USH2A_MOUSE
ID USH2A_MOUSE Reviewed; 5193 AA.
AC Q2QI47; E9QLJ9; Q9JLP3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Usherin;
DE AltName: Full=Usher syndrome type IIa protein homolog;
DE AltName: Full=Usher syndrome type-2A protein homolog;
DE Flags: Precursor;
GN Name=Ush2A; Synonyms=Gm676;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12160733; DOI=10.1006/geno.2002.6823;
RA Huang D., Eudy J.D., Uzvolgyi E., Davis J.R., Talmadge C.B., Pretto D.,
RA Weston M.D., Lehman J.E., Zhou M., Seemayer T.A., Ahmad I.,
RA Kimberling W.J., Sumegi J.;
RT "Identification of the mouse and rat orthologs of the gene mutated in Usher
RT syndrome type IIA and the cellular source of USH2A mRNA in retina, a target
RT tissue of the disease.";
RL Genomics 80:195-203(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu X., Bulgakov O.V., Li T.;
RT "Biochemical and genetic analyses of murine usherin (Ush2A).";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11788194; DOI=10.1016/s0378-5955(01)00344-6;
RA Bhattacharya G., Miller C., Kimberling W.J., Jablonski M.M., Cosgrove D.;
RT "Localization and expression of usherin: a novel basement membrane protein
RT defective in people with Usher's syndrome type IIa.";
RL Hear. Res. 163:1-11(2002).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORM 3), INTERACTION WITH USH1C AND WHRN, AND
RP SUBCELLULAR LOCATION.
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 [6]
RP TISSUE SPECIFICITY.
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 [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH VEZT AND
RP MYO7A.
RX PubMed=17567809; DOI=10.1523/jneurosci.0342-07.2007;
RA Michalski N., Michel V., Bahloul A., Lefevre G., Barral J., Yagi H.,
RA Chardenoux S., Weil D., Martin P., Hardelin J.P., Sato M., Petit C.;
RT "Molecular characterization of the ankle-link complex in cochlear hair
RT cells and its role in the hair bundle functioning.";
RL J. Neurosci. 27:6478-6488(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION IN
RP THE USH2 COMPLEX.
RX PubMed=20502675; DOI=10.1371/journal.pgen.1000955;
RA Yang J., Liu X., Zhao Y., Adamian M., Pawlyk B., Sun X., McMillan D.R.,
RA Liberman M.C., Li T.;
RT "Ablation of whirlin long isoform disrupts the USH2 protein complex and
RT causes vision and hearing loss.";
RL PLoS Genet. 6:E1000955-E1000955(2010).
RN [9]
RP INTERACTION WITH PDZD7 AND WHRN.
RX PubMed=23055499; DOI=10.1523/jneurosci.3071-12.2012;
RA Grati M., Shin J.B., Weston M.D., Green J., Bhat M.A., Gillespie P.G.,
RA Kachar B.;
RT "Localization of PDZD7 to the stereocilia ankle-link associates this
RT scaffolding protein with the Usher syndrome protein network.";
RL J. Neurosci. 32:14288-14293(2012).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=24334608; DOI=10.1093/hmg/ddt629;
RA Zou J., Zheng T., Ren C., Askew C., Liu X.P., Pan B., Holt J.R., Wang Y.,
RA Yang J.;
RT "Deletion of PDZD7 disrupts the Usher syndrome type 2 protein complex in
RT cochlear hair cells and causes hearing loss in mice.";
RL Hum. Mol. Genet. 23:2374-2390(2014).
RN [11]
RP IDENTIFICATION IN THE USH2 COMPLEX.
RX PubMed=25406310; DOI=10.1074/jbc.m114.610535;
RA Chen Q., Zou J., Shen Z., Zhang W., Yang J.;
RT "Whirlin and PDZ domain-containing 7 (PDZD7) proteins are both required to
RT form the quaternary protein complex associated with Usher syndrome type
RT 2.";
RL J. Biol. Chem. 289:36070-36088(2014).
CC -!- FUNCTION: Involved in hearing and vision as member of the USH2 complex
CC (PubMed:20502675). In the inner ear, required for the maintenance of
CC hair bundle ankle formation, which connects growing stereocilia in
CC developing cochlear hair cells (PubMed:20502675, PubMed:24334608). In
CC retina photoreceptors, the USH2 complex is required for the maintenance
CC of periciliary membrane complex that seems to play a role in regulating
CC intracellular protein transport (PubMed:20502675).
CC {ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}.
CC -!- SUBUNIT: Interacts with collagen IV and fibronectin via its laminin
CC EGF-like domains. Interaction with collagen may be required for stable
CC integration into the basement membrane. Interacts with NINL (By
CC similarity). Interacts with USH1C (PubMed:16301217). Component of USH2
CC complex, composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:20502675,
CC PubMed:25406310). Interacts with ADGRV1/MASS1 (via N-terminal PDZ
CC domain) (PubMed:20502675). Interacts (via the cytoplasmic region) with
CC WHRN (PubMed:16301217, PubMed:20502675, PubMed:23055499). Interacts
CC (via the cytoplasmic region) with PDZD7 (PubMed:23055499). Interacts
CC (via the cytoplasmic region) with VEZT and MYO7A (via MyTH4-FERM
CC domains); the interaction associates VEZT with the USH2 complex at the
CC stereocilia base (PubMed:17567809). {ECO:0000250|UniProtKB:O75445,
CC ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:17567809,
CC ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:23055499,
CC ECO:0000269|PubMed:25406310}.
CC -!- SUBCELLULAR LOCATION: Cell projection, stereocilium membrane
CC {ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:24334608}; Single-pass type I membrane protein.
CC Photoreceptor inner segment {ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:24334608}. Note=Component of the interstereocilia
CC ankle links in the inner ear sensory cells (PubMed:20502675,
CC PubMed:24334608). In photoreceptors, localizes at a plasma membrane
CC microdomain in the apical inner segment that surrounds the connecting
CC cilia called periciliary membrane complex (PubMed:20502675,
CC PubMed:24334608). {ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:24334608}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2QI47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2QI47-2; Sequence=VSP_017774, VSP_017775;
CC Name=3;
CC IsoId=Q2QI47-3; Sequence=VSP_017776;
CC -!- TISSUE SPECIFICITY: Present in the testis, epididymis, oviduct, spleen,
CC submaxillary gland, and small and large intestines. Not detected in the
CC brain, skin, lung, skeletal muscle, cardiac muscle, liver or kidney.
CC Expressed in smooth muscle of the colon and the epididymis. Also
CC present in select vascular basement membranes. In the cochlea, it is
CC present in virtually every basement membrane. It is particularly high
CC in the strial capillary basement membranes (SCBMs). In the retina, it
CC is again expressed in all of the basement membranes. It is also very
CC prevalent in the lens capsule and the Bruch's layer between the retinal
CC pigment epithelium and the choroid layer, which is very rich in
CC basement membranes. In neonates in it is widely expressed in the
CC basement membranes of the cochlea. Present in the synaptic terminals of
CC retinal photoreceptors (at protein level).
CC {ECO:0000269|PubMed:11788194, ECO:0000269|PubMed:16301216,
CC ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675}.
CC -!- DOMAIN: The PDZ-binding motif mediates the association with some of the
CC PDZ domains of USH1C and WHRN. {ECO:0000269|PubMed:20502675}.
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DR EMBL; AF151717; AAF70550.1; -; mRNA.
DR EMBL; DQ073638; AAZ23164.1; -; mRNA.
DR EMBL; AC121799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15607.1; -. [Q2QI47-1]
DR RefSeq; NP_067383.3; NM_021408.3. [Q2QI47-1]
DR SMR; Q2QI47; -.
DR BioGRID; 204466; 4.
DR ComplexPortal; CPX-2501; USH2 complex.
DR CORUM; Q2QI47; -.
DR STRING; 10090.ENSMUSP00000050454; -.
DR GlyGen; Q2QI47; 68 sites.
DR iPTMnet; Q2QI47; -.
DR PhosphoSitePlus; Q2QI47; -.
DR PaxDb; Q2QI47; -.
DR PRIDE; Q2QI47; -.
DR ProteomicsDB; 299651; -. [Q2QI47-1]
DR ProteomicsDB; 299653; -. [Q2QI47-3]
DR Antibodypedia; 53933; 51 antibodies from 10 providers.
DR Ensembl; ENSMUST00000060479; ENSMUSP00000050454; ENSMUSG00000026609. [Q2QI47-1]
DR GeneID; 22283; -.
DR KEGG; mmu:22283; -.
DR UCSC; uc007eae.1; mouse. [Q2QI47-2]
DR UCSC; uc007eaf.1; mouse. [Q2QI47-1]
DR CTD; 7399; -.
DR MGI; MGI:1341292; Ush2a.
DR VEuPathDB; HostDB:ENSMUSG00000026609; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000158456; -.
DR HOGENOM; CLU_000067_0_0_1; -.
DR InParanoid; Q2QI47; -.
DR OMA; CNGVITH; -.
DR PhylomeDB; Q2QI47; -.
DR TreeFam; TF330287; -.
DR BioGRID-ORCS; 22283; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ush2a; mouse.
DR PRO; PR:Q2QI47; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q2QI47; protein.
DR Bgee; ENSMUSG00000026609; Expressed in retinal neural layer and 23 other tissues.
DR ExpressionAtlas; Q2QI47; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0002141; C:stereocilia ankle link; IDA:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
DR GO; GO:0060171; C:stereocilium membrane; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:1990696; C:USH2 complex; IDA:UniProtKB.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0017022; F:myosin binding; IPI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0035315; P:hair cell differentiation; IEP:BHF-UCL.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; IC:ComplexPortal.
DR GO; GO:0048496; P:maintenance of animal organ identity; ISO:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 10.
DR CDD; cd00063; FN3; 29.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.40.10; -; 32.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR026915; USH2A.
DR PANTHER; PTHR10574:SF274; PTHR10574:SF274; 16.
DR Pfam; PF00041; fn3; 13.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00060; FN3; 34.
DR SMART; SM00282; LamG; 2.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49265; SSF49265; 21.
DR SUPFAM; SSF49899; SSF49899; 3.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS50853; FN3; 34.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Hearing; Laminin EGF-like domain; Membrane;
KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal;
KW Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..5193
FT /note="Usherin"
FT /id="PRO_0000229805"
FT TOPO_DOM 35..5033
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5034..5054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5055..5193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 268..514
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 515..571
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 572..637
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 638..690
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 691..743
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 744..791
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 792..848
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 853..896
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 897..947
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 948..998
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 999..1049
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1055..1143
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1147..1241
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1242..1357
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1358..1462
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1463..1566
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1511..1700
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1705..1882
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1847..1946
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1948..2045
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2046..2132
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2133..2234
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2235..2321
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2322..2421
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2422..2525
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2526..2613
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2617..2713
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2717..2810
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2811..2914
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2918..3009
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3013..3103
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3395..3489
FT /note="Fibronectin type-III 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3490..3580
FT /note="Fibronectin type-III 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3581..3671
FT /note="Fibronectin type-III 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3672..3766
FT /note="Fibronectin type-III 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3769..3857
FT /note="Fibronectin type-III 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3858..3955
FT /note="Fibronectin type-III 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3956..4059
FT /note="Fibronectin type-III 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4060..4148
FT /note="Fibronectin type-III 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4149..4256
FT /note="Fibronectin type-III 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4257..4346
FT /note="Fibronectin type-III 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4347..4437
FT /note="Fibronectin type-III 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4438..4522
FT /note="Fibronectin type-III 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4523..4625
FT /note="Fibronectin type-III 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4628..4725
FT /note="Fibronectin type-III 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4726..4818
FT /note="Fibronectin type-III 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4819..4921
FT /note="Fibronectin type-III 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4922..5005
FT /note="Fibronectin type-III 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1931..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5191..5193
FT /note="PDZ-binding"
FT COMPBIAS 1936..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2095
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3023
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 515..524
FT /evidence="ECO:0000250"
FT DISULFID 517..533
FT /evidence="ECO:0000250"
FT DISULFID 535..546
FT /evidence="ECO:0000250"
FT DISULFID 549..569
FT /evidence="ECO:0000250"
FT DISULFID 572..581
FT /evidence="ECO:0000250"
FT DISULFID 574..602
FT /evidence="ECO:0000250"
FT DISULFID 605..614
FT /evidence="ECO:0000250"
FT DISULFID 617..635
FT /evidence="ECO:0000250"
FT DISULFID 638..652
FT /evidence="ECO:0000250"
FT DISULFID 640..659
FT /evidence="ECO:0000250"
FT DISULFID 661..670
FT /evidence="ECO:0000250"
FT DISULFID 673..688
FT /evidence="ECO:0000250"
FT DISULFID 691..705
FT /evidence="ECO:0000250"
FT DISULFID 693..712
FT /evidence="ECO:0000250"
FT DISULFID 714..723
FT /evidence="ECO:0000250"
FT DISULFID 726..741
FT /evidence="ECO:0000250"
FT DISULFID 744..756
FT /evidence="ECO:0000250"
FT DISULFID 746..763
FT /evidence="ECO:0000250"
FT DISULFID 765..774
FT /evidence="ECO:0000250"
FT DISULFID 777..789
FT /evidence="ECO:0000250"
FT DISULFID 792..805
FT /evidence="ECO:0000250"
FT DISULFID 794..812
FT /evidence="ECO:0000250"
FT DISULFID 814..823
FT /evidence="ECO:0000250"
FT DISULFID 826..846
FT /evidence="ECO:0000250"
FT DISULFID 867..876
FT /evidence="ECO:0000250"
FT DISULFID 879..894
FT /evidence="ECO:0000250"
FT DISULFID 897..910
FT /evidence="ECO:0000250"
FT DISULFID 899..917
FT /evidence="ECO:0000250"
FT DISULFID 919..928
FT /evidence="ECO:0000250"
FT DISULFID 931..945
FT /evidence="ECO:0000250"
FT DISULFID 948..960
FT /evidence="ECO:0000250"
FT DISULFID 950..967
FT /evidence="ECO:0000250"
FT DISULFID 969..979
FT /evidence="ECO:0000250"
FT DISULFID 982..996
FT /evidence="ECO:0000250"
FT DISULFID 999..1011
FT /evidence="ECO:0000250"
FT DISULFID 1001..1018
FT /evidence="ECO:0000250"
FT DISULFID 1020..1029
FT /evidence="ECO:0000250"
FT DISULFID 1032..1047
FT /evidence="ECO:0000250"
FT DISULFID 1663..1700
FT /evidence="ECO:0000250"
FT DISULFID 1853..1882
FT /evidence="ECO:0000250"
FT VAR_SEQ 1460..1461
FT /note="AP -> GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12160733"
FT /id="VSP_017774"
FT VAR_SEQ 1462..5193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12160733"
FT /id="VSP_017775"
FT VAR_SEQ 5090
FT /note="V -> VFDSVADISDVSSNVTLKSYTMHFE (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017776"
FT CONFLICT 78
FT /note="C -> R (in Ref. 1; AAF70550 and 2; AAZ23164)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="E -> D (in Ref. 1; AAF70550 and 2; AAZ23164)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> R (in Ref. 1; AAF70550 and 2; AAZ23164)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="P -> S (in Ref. 1; AAF70550 and 2; AAZ23164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5193 AA; 569660 MW; 5579C5D8665CA121 CRC64;
MHYLALSPGF LCYTIKTLIL AYLASVLVLA ASQGVFPRLE NVGAFRKVST VPTHATCGFP
GPSTFCRSPV AAEHVQLCTE RLCIQDCPYR SASPLYTALL EGLRSCIPAD DGDLHPYSRS
SSVSFMFGSH QNCPSLRAPR LAAELTLAVW LKLEQGGTMC VIEKTVDGQI VFKVTISEKE
TMFYYRTVNG LQPPIKVMTP GRILMKKWIH LTVQVHQTAI SFFVDGLEEN STAFDTRTLH
DSVTDSVSSV IQVGQSLNGS EQFVGRMQDF RLYNVSLTNR EILEVFSGDF PHLHIQPHCR
CPGSHPRVHP SVQQYCIPNG AGDTPEHRMS RLNPEAHPLS FINDDDVATS WISHVFTNIT
QLYEGVAISI DLENGQYQVL KVITQFSSLQ PVAIRIQRKK ADSSPWEDWQ YFARNCSVWG
MKDNEDLENP NSVNCLQLPD FIPFSHGNVT FDLLTSGQKH RPGYNDFYNS SVLQEFMRAT
QIRLHFHGQY YPAGHTVDWR HQYYAVDEII VSGRCQCHGH AETCDRTRRP YRCLCSPHSF
TEGPQCDRCS PLYNDKPFRS GDNVNAFNCK PCQCHGHASS CHYDASVDPF PLEHNRGGGG
VCDDCQHHTT GRHCESCQDY FYRPVGADPA APDACKLCDC NRAGTRNGSL HCDPIGGQCD
CKRRVSGRQC LQCQDGFYDL QALDPDGCRP CNCNPSGTVD GDITCHQNSG QCSCKANVIG
LRCNRCNFGF KFLQSFNGDG CEPCQCNLHG SVNQLCDPLS GQCACKKEAK GLKCDSCREN
FYGLPWSACE VCDCSKAGSQ PGTVCDTETG QCVCKPNVGG RQCSQCKAGY FNLYQNDSHL
CLTCNCEKMG TVNGSLRCDK STGQCPCKLG VTGLRCHQCK PHRFNLTMDN PQGCQACDCD
SLGTLPGSMC DPISGQCLCL PHRQGRRCEQ CQPGFYSSPS NATGCLPCLC HTAGAVSHIC
NSVTGQCSCH DPSTTGRSCH QCQESYFRFD PLTGRCRPCH CHVAGASNGT CDAVTGQCFC
KEFVTGSKCD TCVPGASHLD VNNLLGCSKT PSQQPPPRGW VQSSSTINVS WSPPECPNAH
WLTYTLFRNG SEIYTTEDEH PYYTQYFLDT SLSPHTAYSY YIETSNVHSS TRSIPVIYET
KPEVSEGHLN LTHIIPVGSD SITLTWTGLS NSSDPVAKYV LSCTPVDSTE PCVSYEGPET
SATIWNLVPF TQYCFSVQGC TNESCFYSLP IIVTTAQAPP QTQGPPTVWK ISPTELRIEW
SPPVDSNGII ISYELYMRRW LSTEESLVFE SHGLVSSHSA LQSVNPSKNL LQQPQASTFI
SGLEPHTEYA FRVLAVNMAG RVSSAWASER TGESVPVFMA PPSVSPLSPH SLSVSWEKPA
ENFTRGEIIG YKISMVSEHF PLHDVPVMCS KMVHFAKSQD QSYIVRGLEP YRTYSFTVSL
CDSVGCVTSA LGSGQTLAAA PAQLRPPMVT GVNSTTVHIR WLPPAGVNGP PPLYHLERKK
SSLPAATAAV TKGTRFVGHG YCRFPRTAHA DFIGIKASFR TRVPEGLILL ALSPGDQEEY
FTLQLKNGRP YFLYNSQGTL VEVTPTDDPS QGYRDGEWHE IIAVRHQAFG QITLDGQYTG
SSSSLNGSSV TGGYTGLFVG GVPQGHSVLQ KRLEIIQRGF VGCLKDVFIM KGYSPSGTWL
PLDWQSSEEQ VNVHPSWEGC PTNLEEGVQF LGAGFLELPS DTFHAAKDFE ISLKFQTDQL
NGLLLFIHNT EGPDFLAVEL KRGLLSFKFN SSLVFTRVDL RLGLADCDGK WNTVSIKKEG
SVVSVRVNAL KKSTSQAGGQ PLLVNSPVYL GGIPRELQDA YRHLTLEPGF RGCVKEVAFA
RGVVVNLASV SSRAVRVNQD GCLSSDSTVN CGGNDSILVY RGSQQSVYES GLQPFTEYLY
RVTASHEGGA VSSDWSRGRT LGTAPQSVPT PSRAQSINGS SVEVAWNEPA VVKGVLEKYV
LKAYSEDSSQ PRVPSASTEL HDTSTHSGVL IGLHPFHSYT VTLTACSRAG CTESSQALSI
STPQEAPQEV QAPVAVALPN SLSFFWSLPR QANGIITQYS LYVDGRLVYT GKGQNYTVTD
LRVFAAYEII VGACTQAGCT NSSQVILHTA QLPPEQVDPP GLTVLDSRTI HVRWKQPRQL
NGILERYILY ILNPIHNSTM WSVVYNSTEK LQAHVLHHLS PGGLYLIRLR VCTGGGCTTS
EPSQALMEET IPEGVPAPRA HSYSPDSFNI SWTEPEYPNG VITTYELYLD DTLIHNSSGL
SCHAYGFDPG SLHTFQVQAC TAKGCALGPL VGNRTLEAPP EGVVNVLVKP EGSREAHVRW
DAPAHPNGRL TYSVHFTGSF YADQAGDNYT LLSGTKTIRG IEGSRLWVLV DGLVPCSHYM
VQVNASNSRG SVLSDPVSVE MPPGAPDGLL SPRLAAAAPT SLQVVWSTPA RNNAPGSPRY
QLQMRPGPST HGRLELFPIP SASLSYEVTG LQPFTVYEFR LVATNGFGTA YSAWTPLMTT
EDKPGPIDAP ILINVKARML SVIWRQPAKC NGAITHYNIY LHGRLYLTVS GRVTNYTVVP
LHPYKAYHFQ VEACTSQGCS KSPSSETVWT LPGNPEGIPS PQLFPYTPTS IIVTWQPSAH
LDLLVENVTI ERRVKGKKEV RNLVTLARSQ AMKFIDNDPA LRPWTRYEYR VLGSTLDGGT
NSSAWVEVTT RPCRPSGVQP PTVRVLAPDT VEVSWKAPLM QNGDILSYEI RMPEPLIKMT
NMSSIMLSHL VKHLIPFTNY SVTIVACSGG NGYLAGCTES PPTLATTHPA PPQELAPLSV
ILLSESDVGI SWQPPSKPNG PNLRYELLRC KIQQPLASNP PEDLNLWHNI YSGTRWFYKD
KGLSRFTTYE YKLFVHNSVG FTPSREVTVT TLAGSPERGA TVTASILNHT AIDVRWKKPT
FQDLQGDVEY YTLFWSSGTS EESLKIFPDV DFHVIGQLSP NVEYQVFLLV FNGVHAINST
VVHVTMWEEE PQGMLPPEVV IINSTAVRVI WTSPSNPNAV VTESSVYVNN KLYKTGTDAP
GSFVLEDLSP FTIYDIQVEV CTKDACVKSN GTQVSTAEDT PSDISIPVIR GITSRSLQID
WTTPANPNGI ILGYDVLRKT WRPCSETQKL TDKPRDELCK AVKCQYPGKV CGHTCYSPGT
KVCCDGLLYD PQPGYSCCED KYIALSPNAT GVCCGGRMWE AQPDHQCCSG HYARILPGEI
CCPDERHNRV SVGFGDACCG TMPYATSGSQ VCCAGRLQDG YRQQCCGGEM VSQDFQCCGG
GEEGMVYSYL PGMLCCGQDY VNMSETICCS ASSGESKAHV RKDDPTPVKC CGTELSPESQ
RCCDGVGYNP LKYVCSDEIS AGMAMKETRV CATICPATMK ATAHCGRCDF NATTHICTVM
RGPLNPTGKK AVEGLCSAAE EIVHSGDVNT HSFIDRDLKP STVYEYRISA WNSYGRGFSQ
SVRASTREDV PEGVKAPRWA RTGKHEDVIF LQWEEPMQSN GPIIHYILFR DGRERFQGTA
LSFTDTQGIQ PLQEYSYQLK ACTAAGCAVS CKVVAATTQR SPENVPPPNI TAQSSETLHL
SWSVPEKMKD AIKAYQLWLD GKGLIYTDTS DRRQHTVTGL QPYTNYSFTL AVCTSVGCTS
SEPCVGQTLQ AAPQGVWVTP RHIIINSTTV ELYWNPPERP NGLISQYQLR RNGSLLLVGG
RDNQSFTDSN LEPGSRYIYK LEARTGGGSS WSEDYLVQMP LWTPEDIHPP CNVTVLGSDS
IFVAWPTPGN LLPKIPVEYS ILLSGGSVTL LVFSVRHRQS AHLKNLSPFT QYEIRIQACQ
NGGCGVSPGT YVRTLEAAPV GLMPPLLKAL GSSCIEVKWM PPTRPNGIIT SYVVHRRPAD
TEEESLLFVW SEGALEFTDD TGTLRPFTLY EYRVRAWNSQ GAVDSPWSTI QTLEAPPRGL
PAPRVQATSA HSAMLNWTEP EAPNGLISQY HVIYQERPDA AAPGSSTVHA FTVTGTSRQA
HLFGLEPFTT YHIGVVAVNS AGKVSSPWTL IKTLESAPSG LMNFTVEQRE KGRALLLQWS
EPVKTNGVIK AYNIFNDGVL EYSGLGRQFL FRRLAPFTLY TLILEACTTA GCAHSVPQPL
WTEEAPPDTQ MAPTIQSVGP TNVRLHWSQP ASPNGKIIHY EVIRRRSEEE DWGNTTWQAD
GNTVFTEYNT QGNAWVYNDT GLQPWRQYAY RICAWNSAGH TCSSWNVVRT LQAPPDGLSP
PEISYVSMSP LQLLISWLPP RHSNGVIQGY RLQRDGVLPA LNFNASTFSY MDSQLLPFST
YSYAILACTG GGCCTSEPTN ITTPEVPPSE VSPPVLWDIS AHQMNVSWSP PSIPNGKIVK
YLLQCDGEEH LAGQGLSFLL SNLQPSTQYN ISLVACTSGG CTASRTTSAW TKEAPPENMD
PPTLHITGPE SIEITWTPPR NPHGLIRSYE LRRDGAIVYV GLETRYHDFT LAPGVEYSYS
VTATNSRGSV LSPLVKGQTS PSAPSGLQPP KLHSGDALEL LADWDPPVRT NGKIINYTLF
VREMFEGKTR AMSINTTHSS FGTRSLTVKH LKPFHRYEVR VQACTALGCT SSEWTSTQTS
EVPPLRQPAP HLEVQTATGG FQPIVAVWWA GPLQPNGKII CFELYRRQVA AWPGTSSSLL
IYNGSFRSFM DSELLPFTEY EYQVWAVNSA GKAASNWTRC RTGPAPPEGL QAPTFHTVSS
TRAVVNISVP SRPNGNISLF RVFSNSSGTH VTLSEGTATQ QTLHDLSPFT TYTIGVEACT
CFNCCSRGPT AELRTHPAPP SGLSPPQVQT LGSRMASVHW TPPLLPNGVI HSYELQLQRA
CPPDSAPRCP PSHTERKYWG PGHRASLAGL QPNTAYGVQV VAYNEAGSTA SGWTNFSTKK
EMPQYQALFS VDSNASMVWV DWSGTFLLNG HLKEYVVTDG GRRVYSGLDT TLYIPRMVDK
IFFFQVTCTT DIGSVKTPLV QYDAATGSGL VLTTPGEKKG AGTKSTEFYS ELWFIMVMAV
VGLILLAIFL SLILQRKIHK EPCIRERPPL VPLQKRMTPL SVYPPGETHV GLADTRLPRS
GTPMSIRSSQ SVSVLRIPSQ SQLSHAYSQS SLHRSVSQLM DMADKKVVTE DSLWETIMGH
SSGLYVDEEE LMNAIKGFSS VTKEHTAFTD THL
