ID G3V8G9_RAT Unreviewed; 2471 AA.
AC G3V8G9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Notch receptor 2 {ECO:0000313|Ensembl:ENSRNOP00000025718.2};
GN Name=Notch2 {ECO:0000313|Ensembl:ENSRNOP00000025718.2,
GN ECO:0000313|RGD:3188};
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 {ECO:0000313|Ensembl:ENSRNOP00000025718.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000025718.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000025718.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
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 [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000025718.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000025718.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NOTCH family.
CC {ECO:0000256|ARBA:ARBA00005847}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; NP_077334.2; NM_024358.2.
DR SMR; G3V8G9; -.
DR Ensembl; ENSRNOT00000025718.5; ENSRNOP00000025718.2; ENSRNOG00000018835.7.
DR GeneID; 29492; -.
DR KEGG; rno:29492; -.
DR CTD; 4853; -.
DR RGD; 3188; Notch2.
DR GeneTree; ENSGT00940000155030; -.
DR HOGENOM; CLU_000576_1_1_1; -.
DR OMA; AHMSEPP; -.
DR OrthoDB; 5473534at2759; -.
DR TreeFam; TF351641; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018835; Expressed in spleen and 20 other cell types or tissues.
DR ExpressionAtlas; G3V8G9; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0060413; P:atrial septum morphogenesis; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0071228; P:cellular response to tumor cell; IEA:Ensembl.
DR GO; GO:1990705; P:cholangiocyte proliferation; IEA:Ensembl.
DR GO; GO:0061073; P:ciliary body morphogenesis; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0072104; P:glomerular capillary formation; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0035622; P:intrahepatic bile duct development; IEA:Ensembl.
DR GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0072015; P:podocyte development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0072014; P:proximal tubule development; IEA:Ensembl.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IEA:Ensembl.
DR GO; GO:2001204; P:regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 26.
DR CDD; cd21703; JMTM_Notch2; 1.
DR Gene3D; 3.30.300.320; -; 1.
DR Gene3D; 3.30.70.3310; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 35.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR008297; Notch.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR022336; Notch_2.
DR InterPro; IPR024600; Notch_C.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF1; PROTEIN CRUMBS HOMOLOG 1; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00008; EGF; 19.
DR Pfam; PF07645; EGF_CA; 5.
DR Pfam; PF12661; hEGF; 7.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PIRSF; PIRSF002279; Notch; 1.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR PRINTS; PR01983; NOTCH.
DR PRINTS; PR01985; NOTCH2.
DR SMART; SM00248; ANK; 6.
DR SMART; SM01334; DUF3454; 1.
DR SMART; SM00181; EGF; 35.
DR SMART; SM00179; EGF_CA; 34.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 15.
DR SUPFAM; SSF57184; Growth factor receptor domain; 6.
DR SUPFAM; SSF90193; Notch domain; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 22.
DR PROSITE; PS00022; EGF_1; 34.
DR PROSITE; PS01186; EGF_2; 27.
DR PROSITE; PS50026; EGF_3; 35.
DR PROSITE; PS01187; EGF_CA; 9.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REPEAT 1876..1908
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1943..1975
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1976..2008
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 2009..2041
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DISULFID 53..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 73..90
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 92..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 133..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 170..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 248..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 286..295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 326..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 364..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 384..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 403..412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 444..453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 482..491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 520..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 558..567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 574..584
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 595..604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 633..642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 649..659
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 670..679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 708..717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 724..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 745..754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 783..792
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 821..830
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 842..859
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 861..870
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 899..908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 937..946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 975..984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1013..1022
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1051..1060
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1089..1098
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1137..1146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1175..1184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1213..1222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1252..1261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1273..1290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1292..1301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1333..1342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1383..1400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1402..1411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2471 AA; 265134 MW; 31C3CBF3F0BB3414 CRC64;
MPALRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGY CRCPEGFLGE
YCQHRDPCEK NRCQNGGTCV TQAMLGKATC RCAPGFTGED CQYSTSHPCF VSRPCQNGGT
CHMLSWDTYE CTCQVGFTGK QCQWTDVCLS HPCENGSTCS SVANQFSCRC PAGITGQKCD
ADINECDIPG RCQHGGTCLN LPGSYRCQCP QGFTGQHCDS PYVPCAPSPC VNGGTCRQTG
DFTSECHCLP GFEGSNCERN IDDCPNHKCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD
ECLLQPNACQ NGGTCTNRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG STCIDRVASF
SCLCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI CTCPQGYKGA DCTEDVDECA
MANSNPCEHA GKCVNTDGAF HCECLKGYAG PRCEMDINEC HSDPCQNDAT CLDKIGGFTC
LCMPGFKGVH CELEVNECQS NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP
CLNGAKCIDH PNGYECQCAT GFTGTLCDEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGL NCEINFDDCA SNPCLHGACV
DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCIND VNGFRCMCPE GPHHPSCYSQ
VNECLSSPCI HGNCTGGLSG YKCLCDAGWV GINCEVDKNE CLSNPCQNGG TCNNLVNGYR
CTCKKGFKGY NCQVNIDECA SNPCLNQGTC LDDVSGYTCH CMLPYTGKNC QTVLAPCSPN
PCENAAVCKE APNFESFTCL CAPGWQGQRC TVDVDECVSK PCMNNGICHN TQGSYMCECP
PGFSGMDCEE DINDCLANPC QNGGSCVDKV NTFSCLCLPG FVGDKCQTDM NECLSEPCKN
GGTCSDYVNS YTCTCPAGFH GVHCENNIDE CTESSCFNGG TCVDGINSFS CLCPVGFTGP
FCLHDINECS SNPCLNSGTC VDGLGTYRCT CPLGYTGKNC QTLVNLCSPS PCKNKGTCAQ
EKARPRCLCP PGWDGAYCDV LNVSCKAAAL QKGVPVEHLC QHSGICINAG NTHHCQCPLG
YTGSYCEEQL DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA GGPHCLNGGQ CVDRIGGYSC RCLPGFAGER
CEGDINECLS NPCSSEGSLD CIQLKNNYQC VCRSAFTGRH CETFLDVCPQ KPCLNGGTCA
VASNVPDGFI CRCPPGFSGA RCQSSCGQVK CRRGEQCVHT ASGPHCFCLN RKDCESGCAS
NPCQHGGTCY PQRQPPYYSC RCSPPFWGSH CESYTAPTST PPATCLSQYC ADKARDGICD
EACNSHACQW DGGDCSLTME DPWANCTSSL RCWEYINNQC DELCNTAECL FDNFECQRNS
KTCKYDKYCA DHFKDNHCDK GCNNEECGWD GLDCAADQPE NLAEGILVIV VLLPPEQLLQ
DSRSFLRALG TLLHTNLRIK QDSQGALMVY PYYGEKSAAM KKQKVARRSL PDEQEQEIIG
SKVFLEIDNR QCVQDSDQCF KNTDAAAALL ASHAIQGTLS YPLVSVVSES EDPRNTPLLY
LLAVAVVIIL FLILLGVIMA KRKRKHGFLW LPEGFTLRRD SSNHKRREPV GQDAVGLKNL
SVQVSEANLI GSTTSEHWGD DEGPQPKKAK AEDDEALLSE DDPVDRRPWT QQHLEAADIR
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED AEDSSANIIT
DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG ADANAQDNMG RCPLHAAVAA
DAQGVFQILI RNRVTDLDAR MNDGTTPLIL AARLAVEGMV AELINCQADV NAVDDHGKSA
LHWAAAVNNV EATLLLLKNG ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD
HMDRLPRDVA RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVLCGPNRS FLSLKHTPMG
KKARRPNTKS TMPTSLPNLA KEAKDVKGSR RKKCLNEKVQ LSESSVTLSP VDSLESPHTY
VSDATSSPMI TSPGILQASP TPLLAAAPAA PVHAQHALSF SNLHEMQPLA PGASTVLPSV
SQLLSHHHIV PPGSGSAGSL GRLHSVPVPS DWMNRVEMSE TQYSEMFGMV LAPAEGTHPG
MAAPQSRAPE GKPIPTQREP LPPIVTFQLI PKGSLAQAAG APQTQSGCPP AVAGPLPSMY
QIPEMARLPS VAFPPTMMPQ QEGQVAQTIV PTYHPFPASV GKYPTPPSQH SYASSNAAER
TPNHGGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGGGG GQRGPGTHMS
EPPHSNMQVY A
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