ID A6KTE6_RAT Unreviewed; 1961 AA. AC A6KTE6; Q6MG89; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 27-MAR-2024, entry version 5. DE SubName: Full=Notch homolog 4, [Drosophila] {ECO:0000313|EMBL:CAE83957.1}; DE SubName: Full=Notch receptor 4 {ECO:0000313|Ensembl:ENSRNOP00000000513.3}; GN Name=Notch4 {ECO:0000313|EMBL:CAE83957.1, GN ECO:0000313|Ensembl:ENSRNOP00000000513.3, ECO:0000313|RGD:1303282}; 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|EMBL:CAE83957.1}; RN [1] {ECO:0000313|EMBL:CAE83957.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83957.1}; RA Boehm S., Borzym K., Gelling S., Gimmel V., Heitmann K., Kosiura A., RA Lang N., Lehrack S., Thiel J., Sontag M., Hurt P., Himmelbauer H., RA Sudbrak R., Reinhardt R.; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAE83957.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83957.1}; RX PubMed=15060004; DOI=10.1101/gr.1987704; RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.; RT "The genomic sequence and comparative analysis of the rat major RT histocompatibility complex."; RL Genome Res. 14:631-639(2004). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000000513.3, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000513.3, 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 [4] {ECO:0000313|Ensembl:ENSRNOP00000000513.3} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000513.3}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX883044; CAE83957.1; -; Genomic_DNA. DR RefSeq; NP_001002827.1; NM_001002827.1. DR IntAct; A6KTE6; 3. DR STRING; 10116.ENSRNOP00000000513; -. DR PaxDb; 10116-ENSRNOP00000000513; -. DR Ensembl; ENSRNOT00000000513.5; ENSRNOP00000000513.3; ENSRNOG00000000442.5. DR GeneID; 406162; -. DR KEGG; rno:406162; -. DR UCSC; RGD:1303282; rat. DR AGR; RGD:1303282; -. DR CTD; 4855; -. DR RGD; 1303282; Notch4. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000163287; -. DR HOGENOM; CLU_000576_0_0_1; -. DR OMA; ACPQVHT; -. DR OrthoDB; 5473534at2759; -. DR TreeFam; TF351641; -. DR Reactome; R-RNO-1912420; Pre-NOTCH Processing in Golgi. DR Reactome; R-RNO-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus. DR Reactome; R-RNO-9604323; Negative regulation of NOTCH4 signaling. DR PRO; PR:Q6MG89; -. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000000442; Expressed in heart and 18 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0005112; F:Notch binding; ISO:RGD. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD. DR GO; GO:0045446; P:endothelial cell differentiation; IDA:RGD. DR GO; GO:0001886; P:endothelial cell morphogenesis; IDA:RGD. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD. DR GO; GO:0001554; P:luteolysis; IEP:RGD. DR GO; GO:0030879; P:mammary gland development; ISO:RGD. DR GO; GO:0001763; P:morphogenesis of a branching structure; ISO:RGD. DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; ISO:RGD. DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD. DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:RGD. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD. DR GO; GO:1903849; P:positive regulation of aorta morphogenesis; ISO:RGD. DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISO:RGD. DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD. DR GO; GO:0070613; P:regulation of protein processing; ISO:RGD. DR GO; GO:0001944; P:vasculature development; ISO:RGD. DR GO; GO:0048845; P:venous blood vessel morphogenesis; ISO:RGD. DR CDD; cd00054; EGF_CA; 17. DR CDD; cd21705; JMTM_Notch4; 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; 26. 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; IPR022355; Notch_4. DR InterPro; IPR000800; Notch_dom. DR InterPro; IPR010660; Notch_NOD_dom. DR InterPro; IPR011656; Notch_NODP_dom. DR PANTHER; PTHR24044:SF489; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 4; 1. DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF00008; EGF; 16. DR Pfam; PF07645; EGF_CA; 3. DR Pfam; PF12661; hEGF; 3. DR Pfam; PF06816; NOD; 1. DR Pfam; PF07684; NODP; 1. DR Pfam; PF00066; Notch; 3. DR PIRSF; PIRSF002279; Notch; 3. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR01452; LNOTCHREPEAT. DR PRINTS; PR01983; NOTCH. DR PRINTS; PR01987; NOTCH4. DR SMART; SM00248; ANK; 5. DR SMART; SM00181; EGF; 28. DR SMART; SM00179; EGF_CA; 21. 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; 16. DR SUPFAM; SSF57184; Growth factor receptor domain; 3. DR SUPFAM; SSF90193; Notch domain; 2. DR PROSITE; PS50297; ANK_REP_REGION; 5. DR PROSITE; PS50088; ANK_REPEAT; 5. DR PROSITE; PS00010; ASX_HYDROXYL; 10. DR PROSITE; PS00022; EGF_1; 27. DR PROSITE; PS01186; EGF_2; 20. DR PROSITE; PS50026; EGF_3; 27. DR PROSITE; PS01187; EGF_CA; 3. DR PROSITE; PS50258; LNR; 3. PE 3: Inferred from homology; KW Activator {ECO:0000256|ARBA:ARBA00023159}; KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE- KW ProRule:PRU00023}; Calcium {ECO:0000256|PIRSR:PIRSR002279-1}; KW 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, KW ECO:0000256|PIRSR:PIRSR002279-2}; 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR002279-1}; 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, ECO:0000256|SAM:SignalP}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..1961 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5041156546" FT TRANSMEM 1403..1421 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1441..1464 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 21..60 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 61..112 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 115..152 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 153..189 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 191..229 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 231..271 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 273..309 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 311..350 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 352..388 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 389..427 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 429..470 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 472..508 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 510..546 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 548..584 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 586..622 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 688..724 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 726..762 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 764..800 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 803..839 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 841..877 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 889..924 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 926..962 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 964..1000 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1002..1040 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1042..1081 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1083..1122 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1126..1167 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1166..1209 FT /note="LNR" FT /evidence="ECO:0000259|PROSITE:PS50258" FT DOMAIN 1210..1241 FT /note="LNR" FT /evidence="ECO:0000259|PROSITE:PS50258" FT DOMAIN 1247..1287 FT /note="LNR" FT /evidence="ECO:0000259|PROSITE:PS50258" FT REPEAT 1625..1657 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 1658..1679 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 1692..1724 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 1725..1757 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 1758..1790 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REGION 1342..1371 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1874..1904 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1922..1961 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1353..1370 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1890..1904 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 452 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 455 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 472 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 475 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 489 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 513 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT BINDING 527 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR002279-1" FT DISULFID 50..59 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 102..111 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 142..151 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 179..188 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 219..228 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 261..270 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 299..308 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 340..349 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 378..387 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 398..415 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 417..426 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 433..449 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 443..458 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 460..469 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2, FT ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 476..487 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 481..496 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 498..507 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2, FT ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 514..525 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 519..534 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2" FT DISULFID 536..545 FT /evidence="ECO:0000256|PIRSR:PIRSR002279-2, FT ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 574..583 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 612..621 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 714..723 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 752..761 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 790..799 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 829..838 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 867..876 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 914..923 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 952..961 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 990..999 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 1011..1028 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 1030..1039 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 1071..1080 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 1112..1121 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 1157..1166 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" SQ SEQUENCE 1961 AA; 206076 MW; 5B1034E29EE07A3C CRC64; MQRQWLLLLL LPLSFPVILT RELLCGGSPE PCANGGTCLR LSQGQGTCQC APGFLGETCQ FPDPCWDTQL CENGGSCQAL LPTAPSSHSP TSPLTPHFSC TCPSGFTGDR CQSPLEELCP PSFCSNGGHC SVQVSGRPQC SCEPGWTGEQ CQLRDFCSAN PCANGGVCLA TYPQIQCRCP TGFEGHICER DVNECFLEPG PCPRGTSCHN TLGSFQCLCP VGQEGPQCKL RKGACLPGTC LNGGTCQLVP EGDTTFHLCL CPPGFTGLNC EMNPDDCVRN QCQNGATCQD GLGTYTCLCP KTWKGWDCSE DIDECEAQGP PRCRNGGTCQ NSAGGFHCVC VSGWGGEGCD ENLDDCAAAT CALGSTCIDR VGSFSCLCPP GRTGLLCHLE DMCLRQPCHV NAQCSTNPLT GSTLCICQPG YSGPTCHQDL DECQMAQQGP SPCEHGGSCI NTPGSFNCLC LPGYTGSRCE ADHNECLSQP CHPGSTCLDL LATFQCLCPP GLEGRLCEVE INECASNPCL NQAACHDQLN GFLCLCLPGF TGARCEKDMD ECSSAPCANG GHCQDQPGAF HCECLPGFEG PRCETEADEC RSDPCPVGAS CLDLPGAFLC LCRPGFTGQL CEVPLCSPIL CQPGQQCQDQ EHRAPCLCPD GSPGCVPAED DCPCHHGHCQ RSLCVCNEGW TGPECETELG GCLSTPCAHG GTCHPQPSGY NCSCLAGYTG LTCSEEITAC HSGPCLNGGS CSIHPEGYSC TCPPSHTGPH CQTAVDHCAS ASCLNGGTCM SKPGTFFCHC ATGFQGLHCE KKIHPSCADN PCRNKATCQD TPRGARCLCS PGYTGSSCQT LIDLCARKPC PHTARCLQSG PSFHCLCHQG WTGSLCDLPL SCQAAAMSQG VEISNLCQNG GLCIDTGSSY FCRCPPGFEG KLCQDTVNPC TSKPCLHGAT CVPQPNGYVC QCAPGYEGQN CSKVHDACQS GPCHNHGTCT PRPGGFHCAC PPGFVGLRCE GDVDECLDRP CHPSGTASCH SLANAFYCQC LPGHTGQRCE VEMDLCQSQP CSNGGSCEVT TGPPPGFTCR CPEGFEGPTC SRKAPACGNH HCHNGGLCLP SPKPGSPPLC ACLSGFGGPD CLTPPAPPGC GPPSPCMHNG SCTETPGLGN PGFQCTCPPD SPGPRCQRPG ANGCEGRGGD GACDAGCSGP GGDWDGGDCS LGVPDPWKGC PPHSQCWLLF RDGRCHPQCD SEECLFDGYD CEIPPTCTPA YDQYCRDHFH NGHCEKGCNN AQCGWDGGDC RPEGDDSEGG PSLALLVVLS PPALDQQLLA LARVLSLTLR VGLWVRKDSE GRNMVFPYPG TRAKEELSGT RDSSSWERQA PHTQTPGKET ESLGAGFVVV MGVDLSRCGP EHPASRCPRD SGLLLRFLAA MAAVGALEPL LPGPLLAAHP QAGTGSPATR LPWPILCSPV VGVLLLALGA LLVLQLIRRR RREHGALWLP PGFIRRPQTQ QAPHRRRPPL GEDNIGLKAL KPEAEVDEDG VVMCSGPEEG EAEKTASASR CQLWPLRSGC EGLPQAVMLT PPQECESELP DSDTCGPDGV TPLMSAVFCG GVQSTTVQRL GLGNPEPWEP LLDRGACPQA HTVGTGETPL HLAARFSRPT AARRLLEAGA NPNQPDRAGR TPLHTAVAAD AREVCQLLLA SRQTAVDART DDGTTPLMLA ARLAVEDLVE ELIAARADVG ARDKRGKTAL HWAAAVNNAR AARCLLQTGA DKDAQDSREQ TPLFLAAREG AVEVAQLLLE IGAARGLRDQ AGLAPADVAR QRSHWDLLTL LEGAGPITQE ARSHARNTPG GGAAPRCRTL SAGARPRGGG ACLQARTWSV DLGARRGAVY ARCRSRSGGS GGPSMRGRRL SADSRGRRGA RVSQDDWPRD WVALEACGSA CSAPIPPPSL TPSPERGSPQ VSWGLPVHQE VPLNSGGRNQ N //