ID USH1C_MOUSE Reviewed; 910 AA. AC Q9ES64; Q91XD1; Q9CVG7; Q9ES65; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 164. DE RecName: Full=Harmonin; DE AltName: Full=PDZ domain-containing protein; DE AltName: Full=Usher syndrome type-1C protein homolog; GN Name=Ush1c; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAG12458.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND RP ALTERNATIVE SPLICING. RC TISSUE=Inner ear {ECO:0000269|PubMed:10973247}; RX PubMed=10973247; DOI=10.1038/79171; RA Verpy E., Leibovici M., Zwaenepoel I., Liu X.-Z., Gal A., Salem N., RA Mansour A., Blanchard S., Kobayashi I., Keats B.J.B., Slim R., Petit C.; RT "A defect in harmonin, a PDZ domain-containing protein expressed in the RT inner ear sensory hair cells, underlies Usher syndrome type 1C."; RL Nat. Genet. 26:51-55(2000). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Verpy E., Leibovici M., Zwaenepoel I., Blanchard S., Petit C.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon {ECO:0000269|PubMed:15489334}; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 740-852 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP INTERACTION WITH ANKS4B. 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 [6] RP INTERACTION WITH ANKS4B, AND DOMAIN. RX PubMed=15461667; DOI=10.1111/j.1365-2443.2004.00776.x; RA Johnston A.M., Naselli G., Niwa H., Brodnicki T., Harrison L.C., RA Gonez L.J.; RT "Harp (harmonin-interacting, ankyrin repeat-containing protein), a novel RT protein that interacts with harmonin in epithelial tissues."; RL Genes Cells 9:967-982(2004). RN [7] RP INTERACTION WITH SLC4A7. RX PubMed=16301216; DOI=10.1093/hmg/ddi417; RA Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K., RA te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H., Wolfrum U.; RT "Scaffold protein harmonin (USH1C) provides molecular links between Usher RT syndrome type 1 and type 2."; RL Hum. Mol. Genet. 14:3933-3943(2005). RN [8] RP INTERACTION WITH USH2A. RX PubMed=16301217; DOI=10.1093/hmg/ddi416; RA Adato A., Lefevre G., Delprat B., Michel V., Michalski N., Chardenoux S., RA Weil D., El-Amraoui A., Petit C.; RT "Usherin, the defective protein in Usher syndrome type IIA, is likely to be RT a component of interstereocilia ankle links in the inner ear sensory RT cells."; RL Hum. Mol. Genet. 14:3921-3932(2005). RN [9] RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CDH23 AND WITH F-ACTIN, AND RP SUBCELLULAR LOCATION. RX PubMed=19447093; DOI=10.1016/j.neuron.2009.04.006; RA Grillet N., Xiong W., Reynolds A., Kazmierczak P., Sato T., Lillo C., RA Dumont R.A., Hintermann E., Sczaniecka A., Schwander M., Williams D., RA Kachar B., Gillespie P.G., Muller U.; RT "Harmonin mutations cause mechanotransduction defects in cochlear hair RT cells."; RL Neuron 62:375-387(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=24725409; DOI=10.1016/j.cell.2014.01.067; RA Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E., RA Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A., RA Kachar B., Tyska M.J.; RT "Intestinal brush border assembly driven by protocadherin-based RT intermicrovillar adhesion."; RL Cell 157:433-446(2014). RN [12] RP INTERACTION WITH CDHR2 AND MYO7B. RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020; RA Li J., He Y., Lu Q., Zhang M.; RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush RT border microvilli tip-link complex."; RL Dev. Cell 36:179-189(2016). RN [13] RP FUNCTION. RX PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022; RA Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., Tyska M.J.; RT "ANKS4B is essential for intermicrovillar adhesion complex formation."; RL Dev. Cell 36:190-200(2016). RN [14] RP STRUCTURE BY NMR OF 742-849. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the third PDZ domain of mouse harmonin."; RL Submitted (MAY-2004) to the PDB data bank. CC -!- FUNCTION: Anchoring/scaffolding protein that is a part of the CC functional network formed by USH1C, USH1G, CDH23 and MYO7A that CC mediates mechanotransduction in cochlear hair cells. Required for CC normal development and maintenance of cochlear hair cell bundles CC (PubMed:19447093). As part of the intermicrovillar adhesion CC complex/IMAC plays a role in brush border differentiation, controlling CC microvilli organization and length. Probably plays a central regulatory CC role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B CC to the microvilli tips (PubMed:24725409, PubMed:26812018). CC {ECO:0000269|PubMed:19447093, ECO:0000269|PubMed:24725409, CC ECO:0000269|PubMed:26812018}. CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, CC USH1C, CDHR2 and CDHR5 (By similarity). Part of a complex composed of CC USH1C, USH1G and MYO7A (By similarity). Interacts with F-actin CC (PubMed:19447093). Interacts with USH2A (PubMed:16301217). Interacts CC with SLC4A7 (PubMed:16301216). Interacts (via PDZ1 domain) with the C- CC terminus of USHBP1 (By similarity). Interacts (via N-terminus and PDZ 2 CC domain) with CDH23 (PubMed:19447093). Interacts with USH1G (By CC similarity). Interacts with MYO7B (PubMed:26812017). Interacts with CC CDHR2 and CDHR5; may mediate their interaction with MYO7B at the CC microvilli tip (By similarity) (PubMed:26812017). Interacts (via PDZ 1 CC domain) with ANKS4B (PubMed:12588794, PubMed:15461667). Interacts (via CC PDZ 1 domain) with DOCK4 (By similarity). CC {ECO:0000250|UniProtKB:Q9Y6N9, ECO:0000269|PubMed:12588794, CC ECO:0000269|PubMed:15461667, ECO:0000269|PubMed:16301216, CC ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:19447093, CC ECO:0000269|PubMed:26812017}. CC -!- INTERACTION: CC Q9ES64; Q99PJ1: Pcdh15; NbExp=3; IntAct=EBI-7418968, EBI-6556746; CC Q9ES64-3; Q99PF4: Cdh23; NbExp=2; IntAct=EBI-7418919, EBI-7419021; CC Q9ES64-3; Q99PJ1: Pcdh15; NbExp=2; IntAct=EBI-7418919, EBI-6556746; CC Q9ES64-3; Q8BTY2: Slc4a7; NbExp=2; IntAct=EBI-7418919, EBI-11621670; CC Q9ES64-3; Q80T11: Ush1g; NbExp=3; IntAct=EBI-7418919, EBI-7418889; CC Q9ES64-3; Q8WXG9-1: ADGRV1; Xeno; NbExp=2; IntAct=EBI-7418919, EBI-11621707; CC Q9ES64-3; O75445-1: USH2A; Xeno; NbExp=2; IntAct=EBI-7418919, EBI-11621644; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9Y6N9}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:19447093}. Cell projection, microvillus CC {ECO:0000269|PubMed:24725409}. Note=Colocalizes with F-actin CC (PubMed:19447093). Detected at the tip of cochlear hair cell CC stereocilia (PubMed:19447093). Enriched in microvilli of the intestinal CC brush border (PubMed:24725409). {ECO:0000269|PubMed:19447093, CC ECO:0000269|PubMed:24725409}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms exist. {ECO:0000269|PubMed:10973247}; CC Name=3 {ECO:0000305}; Synonyms=b3 {ECO:0000269|PubMed:10973247}; CC IsoId=Q9ES64-1; Sequence=Displayed; CC Name=2 {ECO:0000305}; Synonyms=b2 {ECO:0000305}; CC IsoId=Q9ES64-2; Sequence=VSP_050532, VSP_050534; CC Name=1 {ECO:0000305}; Synonyms=a1 {ECO:0000269|PubMed:10973247}; CC IsoId=Q9ES64-3; Sequence=VSP_050530, VSP_050531, VSP_050533; CC -!- TISSUE SPECIFICITY: Detected in stereocilia of cochlear hair cells (at CC protein level). Isoform 1 is expressed in the eye, cochlea, vestibule, CC heart, kidney, small intestine and testis; it is barely visible in CC skeletal muscle, liver, and lung and is absent from the brain. Isoforms CC 2 and 3 are expressed in the cochlea and vestibule. CC {ECO:0000269|PubMed:10973247, ECO:0000269|PubMed:19447093, CC ECO:0000269|PubMed:24725409}. CC -!- DOMAIN: The PDZ 1 domain mediates interaction with ANKS4B, USHBP1, CC USH1G, SLC4A7. {ECO:0000250|UniProtKB:Q9Y6N9, CC ECO:0000269|PubMed:15461667}. CC -!- DOMAIN: The N-terminal region constitutes an independently folded CC domain that has structural similarity with the CCM2 C-terminus, despite CC very low sequence similarity. {ECO:0000250|UniProtKB:Q9Y6N9}. CC -!- DISRUPTION PHENOTYPE: Mice lacking Ush1c display abnormal brush border CC morphology along the length of the intestinal tract. CC {ECO:0000269|PubMed:24725409}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF228925; AAG12458.1; -; mRNA. DR EMBL; AF228924; AAG12457.1; -; mRNA. DR EMBL; AY103465; AAM44072.1; -; mRNA. DR EMBL; BC010819; AAH10819.1; -; mRNA. DR EMBL; AK008274; BAB25568.2; -; mRNA. DR CCDS; CCDS21276.1; -. [Q9ES64-1] DR CCDS; CCDS85309.1; -. [Q9ES64-2] DR RefSeq; NP_001157205.1; NM_001163733.1. DR RefSeq; NP_076138.2; NM_023649.2. DR RefSeq; NP_710143.2; NM_153677.2. DR PDB; 1V6B; NMR; -; A=742-849. DR PDBsum; 1V6B; -. DR AlphaFoldDB; Q9ES64; -. DR BMRB; Q9ES64; -. DR SMR; Q9ES64; -. DR BioGRID; 215143; 5. DR CORUM; Q9ES64; -. DR IntAct; Q9ES64; 6. DR MINT; Q9ES64; -. DR STRING; 10090.ENSMUSP00000009667; -. DR iPTMnet; Q9ES64; -. DR PhosphoSitePlus; Q9ES64; -. DR jPOST; Q9ES64; -. DR MaxQB; Q9ES64; -. DR PaxDb; 10090-ENSMUSP00000009667; -. DR PeptideAtlas; Q9ES64; -. DR ProteomicsDB; 299648; -. [Q9ES64-1] DR ProteomicsDB; 299649; -. [Q9ES64-2] DR ProteomicsDB; 299650; -. [Q9ES64-3] DR DNASU; 72088; -. DR GeneID; 72088; -. DR KEGG; mmu:72088; -. DR UCSC; uc009gyh.2; mouse. [Q9ES64-3] DR AGR; MGI:1919338; -. DR CTD; 10083; -. DR MGI; MGI:1919338; Ush1c. DR eggNOG; KOG3528; Eukaryota. DR InParanoid; Q9ES64; -. DR OrthoDB; 2913575at2759; -. DR PhylomeDB; Q9ES64; -. DR BioGRID-ORCS; 72088; 1 hit in 77 CRISPR screens. DR EvolutionaryTrace; Q9ES64; -. DR PRO; PR:Q9ES64; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9ES64; Protein. DR GO; GO:0045177; C:apical part of cell; ISO:MGI. DR GO; GO:0005903; C:brush border; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005902; C:microvillus; IDA:UniProtKB. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0002142; C:stereocilia ankle link complex; IBA:GO_Central. DR GO; GO:0032420; C:stereocilium; IDA:MGI. DR GO; GO:0032426; C:stereocilium tip; IBA:GO_Central. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:1990435; C:upper tip-link density; IDA:MGI. DR GO; GO:0030507; F:spectrin binding; ISO:MGI. DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI. DR GO; GO:1904970; P:brush border assembly; IMP:UniProtKB. DR GO; GO:0050957; P:equilibrioception; ISO:MGI. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI. DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0030046; P:parallel actin filament bundle assembly; IDA:MGI. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI. DR GO; GO:1904106; P:protein localization to microvillus; IMP:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI. DR GO; GO:0032532; P:regulation of microvillus length; IMP:UniProtKB. DR GO; GO:0046549; P:retinal cone cell development; IBA:GO_Central. DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR CDD; cd07353; harmonin_N; 1. DR CDD; cd00992; PDZ_signaling; 3. DR Gene3D; 1.20.1160.20; -; 1. DR Gene3D; 2.30.42.10; -; 3. DR InterPro; IPR030237; Harmonin_N. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR23116:SF36; HARMONIN; 1. DR PANTHER; PTHR23116; PDZ DOMAIN CONTAINING WHIRLIN AND HARMONIN-RELATED; 1. DR Pfam; PF00595; PDZ; 3. DR Pfam; PF21219; USH1C_N; 1. DR SMART; SM00228; PDZ; 3. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR PROSITE; PS50106; PDZ; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Coiled coil; KW Cytoplasm; Cytoskeleton; Differentiation; Hearing; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..910 FT /note="Harmonin" FT /id="PRO_0000065728" FT DOMAIN 87..171 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143, FT ECO:0000305" FT DOMAIN 211..295 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143, FT ECO:0000305" FT DOMAIN 752..839 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143, FT ECO:0000305" FT REGION 1..86 FT /note="N-terminal domain" FT /evidence="ECO:0000250|UniProtKB:Q9Y6N9" FT REGION 194..833 FT /note="Mediates interaction with MYO7B" FT /evidence="ECO:0000250|UniProtKB:Q9Y6N9" FT REGION 563..688 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 890..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 299..377 FT /evidence="ECO:0000255" FT COILED 417..482 FT /evidence="ECO:0000255" FT COMPBIAS 563..580 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..616 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 651..666 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 670..684 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 404..423 FT /note="SFGWFYRYDGKFPTIRKKAK -> YDQGVEPADHLDGSTEEQRQ (in FT isoform 1)" FT /evidence="ECO:0000303|PubMed:10973247, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072" FT /id="VSP_050530" FT VAR_SEQ 424..727 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:10973247, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072" FT /id="VSP_050531" FT VAR_SEQ 850..859 FT /note="SSLPSSAAES -> RKPPAGPKAA (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_050532" FT VAR_SEQ 850..852 FT /note="SSL -> TFF (in isoform 1)" FT /evidence="ECO:0000303|PubMed:10973247, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072" FT /id="VSP_050533" FT VAR_SEQ 860..910 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_050534" FT CONFLICT 375 FT /note="E -> K (in Ref. 3; AAH10819)" FT /evidence="ECO:0000305" FT CONFLICT 740 FT /note="Y -> H (in Ref. 4; BAB25568)" FT /evidence="ECO:0000305" FT HELIX 745..748 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 753..760 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 767..771 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 774..776 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 778..783 FT /evidence="ECO:0007829|PDB:1V6B" FT HELIX 789..793 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 801..807 FT /evidence="ECO:0007829|PDB:1V6B" FT HELIX 815..828 FT /evidence="ECO:0007829|PDB:1V6B" FT STRAND 831..838 FT /evidence="ECO:0007829|PDB:1V6B" SQ SEQUENCE 910 AA; 102285 MW; 427B97953BA5D941 CRC64; MDRKVAREFR HKVDFLIEND AEKDYLYDVL RMYHQTMDVA VLVGDLKLVI NEPNRLPLFD AIRPLIPLKH QVEYDQLTPR RSRKLKEVRL DRLHPEGLGL SVRGGLEFGC GLFISHLIKG GQADSVGLQV GDEIVRINGY SISSCTHEEV INLIRTKKTV SIKVRHIGLI PVKSSPEESL KWQYVDQFVS ESGGVRGGLG SPGNRTTKEK KVFISLVGSR GLGCSISSGP IQKPGIFVSH VKPGSLSAEV GLETGDQIVE VNGIDFTNLD HKEAVNVLKS SRSLTISIVA GAGRELFMTD RERLEEARQR ELQRQELLMQ KRLAMESNKI LQEQQEMERQ RRKEIAQKAA EENERYRKEM EQISEEEEKF KKQWEEDWGS KEQLILPKTI TAEVHPVPLR KPKSFGWFYR YDGKFPTIRK KAKEKKKAKY DSLQDLRKNK KELEFEQKLY KEKEEMLEKE KQLKINRLAQ EVSETEREDL EESEKTQYWV ERLCQTRLEQ ISSAENEIPE MTTGPPPPPP SVSPLAPPLR RFAGGIHLHT TDLDDIPLDM FYYPPKTPSA LPVMPHPPSV NSPSKVPAPP VLPSSGHVSS SSSPWVQRTP PPIPIPPPPS IPTQDLTPTR PLPSALEEAL GNHPFRTGDP GHPADDWEAN THSGKPSSSP TTERSFPPAP KTFCPSPQPP RGPGVSTISK PVMVHQEHNF VYRPAVKSEV LPQEMLKRMV VYQTAFRQDF RKYEEGFDPY SMFSPEQIAG KDVRLLRIKK EGSLDLALEG GVDSPVGKVV VSAVYEGGAA ERHGGVVKGD EIMAINGKIV TDYTLAEAEA ALQKAWNQGG DWIDLVVAVC PPKEYDDELS SLPSSAAESP QLARKQLEAY EPVCRHGFFL QLEPTNLLLK SRERNQTDPS WRPASSAPSP //