USH2A_RAT
ID USH2A_RAT Reviewed; 5125 AA.
AC Q8K3K1; F1M2F9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 114.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
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).
CC -!- FUNCTION: Involved in hearing and vision as member of the USH2 complex.
CC In the inner ear, required for the hair bundle ankle formation, which
CC connects growing stereocilia in developing cochlear hair cells. 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. {ECO:0000250|UniProtKB:Q2QI47}.
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. Interacts (via the cytoplasmic
CC region) with PDZD7. Component of USH2 complex, composed of ADGRV1,
CC PDZD7, USH2A and WHRN. Interacts with ADGRV1/MASS1 (via N-terminal PDZ
CC domain). Interacts (via the cytoplasmic region) with WHRN. 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 (By similarity). {ECO:0000250|UniProtKB:O75445,
CC ECO:0000250|UniProtKB:Q2QI47}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, stereocilium membrane
CC {ECO:0000250|UniProtKB:Q2QI47}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q2QI47}. Note=Component of the interstereocilia
CC ankle links in the inner ear sensory cells. In photoreceptors,
CC localizes at a plasma membrane microdomain in the apical inner segment
CC that surrounds the connecting cilia called periciliary membrane
CC complex. {ECO:0000250|UniProtKB:Q2QI47}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q8K3K1-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3K1-1; Sequence=VSP_059945;
CC -!- TISSUE SPECIFICITY: Present in the synaptic terminals of inner ear hair
CC cells (at protein level). Predominantly expressed in the retina and
CC cochlea. Weakly expressed in brain and kidney. Detectable from E17 in
CC the neural epithelium, but not in the retinal pigment epithelium (RPE)
CC of the developing retina. After birth, it is expressed at P7 and
CC remains expressed during adulthood. {ECO:0000269|PubMed:12160733,
CC ECO:0000269|PubMed:16301216}.
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DR EMBL; AY077844; AAL78289.1; -; mRNA.
DR EMBL; AABR07022087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07022095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q8K3K1; -.
DR IntAct; Q8K3K1; 1.
DR STRING; 10116.ENSRNOP00000004992; -.
DR GlyGen; Q8K3K1; 19 sites.
DR PhosphoSitePlus; Q8K3K1; -.
DR PaxDb; Q8K3K1; -.
DR UCSC; RGD:628777; rat. [Q8K3K1-2]
DR RGD; 628777; Ush2a.
DR eggNOG; KOG1836; Eukaryota.
DR HOGENOM; CLU_000067_0_0_1; -.
DR InParanoid; Q8K3K1; -.
DR PhylomeDB; Q8K3K1; -.
DR PRO; PR:Q8K3K1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:1990075; C:periciliary membrane compartment; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0002141; C:stereocilia ankle link; ISS:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0032421; C:stereocilium bundle; ISO:RGD.
DR GO; GO:0060171; C:stereocilium membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:1990696; C:USH2 complex; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0035315; P:hair cell differentiation; ISO:RGD.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; ISO:RGD.
DR GO; GO:0048496; P:maintenance of animal organ identity; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
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; 31.
DR CDD; cd00110; LamG; 2.
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; 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; 12.
DR Pfam; PF00053; Laminin_EGF; 9.
DR Pfam; PF00054; Laminin_G_1; 2.
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; 6.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS50853; FN3; 33.
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; Vision.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..5125
FT /note="Usherin"
FT /id="PRO_0000229806"
FT DOMAIN 273..513
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 514..570
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 571..636
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 637..689
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 690..742
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 743..790
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 791..842
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 843..895
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 896..946
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 947..997
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 998..1048
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1054..1142
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1146..1240
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1241..1356
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1357..1461
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1510..1697
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1702..1879
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1857..1943
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1945..2042
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2043..2132
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2133..2230
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2231..2318
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2319..2421
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2425..2519
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2520..2613
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2614..2709
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2713..2806
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2807..2910
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2914..3005
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3009..3099
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3380..3485
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3486..3577
FT /note="Fibronectin type-III 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3580..3670
FT /note="Fibronectin type-III 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3672..3762
FT /note="Fibronectin type-III 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3765..3852
FT /note="Fibronectin type-III 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3853..3950
FT /note="Fibronectin type-III 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3951..4054
FT /note="Fibronectin type-III 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4055..4143
FT /note="Fibronectin type-III 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4144..4251
FT /note="Fibronectin type-III 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4252..4344
FT /note="Fibronectin type-III 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4345..4432
FT /note="Fibronectin type-III 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4433..4517
FT /note="Fibronectin type-III 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4518..4620
FT /note="Fibronectin type-III 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4625..4720
FT /note="Fibronectin type-III 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4721..4813
FT /note="Fibronectin type-III 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4814..4916
FT /note="Fibronectin type-III 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1930..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 514..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 516..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 534..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 548..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 571..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 573..601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 604..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 616..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 637..651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 639..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 660..669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 672..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 690..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 692..711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 713..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 725..740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 743..755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 745..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 764..773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 776..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 791..804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 793..811
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 813..822
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 825..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 843..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 845..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 866..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 878..893
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 896..909
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 898..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 918..927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 930..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 947..959
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 949..966
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 981..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 998..1010
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1000..1017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1019..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1031..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1660..1697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1850..1879
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT VAR_SEQ 1457..5125
FT /note="AAAPAQLRSPMVTGVTSTTVHIRWLPPAEVNGPPPLYRLERRESFLPAATAA
FT RTKGTRFMGDGYCRFPRTAHPDFIGIKASFWTRVPEGLILLALHPDNQEEYFALQLKSG
FT RPYFLYNPQGSLVEVTTADDHSQQYSDGQWHEITAIRHQSFGQITLDEQYTDSSASLNG
FT SSVTGGYTRLFVGGLPQGHTILQKRPVRRGFVGCLKDVSILKGSSPSGTWLPLDWQSSE
FT EQVNVHHSWEGCPTDLEEGVQFLGAGFLELRSDTFHAAKDFEISLKFQTDQLNGLLLFI
FT HNTEGLDFLAMELKSGLLSFQLNSSRILTRVEVRLGRTHCDGKWNRVTIRREGSMVSVG
FT VNELTKSTSRAGDQPPLLTSPVYLGGIPQELQASYRHLTLEQGFRGCVKEVAFTRGAVV
FT NLASVSSRAVRVNQDGCLSSDSTVNCGGNDSILVYRGSRQSVYESGLQPFTEYLYRVTA
FT SHKGGSVSSDWSRGRTLGSAPHSVPTPSRAQSINGYSVEVAWNEPAMVKGVLEKYILKA
FT YSEDSAQPHMPSASTEFNNTDIRTGILTGLHPFHSYAVTLTACSRAGCTESSRALSIST
FT PQEAPQEVQAPVAEALPNSLSFFWSPPRQANGIITQYSLYMDGRLVYTGKGQNYTVTDL
FT RVFTAYEITVGACTRAGCTNSSRVILHTAQLPPERVDPPVLAILDSRTVHIQWKQPRQL
FT NGILERYILYTLNPTHNSTVWDVVYNSTENLQTHLLYHLSPGCLYLIKLGACTGGGCTT
FT SEPSQALMDETVPEGVPAPRAHSHSPDSFNISWTEPGHPNGVITTYELYLDGTLIHNSS
FT ELSCHAYGFDPGSLHTFQVQACTAKGCALGPLVENRTLEAPPEGTVNLFVKPEGSREAA
FT VRWDAPPHPNGRLTYSVLITGNFYADQAGDNYTLLSSTKTVHSSKGDRLWVLVDRLVPC
FT SNYTVQVNASNSQGSVLSDRVSVEMPPGAPDGLLSPRLAAATPTSLQVVWSTPARNNAP
FT GSPRYQLQMRPDPSTRGLLELFPIPSALLSYEVTGLQPFTVYEFRLVATNGFGSAYSDW
FT TPLMTTEDKPGPMDAPVLNVKAGMMSVAWRKPTECNGAITHYNIYQHGRLYLTVSGGVT
FT NCTVVHLRPHTAYQFQIEACSSKGCSMSPASETVWTLPGTPEGIPGPELLPYTPTKIIV
FT SWQPPTHLDGLVENITIERRVKEQEEVRSLVILPRSQAVRFIDNDPALRPWTHYEYRVL
FT GSTLNGGTNSSAWVEVTTRPSRPSGVQPPTVHVLGPDAVEVTWKAPLIRNGDIVSYEIR
FT MPDPLIEITNVTSFVLSHLVKHLIPFTNYSVSIVACSGGHGYLGGCTESLPTFATTHPA
FT LPQELTPLSISLLGQSYVGISWQPPSKPNGPNLRYELLRRKIQQPLASNPPEDLNLWHN
FT IYSGTRRFYEDKGLSRFTTYEYKLFVHNSLGFTPSQEVTVTTLAGSPERGATVTASILN
FT HTAIDVRWKRPTFQDLQGDVEYYTLFWSSGTSVESLKIFPDVDFHVIGHLAPNVEYQVF
FT LLVFNGVHAINSTVVRVTTWEEEPRGMRPPEVVIINSTAVRVIWTSPSNPNAVITESSV
FT YANNELHKAGAGAPGSFTLEDLSPFTIYDIQVEVCTKDACVKSSGTQVSTAEDTPSGIS
FT IPIIRDITSRSLQIDWTAPGNPNGIILGYDVLRKTWRLCSETQKLTDKPRDELCKAVKC
FT QYPGNVCGHTCYSPGTKVCCDGLLYDPQPGYSCCEEKYIALLPNSTGVCCGGRQREAQP
FT DHQCCSGHYIRILPGEICCPDERHNRVSVGFGDACCGTMPYATSGSQVCCAGKLQDGYR
FT RQCCGGEMVSQDFKCCGGGEEGMVYSSLPGMLCCGQDYVNMSDTICCSASSGDSKAHVR
FT GSDPMPVRCCHTELIPESQQCCDGVGYNPVKYVCSDEISAGMATEETRVCATVCPATMR
FT ATAHCGQCDFNATTHICTVSRGPLNPIGKETAEGLCSTAEEIVHSGDENTRSFIDTDLE
FT PSTVYEYRVSVWNSYGRGFSQSVRASTREDVPQGVTAPRWARTGNHEDVIFLTWKEPTQ
FT SNGPITHYILLRDGRERFQGAALSFTDTQGIQPLQEYSYQLKACTAAGCADSCKVVATA
FT TRGVLESVPPPNITAQSPETLHLSWSVPEKRNDAIKEYQLWLDGKGLIYTDTNDRRQHT
FT VTGLQPHTNYSFTLSACTSVGCTSSEPSVGQTLQAAPQGVWVTPRHIIINSTTVELYWN
FT PPERPNGVISQYRLRRNGSLLLVGGRDDQSFTDKNLEPNSRYIYTLEARTGGGSSLSEE
FT YLVQMPMWTPEDVHPPCNVTVLGSDSIFVAWPAPGILLPKIPVEYSILLSGGNMMLLTF
FT SVGLRQSAYLKNLAPFTQYEIRIQACQEGCGVSPGTHVRTLEAAPVGLMPPLLKALGSH
FT CIEVKWTPPTRPNGIITSYVIHRRPADTEEESLLFVWSEGALEFTDDTDTLRPFTLYEY
FT RVRAWNSKGVVDSPWSSVQTLEAPPQDLPAPWVQVTSAHSVLLNWTEPEAPNGLISQYH
FT VIYQERPDEAAPGSSTVHAFTVKGSSRQAHLFGLEPFTTYHIGVAAVNRAGKVSSPWTL
FT IKTLESAPSGLMNFTAEQREGGRALLLQWSEPVRTNGVIKAYNVFSDGLPEYSGLGRQF
FT LFRRLAPFTLYILTLEACTAAGCAHSVPQTLWTEEAPPDSQMAPTIQSVEPTSVRLHWS
FT QPANPNGKIIRYEVIRRRLQGEDWGNRTVQADENTVFTEYNTEGNGWVCTDTGLQPWGL
FT YSYRICTWNSAGHTCSSWSVVRTSQAPPDGLSPPEVSYVSTSPLQLLISWFAPRHTNGV
FT IQSYRLQRNGVFAAASFNSSTFSYTDGQLLPFTTYSYAVLACTGGGCCTSEPTNITTPE
FT ASPAGVSPPVLWAIGAHQINVSWSPPSVPNGKIAKYLLHCDGEEHLAGQDLSLLLSNLR
FT PFTQYNVSLVACTKGGCTASRVASAWTMEAPPEDMDPPTLHVMGPESIEITWAPPRNPH
FT GQIRSYELRRDGAIVYIGLETRYHDFILTPGVQYGYTVTATNSRGSVLSPLVKGQTSPS
FT APSGLQPPKLRAGEALELLVNWNPPVRTNGKITNYTLFIRELLEGEIRTMCINTTHSSF
FT GTRSLAVKHLKPFHRYEVRVQACTALGCTSSEWTPTQTSEIPPLLQPAPHLEVQTAAGG
FT FQPIVAVWWAGPLQPHGKIVRFELYRRQTASWPGTSSPLLIYNGSLSSFTDRELLPFTE
FT YEYQVWAVNSAGKVASNWTWCRTGPAPPEGLKAPTFHTVSSTQAVVNISAPSKPNGNIS
FT LFRVFSNSSGTHVMLSEGMATQQTLHDLRPFTTYAIGVEACTCFNCCSRGPTAELRTHP
FT APPSGLSPPQVQTLGSRMASFQWAPPQLPNGVIHSYELQLHRACPPDSAPHCPPSPTER
FT KYWGPGHRASLAGLQPNTAYGVQVVAHNEAGSTASGWTSFRTKKEMPQYQALFSVDSNA
FT STVWVDWSGTFVLNGQLKEYVVTDGGRRVYSGLDTTLYIPRTVDKTFFFQVTCTTDIGS
FT VKTPLVQYDATTGFGLVLTTPGGKKGAGTKSTEFYTDTRLPRSGTPVSIRSSQSVSVLR
FT IPSQSQLSHAYSQGSLHRSVSQLMDSPDKKALTEDSLWETIMGHSSGLCVDEEELMNAI
FT KGFSSVTKEHTAFTDTHL -> TAGKNVLTNTKKCTHVGNQYYRSAVLWASYMSSLFTA
FT PSSDILDVVYLESFKQNQH (in isoform 2)"
FT /id="VSP_059945"
FT CONFLICT 52
FT /note="S -> T (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..211
FT /note="HT -> LS (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> F (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..246
FT /note="MDSV -> TDSA (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> D (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="R -> Q (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="D -> G (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="C -> G (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="K -> E (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 887..890
FT /note="MDNP -> VDNL (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="D -> E (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 905..908
FT /note="LGSM -> PGST (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 924..939
FT /note="ERRCVQCQPGCYSSPS -> GRRCERCQPGFYSSPG (in Ref. 1;
FT AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 948..957
FT /note="LCHTVATKNC -> SCHTAGAVSH (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 965..969
FT /note="HCYCP -> QCSCR (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 976..978
FT /note="LSW -> QSC (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 984..996
FT /note="RYFRFDPLTGRCR -> HYFGFDPRTGRCQ (in Ref. 1;
FT AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002..1012
FT /note="VAGASNGTCDA -> LEGALNETCDV (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="T -> I (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044..1045
FT /note="LA -> FG (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1441
FT /note="A -> Y (in Ref. 1; AAL78289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5125 AA; 562986 MW; 9CC58BA0D18511D0 CRC64;
MYYLALSSGF LGQAIKTSIL AYLASVLLAA SQGVFPRLEN VGAFKKVSIV PSHATCGYPG
PSTFCRSAVA AEHAQLCAER LCIQDCPYRS ASPPYTALLE GLRSCIPADH GDLHPYSRSN
STSFIFGSHK NCPSLQAPRL AAEFTLAVWL KPERGSTMCV LEKTADGQIV FKVTISERET
MFYYRTVNGL QPPIKVMTPG RILMKKWIHH TVQVHETEVS SFVDGLEENS TAFDTRTLRD
SIMDSVPSTV LIGQSLNGSE LFVGRMQDFR LYNVSLTNRE ILELFSGDLP HLHIQSHCRC
PGSHPRVHPS VQQYCIPNGV EDTLQHRVSR LNPEAHPLSF INDDDVATSW ISHVFTDITQ
LNQGVAISID LENGQYQVFQ ITIRFSSPQP VAMRIQRKKA DKSLWEDWQY FARNCSVWGM
KNNGDLENPN SVNCLQFPEF IPFSHGNVTF DLLTSGQKHR PGDYDFYNSS LLQEFMTATQ
IRLYFRGLFY PAWHTVDSRH RYYAVDEITI IGRCQCHGHA ETCDRTRRPY RCLCSPHSFT
EGPQCGRCSP LYNDKPFRSG NKVHAFNCKP CQCHGHASSC HYDASMDPFP LEYNRGGGGV
CDDCQHHTTG RNCESCQDYF YRPIGADPAD PEVCKHCDCN RDGTRNGSLL CDLVGDQCDC
KRRVSGRRCF RCHIGFYGLQ ALDPDCCRPC DCNPSGTVDG DITCHHNSGQ CSCKANVIGL
RCDRCSFGFK FLRSLNADGC EPCHCNLHGS VNQLCDPLSG QCVCKKEAKG LRCDVCRENF
YGLPWSACEV CDCNRAGTQA GTVCDAETGQ CVCKPSVGGR RCSECKEGYF NLRQNDSHLC
LPCNCEKTGT VNGSLLCDKS TGQCPCKLGV TGLRCHQCKP HRFNLTMDNP QGCQACDCDS
LGTLLGSMCD PVSGQCLCLP HRQERRCVQC QPGCYSSPSN ATGCLPCLCH TVATKNCICN
SVTGHCYCPD PSTTGLSWHQ CQDRYFRFDP LTGRCRPCHC HVAGASNGTC DAVTGQCFCK
EFVTGSKCDT CVPGASHLDV NNLLACSKTP SQQPPPRGRV QSSSAINLSW SPPDFPNAHW
LTYTLFRDDS EIYTTDDQHP YYTQYFLDTS LSPHTAYSYY IETSNVHSST RSIPVIYKTK
PEGSEGHLNL THIIPVASDS ITLVWTGLSN HSGPIEKYVL SCTPVDHTEP CVSYEGPETS
ATIRNLVPFT QYCFSVQGCT NGSCLYSSPI TVTTAQAPPQ RQEPPTVWKI SPTELKVEWS
RPVDSNGVII RYELYMKRWP STEESLVFES HGWFHSHPAS PSANQSENVL QDPQVSTVLS
GLDPHTEYAF RVLAVNMAGS VSSAWASERT GESAPVFMAA PSVSPLSPYS LSVSWEKPAE
NFTRGEIIGY KISMVSERSP QRDVPVMCSK LVHFAESQDQ SYIVQRLKPY RTYSFTVSLC
ASVGCVTSAL GEGQTLAAAP AQLRSPMVTG VTSTTVHIRW LPPAEVNGPP PLYRLERRES
FLPAATAART KGTRFMGDGY CRFPRTAHPD FIGIKASFWT RVPEGLILLA LHPDNQEEYF
ALQLKSGRPY FLYNPQGSLV EVTTADDHSQ QYSDGQWHEI TAIRHQSFGQ ITLDEQYTDS
SASLNGSSVT GGYTRLFVGG LPQGHTILQK RPVRRGFVGC LKDVSILKGS SPSGTWLPLD
WQSSEEQVNV HHSWEGCPTD LEEGVQFLGA GFLELRSDTF HAAKDFEISL KFQTDQLNGL
LLFIHNTEGL DFLAMELKSG LLSFQLNSSR ILTRVEVRLG RTHCDGKWNR VTIRREGSMV
SVGVNELTKS TSRAGDQPPL LTSPVYLGGI PQELQASYRH LTLEQGFRGC VKEVAFTRGA
VVNLASVSSR AVRVNQDGCL SSDSTVNCGG NDSILVYRGS RQSVYESGLQ PFTEYLYRVT
ASHKGGSVSS DWSRGRTLGS APHSVPTPSR AQSINGYSVE VAWNEPAMVK GVLEKYILKA
YSEDSAQPHM PSASTEFNNT DIRTGILTGL HPFHSYAVTL TACSRAGCTE SSRALSISTP
QEAPQEVQAP VAEALPNSLS FFWSPPRQAN GIITQYSLYM DGRLVYTGKG QNYTVTDLRV
FTAYEITVGA CTRAGCTNSS RVILHTAQLP PERVDPPVLA ILDSRTVHIQ WKQPRQLNGI
LERYILYTLN PTHNSTVWDV VYNSTENLQT HLLYHLSPGC LYLIKLGACT GGGCTTSEPS
QALMDETVPE GVPAPRAHSH SPDSFNISWT EPGHPNGVIT TYELYLDGTL IHNSSELSCH
AYGFDPGSLH TFQVQACTAK GCALGPLVEN RTLEAPPEGT VNLFVKPEGS REAAVRWDAP
PHPNGRLTYS VLITGNFYAD QAGDNYTLLS STKTVHSSKG DRLWVLVDRL VPCSNYTVQV
NASNSQGSVL SDRVSVEMPP GAPDGLLSPR LAAATPTSLQ VVWSTPARNN APGSPRYQLQ
MRPDPSTRGL LELFPIPSAL LSYEVTGLQP FTVYEFRLVA TNGFGSAYSD WTPLMTTEDK
PGPMDAPVLN VKAGMMSVAW RKPTECNGAI THYNIYQHGR LYLTVSGGVT NCTVVHLRPH
TAYQFQIEAC SSKGCSMSPA SETVWTLPGT PEGIPGPELL PYTPTKIIVS WQPPTHLDGL
VENITIERRV KEQEEVRSLV ILPRSQAVRF IDNDPALRPW THYEYRVLGS TLNGGTNSSA
WVEVTTRPSR PSGVQPPTVH VLGPDAVEVT WKAPLIRNGD IVSYEIRMPD PLIEITNVTS
FVLSHLVKHL IPFTNYSVSI VACSGGHGYL GGCTESLPTF ATTHPALPQE LTPLSISLLG
QSYVGISWQP PSKPNGPNLR YELLRRKIQQ PLASNPPEDL NLWHNIYSGT RRFYEDKGLS
RFTTYEYKLF VHNSLGFTPS QEVTVTTLAG SPERGATVTA SILNHTAIDV RWKRPTFQDL
QGDVEYYTLF WSSGTSVESL KIFPDVDFHV IGHLAPNVEY QVFLLVFNGV HAINSTVVRV
TTWEEEPRGM RPPEVVIINS TAVRVIWTSP SNPNAVITES SVYANNELHK AGAGAPGSFT
LEDLSPFTIY DIQVEVCTKD ACVKSSGTQV STAEDTPSGI SIPIIRDITS RSLQIDWTAP
GNPNGIILGY DVLRKTWRLC SETQKLTDKP RDELCKAVKC QYPGNVCGHT CYSPGTKVCC
DGLLYDPQPG YSCCEEKYIA LLPNSTGVCC GGRQREAQPD HQCCSGHYIR ILPGEICCPD
ERHNRVSVGF GDACCGTMPY ATSGSQVCCA GKLQDGYRRQ CCGGEMVSQD FKCCGGGEEG
MVYSSLPGML CCGQDYVNMS DTICCSASSG DSKAHVRGSD PMPVRCCHTE LIPESQQCCD
GVGYNPVKYV CSDEISAGMA TEETRVCATV CPATMRATAH CGQCDFNATT HICTVSRGPL
NPIGKETAEG LCSTAEEIVH SGDENTRSFI DTDLEPSTVY EYRVSVWNSY GRGFSQSVRA
STREDVPQGV TAPRWARTGN HEDVIFLTWK EPTQSNGPIT HYILLRDGRE RFQGAALSFT
DTQGIQPLQE YSYQLKACTA AGCADSCKVV ATATRGVLES VPPPNITAQS PETLHLSWSV
PEKRNDAIKE YQLWLDGKGL IYTDTNDRRQ HTVTGLQPHT NYSFTLSACT SVGCTSSEPS
VGQTLQAAPQ GVWVTPRHII INSTTVELYW NPPERPNGVI SQYRLRRNGS LLLVGGRDDQ
SFTDKNLEPN SRYIYTLEAR TGGGSSLSEE YLVQMPMWTP EDVHPPCNVT VLGSDSIFVA
WPAPGILLPK IPVEYSILLS GGNMMLLTFS VGLRQSAYLK NLAPFTQYEI RIQACQEGCG
VSPGTHVRTL EAAPVGLMPP LLKALGSHCI EVKWTPPTRP NGIITSYVIH RRPADTEEES
LLFVWSEGAL EFTDDTDTLR PFTLYEYRVR AWNSKGVVDS PWSSVQTLEA PPQDLPAPWV
QVTSAHSVLL NWTEPEAPNG LISQYHVIYQ ERPDEAAPGS STVHAFTVKG SSRQAHLFGL
EPFTTYHIGV AAVNRAGKVS SPWTLIKTLE SAPSGLMNFT AEQREGGRAL LLQWSEPVRT
NGVIKAYNVF SDGLPEYSGL GRQFLFRRLA PFTLYILTLE ACTAAGCAHS VPQTLWTEEA
PPDSQMAPTI QSVEPTSVRL HWSQPANPNG KIIRYEVIRR RLQGEDWGNR TVQADENTVF
TEYNTEGNGW VCTDTGLQPW GLYSYRICTW NSAGHTCSSW SVVRTSQAPP DGLSPPEVSY
VSTSPLQLLI SWFAPRHTNG VIQSYRLQRN GVFAAASFNS STFSYTDGQL LPFTTYSYAV
LACTGGGCCT SEPTNITTPE ASPAGVSPPV LWAIGAHQIN VSWSPPSVPN GKIAKYLLHC
DGEEHLAGQD LSLLLSNLRP FTQYNVSLVA CTKGGCTASR VASAWTMEAP PEDMDPPTLH
VMGPESIEIT WAPPRNPHGQ IRSYELRRDG AIVYIGLETR YHDFILTPGV QYGYTVTATN
SRGSVLSPLV KGQTSPSAPS GLQPPKLRAG EALELLVNWN PPVRTNGKIT NYTLFIRELL
EGEIRTMCIN TTHSSFGTRS LAVKHLKPFH RYEVRVQACT ALGCTSSEWT PTQTSEIPPL
LQPAPHLEVQ TAAGGFQPIV AVWWAGPLQP HGKIVRFELY RRQTASWPGT SSPLLIYNGS
LSSFTDRELL PFTEYEYQVW AVNSAGKVAS NWTWCRTGPA PPEGLKAPTF HTVSSTQAVV
NISAPSKPNG NISLFRVFSN SSGTHVMLSE GMATQQTLHD LRPFTTYAIG VEACTCFNCC
SRGPTAELRT HPAPPSGLSP PQVQTLGSRM ASFQWAPPQL PNGVIHSYEL QLHRACPPDS
APHCPPSPTE RKYWGPGHRA SLAGLQPNTA YGVQVVAHNE AGSTASGWTS FRTKKEMPQY
QALFSVDSNA STVWVDWSGT FVLNGQLKEY VVTDGGRRVY SGLDTTLYIP RTVDKTFFFQ
VTCTTDIGSV KTPLVQYDAT TGFGLVLTTP GGKKGAGTKS TEFYTDTRLP RSGTPVSIRS
SQSVSVLRIP SQSQLSHAYS QGSLHRSVSQ LMDSPDKKAL TEDSLWETIM GHSSGLCVDE
EELMNAIKGF SSVTKEHTAF TDTHL
