USH1C_MOUSE
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 25-MAY-2022, entry version 159.
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}.
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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; Q9ES64; -.
DR PeptideAtlas; Q9ES64; -.
DR PRIDE; 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 CTD; 10083; -.
DR MGI; MGI:1919338; Ush1c.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q9ES64; -.
DR OrthoDB; 1252899at2759; -.
DR PhylomeDB; Q9ES64; -.
DR BioGRID-ORCS; 72088; 1 hit in 72 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:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0032029; F:myosin tail binding; ISO: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 Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR030237; Harmonin.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR23116:SF36; PTHR23116:SF36; 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; 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
