422}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}. Cell
CC projection, stereocilium {ECO:0000269|PubMed:26173970,
CC ECO:0000269|PubMed:26426422}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q9Z309}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9Z309}. Note=Colocalized with ITGA7 at the
CC myotendinous junctions (MTJ) and at the neuromuscular junctions (NMJ)
CC (By similarity). Localizes in the cuticular plate along and at the tip
CC of the stereocilia of vestibular sensory hair cells (PubMed:26173970,
CC PubMed:26426422). {ECO:0000250|UniProtKB:Q9Z309,
CC ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75838-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75838-2; Sequence=VSP_053864;
CC Name=3;
CC IsoId=O75838-3; Sequence=VSP_053863;
CC Name=4;
CC IsoId=O75838-4; Sequence=VSP_054777;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:23023331).
CC {ECO:0000269|PubMed:23023331}.
CC -!- DISEASE: Deafness, autosomal recessive, 48 (DFNB48) [MIM:609439]: 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. DFNB48 patients have prelingual onset of severe to
CC profound sensorineural hearing loss affecting all frequencies.
CC {ECO:0000269|PubMed:23023331, ECO:0000269|PubMed:26173970,
CC ECO:0000269|PubMed:26426422}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Usher syndrome 1J (USH1J) [MIM:614869]: 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:23023331}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The binding of either calcium or magnesium significantly
CC increases the structural stability of the protein in comparison to apo-
CC CIB (calcium- and magnesium-free form) (PubMed:22779914).
CC {ECO:0000269|PubMed:22779914}.
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DR EMBL; AB012955; BAA33584.1; -; mRNA.
DR EMBL; AK293167; BAG56711.1; -; mRNA.
DR EMBL; AC090260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99183.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99184.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99186.1; -; Genomic_DNA.
DR EMBL; BC033108; AAH33108.1; -; mRNA.
DR EMBL; BC047381; AAH47381.1; -; mRNA.
DR CCDS; CCDS10296.1; -. [O75838-1]
DR CCDS; CCDS61722.1; -. [O75838-3]
DR CCDS; CCDS61723.1; -. [O75838-4]
DR RefSeq; NP_001258817.1; NM_001271888.1. [O75838-3]
DR RefSeq; NP_001258818.1; NM_001271889.1. [O75838-4]
DR RefSeq; NP_001288153.1; NM_001301224.1.
DR RefSeq; NP_006374.1; NM_006383.3. [O75838-1]
DR RefSeq; XP_005254183.1; XM_005254126.3. [O75838-2]
DR RefSeq; XP_006720437.1; XM_006720374.2. [O75838-3]
DR AlphaFoldDB; O75838; -.
DR SMR; O75838; -.
DR BioGRID; 115773; 99.
DR IntAct; O75838; 1.
DR STRING; 9606.ENSP00000258930; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR TCDB; 8.A.82.1.10; the calmodulin calcium binding protein (calmodulin) family.
DR iPTMnet; O75838; -.
DR PhosphoSitePlus; O75838; -.
DR BioMuta; CIB2; -.
DR jPOST; O75838; -.
DR MassIVE; O75838; -.
DR PaxDb; O75838; -.
DR PeptideAtlas; O75838; -.
DR PRIDE; O75838; -.
DR Antibodypedia; 14987; 206 antibodies from 28 providers.
DR DNASU; 10518; -.
DR Ensembl; ENST00000258930.8; ENSP00000258930.3; ENSG00000136425.14. [O75838-1]
DR Ensembl; ENST00000539011.5; ENSP00000442459.1; ENSG00000136425.14. [O75838-3]
DR Ensembl; ENST00000557846.5; ENSP00000453488.1; ENSG00000136425.14. [O75838-4]
DR GeneID; 10518; -.
DR KEGG; hsa:10518; -.
DR MANE-Select; ENST00000258930.8; ENSP00000258930.3; NM_006383.4; NP_006374.1.
DR UCSC; uc002bdb.3; human. [O75838-1]
DR CTD; 10518; -.
DR DisGeNET; 10518; -.
DR GeneCards; CIB2; -.
DR GeneReviews; CIB2; -.
DR HGNC; HGNC:24579; CIB2.
DR HPA; ENSG00000136425; Tissue enhanced (lymphoid).
DR MalaCards; CIB2; -.
DR MIM; 605564; gene.
DR MIM; 609439; phenotype.
DR MIM; 614869; phenotype.
DR neXtProt; NX_O75838; -.
DR OpenTargets; ENSG00000136425; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 231169; Usher syndrome type 1.
DR PharmGKB; PA134927274; -.
DR VEuPathDB; HostDB:ENSG00000136425; -.
DR eggNOG; KOG0038; Eukaryota.
DR GeneTree; ENSGT00940000157327; -.
DR HOGENOM; CLU_061288_6_0_1; -.
DR InParanoid; O75838; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; O75838; -.
DR TreeFam; TF313865; -.
DR PathwayCommons; O75838; -.
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; O75838; -.
DR BioGRID-ORCS; 10518; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; CIB2; human.
DR GenomeRNAi; 10518; -.
DR Pharos; O75838; Tbio.
DR PRO; PR:O75838; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75838; protein.
DR Bgee; ENSG00000136425; Expressed in right atrium auricular region and 190 other tissues.
DR ExpressionAtlas; O75838; baseline and differential.
DR Genevisible; O75838; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0032437; C:cuticular plate; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005927; C:muscle tendon junction; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Cilium;
KW Cytoplasm; Deafness; Disease variant; Magnesium; Membrane; Metal-binding;
KW Non-syndromic deafness; Reference proteome; Repeat; Retinitis pigmentosa;
KW Usher syndrome.
FT CHAIN 1..187
FT /note="Calcium and integrin-binding family member 2"
FT /id="PRO_0000073534"
FT DOMAIN 66..101
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 103..138
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053863"
FT VAR_SEQ 18..66
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054777"
FT VAR_SEQ 181..187
FT /note="STFHIRI -> RCCHYRGRAWAGQSRAGRDVGAEAPITRYL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053864"
FT VARIANT 64
FT /note="E -> D (in USH1J; dbSNP:rs145415848)"
FT /evidence="ECO:0000269|PubMed:23023331"
FT /id="VAR_069086"
FT VARIANT 66
FT /note="R -> W (in DFNB48; unknown pathological
FT significance; no loss on localization to stereocilia; does
FT not affect ATP-induced calcium release; dbSNP:rs780168150)"
FT /evidence="ECO:0000269|PubMed:26173970"
FT /id="VAR_074552"
FT VARIANT 75
FT /note="V -> M (found in a family with deafness carrying a
FT likely pathogenic mutation in PDZD7; unknown pathological
FT significance; dbSNP:rs758743502)"
FT /evidence="ECO:0000269|PubMed:26416264"
FT /id="VAR_080825"
FT VARIANT 91
FT /note="F -> S (in DFNB48; no loss on localization to
FT stereocilia; does not affect ATP-induced calcium release;;
FT dbSNP:rs397515411)"
FT /evidence="ECO:0000269|PubMed:23023331,
FT ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422"
FT /id="VAR_069087"
FT VARIANT 99
FT /note="C -> W (in DFNB48; inhibits the ability to decrease
FT ATP-induced calcium release; dbSNP:rs370965183)"
FT /evidence="ECO:0000269|PubMed:23023331"
FT /id="VAR_069088"
FT VARIANT 123
FT /note="I -> T (in DFNB48; stimulates the ability to
FT decrease ATP-induced calcium release; dbSNP:rs397515412)"
FT /evidence="ECO:0000269|PubMed:23023331"
FT /id="VAR_069089"
FT VARIANT 186
FT /note="R -> W (in DFNB48; does not affect the localization
FT in the cuticular plate or to the tip of stereocilia;
FT inhibits the ability to decrease ATP-induced calcium
FT release; does not affect binding with WHRN;
FT dbSNP:rs370359511)"
FT /evidence="ECO:0000269|PubMed:26426422"
FT /id="VAR_077559"
SQ SEQUENCE 187 AA; 21644 MW; D51F6C25AD381BEF CRC64;
MGNKQTIFTE EQLDNYQDCT FFNKKDILKL HSRFYELAPN LVPMDYRKSP IVHVPMSLII
QMPELRENPF KERIVAAFSE DGEGNLTFND FVDMFSVLCE SAPRELKANY AFKIYDFNTD
NFICKEDLEL TLARLTKSEL DEEEVVLVCD KVIEEADLDG DGKLGFADFE DMIAKAPDFL
STFHIRI
