GenomeNet

Database: UniProt
Entry: Q2QI47
LinkDB: Q2QI47
Original site: Q2QI47 
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   16-JAN-2019, entry version 115.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Pretto D., 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
RT   Usher syndrome type IIA and the cellular source of USH2A mRNA in
RT   retina, a target 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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.,
RA   Cosgrove D.;
RT   "Localization and expression of usherin: a novel basement membrane
RT   protein 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.,
RA   Chardenoux S., Weil D., El-Amraoui A., Petit C.;
RT   "Usherin, the defective protein in Usher syndrome type IIA, is likely
RT   to be a component of interstereocilia ankle links in the inner ear
RT   sensory 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.,
RA   Wolfrum U.;
RT   "Scaffold protein harmonin (USH1C) provides molecular links between
RT   Usher 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
RP   AND 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
RP   IN 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.,
RA   McMillan D.R., Liberman M.C., Li T.;
RT   "Ablation of whirlin long isoform disrupts the USH2 protein complex
RT   and 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.,
RA   Wang Y., Yang J.;
RT   "Deletion of PDZD7 disrupts the Usher syndrome type 2 protein complex
RT   in 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
RT   required to form the quaternary protein complex associated with Usher
RT   syndrome type 2.";
RL   J. Biol. Chem. 289:36070-36088(2014).
CC   -!- FUNCTION: Involved in hearing and vision as member of the USH2
CC       complex (PubMed:20502675). In the inner ear, required for the
CC       maintenance of hair bundle ankle formation, which connects growing
CC       stereocilia in developing cochlear hair cells (PubMed:20502675,
CC       PubMed:24334608). In retina photoreceptors, the USH2 complex is
CC       required for the maintenance of periciliary membrane complex that
CC       seems to play a role in regulating intracellular protein transport
CC       (PubMed:20502675). {ECO:0000269|PubMed:20502675,
CC       ECO:0000269|PubMed:24334608}.
CC   -!- SUBUNIT: Interacts with collagen IV and fibronectin via its
CC       laminin EGF-like domains. Interaction with collagen may be
CC       required for stable integration into the basement membrane.
CC       Interacts with NINL (By similarity). Interacts with USH1C
CC       (PubMed:16301217). Component of USH2 complex, composed of ADGRV1,
CC       PDZD7, USH2A and WHRN (PubMed:20502675, PubMed:25406310).
CC       Interacts with ADGRV1/MASS1 (via N-terminal PDZ domain)
CC       (PubMed:20502675). Interacts (via the cytoplasmic region) with
CC       WHRN (PubMed:16301217, PubMed:20502675, PubMed:23055499).
CC       Interacts (via the cytoplasmic region) with PDZD7
CC       (PubMed:23055499). Interacts (via the cytoplasmic region) with
CC       VEZT and MYO7A (via MyTH4-FERM domains); the interaction
CC       associates VEZT with the USH2 complex at the stereocilia base
CC       (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
CC       interstereocilia ankle links in the inner ear sensory cells
CC       (PubMed:20502675, PubMed:24334608). In photoreceptors, localizes
CC       at a plasma membrane microdomain in the apical inner segment taht
CC       surrounds the connecting cilia called periciliary membrane complex
CC       (PubMed:20502675, 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,
CC       spleen, submaxillary gland, and small and large intestines. Not
CC       detected in the brain, skin, lung, skeletal muscle, cardiac
CC       muscle, liver or kidney. Expressed in smooth muscle of the colon
CC       and the epididymis. Also present in select vascular basement
CC       membranes. In the cochlea, it is present in virtually every
CC       basement membrane. It is particularly high in the strial capillary
CC       basement membranes (SCBMs). In the retina, it is again expressed
CC       in all of the basement membranes. It is also very prevalent in the
CC       lens capsule and the Bruch's layer between the retinal pigment
CC       epithelium and the choroid layer, which is very rich in basement
CC       membranes. At postnatal day 0 in it is widely expressed in the
CC       basement membranes of the cochlea. Present in the synaptic
CC       terminals of 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
CC       of the PDZ domains of USH1C and WHRN.
CC       {ECO:0000269|PubMed:20502675}.
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   UniGene; Mm.331238; -.
DR   ProteinModelPortal; Q2QI47; -.
DR   SMR; Q2QI47; -.
DR   BioGrid; 204466; 2.
DR   CORUM; Q2QI47; -.
DR   STRING; 10090.ENSMUSP00000050454; -.
DR   iPTMnet; Q2QI47; -.
DR   PhosphoSitePlus; Q2QI47; -.
DR   PaxDb; Q2QI47; -.
DR   PRIDE; Q2QI47; -.
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   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410Y1E5; LUCA.
DR   GeneTree; ENSGT00940000158456; -.
DR   HOGENOM; HOG000124780; -.
DR   HOVERGEN; HBG094138; -.
DR   InParanoid; Q2QI47; -.
DR   KO; K19636; -.
DR   OMA; CTKYACV; -.
DR   OrthoDB; 5155at2759; -.
DR   TreeFam; TF330287; -.
DR   ChiTaRS; Ush2a; mouse.
DR   PRO; PR:Q2QI47; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026609; Expressed in 15 organ(s), highest expression level in testis.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032420; C:stereocilium; ISO: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:1990696; C:USH2 complex; IDA:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0017022; F:myosin binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI: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:0060113; P:inner ear receptor cell differentiation; IMP:MGI.
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:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 29.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   Gene3D; 2.60.40.10; -; 33.
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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   InterPro; IPR026915; USH2A.
DR   PANTHER; PTHR10574:SF274; PTHR10574:SF274; 15.
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;
KW   Complete proteome; Disulfide bond; Glycoprotein; Hearing;
KW   Laminin EGF-like domain; Membrane; Reference proteome; Repeat;
KW   Secreted; Sensory transduction; Signal; Transmembrane;
KW   Transmembrane helix; Vision.
FT   SIGNAL        1     34       {ECO:0000255}.
FT   CHAIN        35   5193       Usherin.
FT                                /FTId=PRO_0000229805.
FT   TOPO_DOM     35   5033       Extracellular. {ECO:0000255}.
FT   TRANSMEM   5034   5054       Helical. {ECO:0000255}.
FT   TOPO_DOM   5055   5193       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      268    514       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      515    571       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      572    637       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      638    690       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      691    743       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      744    791       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      792    848       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      853    896       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      897    947       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      948    998       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      999   1049       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1055   1143       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1147   1241       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1242   1357       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1358   1462       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1463   1566       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1511   1700       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1705   1882       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1847   1946       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1948   2045       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2046   2132       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2133   2234       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2235   2321       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2322   2421       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2422   2525       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2526   2613       Fibronectin type-III 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2617   2713       Fibronectin type-III 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2717   2810       Fibronectin type-III 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2811   2914       Fibronectin type-III 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2918   3009       Fibronectin type-III 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3013   3103       Fibronectin type-III 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3395   3489       Fibronectin type-III 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3490   3580       Fibronectin type-III 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3581   3671       Fibronectin type-III 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3672   3766       Fibronectin type-III 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3769   3857       Fibronectin type-III 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3858   3955       Fibronectin type-III 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     3956   4059       Fibronectin type-III 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4060   4148       Fibronectin type-III 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4149   4256       Fibronectin type-III 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4257   4346       Fibronectin type-III 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4347   4437       Fibronectin type-III 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4438   4522       Fibronectin type-III 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4523   4625       Fibronectin type-III 32.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4628   4725       Fibronectin type-III 33.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4726   4818       Fibronectin type-III 34.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4819   4921       Fibronectin type-III 35.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     4922   5005       Fibronectin type-III 36.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   MOTIF      5191   5193       PDZ-binding.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    258    258       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    358    358       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    415    415       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    647    647       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    836    836       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    853    853       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    885    885       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    941    941       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1008   1008       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1068   1068       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1089   1089       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1150   1150       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1171   1171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1222   1222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1382   1382       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1473   1473       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1626   1626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1770   1770       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1894   1894       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1958   1958       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2095   2095       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2121   2121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2177   2177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2186   2186       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2249   2249       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2276   2276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2313   2313       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2368   2368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2404   2404       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2575   2575       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2647   2647       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2701   2701       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2761   2761       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2779   2779       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2928   2928       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2998   2998       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3023   3023       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3090   3090       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3208   3208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3322   3322       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3411   3411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3589   3589       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3645   3645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3686   3686       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3712   3712       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3723   3723       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3772   3772       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3976   3976       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4063   4063       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4194   4194       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4218   4218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4304   4304       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4340   4340       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4365   4365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4410   4410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4556   4556       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4575   4575       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4683   4683       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4716   4716       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4746   4746       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4756   4756       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4765   4765       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4915   4915       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4934   4934       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    515    524       {ECO:0000250}.
FT   DISULFID    517    533       {ECO:0000250}.
FT   DISULFID    535    546       {ECO:0000250}.
FT   DISULFID    549    569       {ECO:0000250}.
FT   DISULFID    572    581       {ECO:0000250}.
FT   DISULFID    574    602       {ECO:0000250}.
FT   DISULFID    605    614       {ECO:0000250}.
FT   DISULFID    617    635       {ECO:0000250}.
FT   DISULFID    638    652       {ECO:0000250}.
FT   DISULFID    640    659       {ECO:0000250}.
FT   DISULFID    661    670       {ECO:0000250}.
FT   DISULFID    673    688       {ECO:0000250}.
FT   DISULFID    691    705       {ECO:0000250}.
FT   DISULFID    693    712       {ECO:0000250}.
FT   DISULFID    714    723       {ECO:0000250}.
FT   DISULFID    726    741       {ECO:0000250}.
FT   DISULFID    744    756       {ECO:0000250}.
FT   DISULFID    746    763       {ECO:0000250}.
FT   DISULFID    765    774       {ECO:0000250}.
FT   DISULFID    777    789       {ECO:0000250}.
FT   DISULFID    792    805       {ECO:0000250}.
FT   DISULFID    794    812       {ECO:0000250}.
FT   DISULFID    814    823       {ECO:0000250}.
FT   DISULFID    826    846       {ECO:0000250}.
FT   DISULFID    867    876       {ECO:0000250}.
FT   DISULFID    879    894       {ECO:0000250}.
FT   DISULFID    897    910       {ECO:0000250}.
FT   DISULFID    899    917       {ECO:0000250}.
FT   DISULFID    919    928       {ECO:0000250}.
FT   DISULFID    931    945       {ECO:0000250}.
FT   DISULFID    948    960       {ECO:0000250}.
FT   DISULFID    950    967       {ECO:0000250}.
FT   DISULFID    969    979       {ECO:0000250}.
FT   DISULFID    982    996       {ECO:0000250}.
FT   DISULFID    999   1011       {ECO:0000250}.
FT   DISULFID   1001   1018       {ECO:0000250}.
FT   DISULFID   1020   1029       {ECO:0000250}.
FT   DISULFID   1032   1047       {ECO:0000250}.
FT   DISULFID   1663   1700       {ECO:0000250}.
FT   DISULFID   1853   1882       {ECO:0000250}.
FT   VAR_SEQ    1460   1461       AP -> GK (in isoform 2).
FT                                {ECO:0000303|PubMed:12160733}.
FT                                /FTId=VSP_017774.
FT   VAR_SEQ    1462   5193       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12160733}.
FT                                /FTId=VSP_017775.
FT   VAR_SEQ    5090   5090       V -> VFDSVADISDVSSNVTLKSYTMHFE (in
FT                                isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_017776.
FT   CONFLICT     78     78       C -> R (in Ref. 1; AAF70550 and 2;
FT                                AAZ23164). {ECO:0000305}.
FT   CONFLICT    178    178       E -> D (in Ref. 1; AAF70550 and 2;
FT                                AAZ23164). {ECO:0000305}.
FT   CONFLICT    206    206       K -> R (in Ref. 1; AAF70550 and 2;
FT                                AAZ23164). {ECO:0000305}.
FT   CONFLICT    624    624       P -> S (in Ref. 1; AAF70550 and 2;
FT                                AAZ23164). {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
//
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