NOTC3_RAT
ID NOTC3_RAT Reviewed; 2319 AA.
AC Q9R172;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 25-MAY-2022, entry version 177.
DE RecName: Full=Neurogenic locus notch homolog protein 3;
DE Short=Notch 3;
DE Contains:
DE RecName: Full=Notch 3 extracellular truncation;
DE Contains:
DE RecName: Full=Notch 3 intracellular domain;
DE Flags: Precursor;
GN Name=Notch3;
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].
RA Haritunians T., Boulter J., Weinmaster G., Schanen N.C.;
RT "Rattus norvegicus mRNA for Notch 3.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=11182080; DOI=10.1016/s0896-6273(01)00179-9;
RA Tanigaki K., Nogaki F., Takahashi J., Tashiro K., Kurooka H., Honjo T.;
RT "Notch1 and Notch3 instructively restrict bFGF-responsive multipotent
RT neural progenitor cells to an astroglial fate.";
RL Neuron 29:45-55(2001).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11438922; DOI=10.1002/cne.1059.abs;
RA Irvin D.K., Zurcher S.D., Nguyen T., Weinmaster G., Kornblum H.I.;
RT "Expression patterns of Notch1, Notch2, and Notch3 suggest multiple
RT functional roles for the Notch-DSL signaling system during brain
RT development.";
RL J. Comp. Neurol. 436:167-181(2001).
CC -!- FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1,
CC Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand
CC activation through the released notch intracellular domain (NICD) it
CC forms a transcriptional activator complex with RBPJ/RBPSUH and
CC activates genes of the enhancer of split locus. Affects the
CC implementation of differentiation, proliferation and apoptotic programs
CC (By similarity). Acts instructively to control the cell fate
CC determination of CNS multipotent progenitor cells, resulting in
CC astroglial induction and neuron/oligodendrocyte suppression.
CC {ECO:0000250, ECO:0000269|PubMed:11182080}.
CC -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and a N-terminal
CC fragment N(EC) which are probably linked by disulfide bonds. Interacts
CC with MAML1, MAML2 and MAML3 which act as transcriptional coactivators
CC for NOTCH3. Interacts with PSMA1 (By similarity). Interacts with HIF1AN
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM47};
CC Single-pass type I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Notch 3 intracellular domain]: Nucleus.
CC Note=Following proteolytical processing NICD is translocated to the
CC nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in postnatal central nervous system (CNS)
CC germinal zones and, in early postnatal life, within numerous cells
CC throughout the CNS. It is more highly localized to ventricular germinal
CC zones. {ECO:0000269|PubMed:11438922}.
CC -!- DOMAIN: The EGF-like domains 10 and 11 are required for binding the
CC ligands JAG1 and DLL1. {ECO:0000250|UniProtKB:Q9UM47}.
CC -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form which
CC is proteolytically cleaved by a furin-like convertase in the trans-
CC Golgi network before it reaches the plasma membrane to yield an active,
CC ligand-accessible form. Cleavage results in a C-terminal fragment N(TM)
CC and a N-terminal fragment N(EC). Following ligand binding, it is
CC cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-
CC associated intermediate fragment called notch extracellular truncation
CC (NEXT). This fragment is then cleaved by presenilin dependent gamma-
CC secretase to release a notch-derived peptide containing the
CC intracellular domain (NICD) from the membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q61982}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Hydroxylated by HIF1AN. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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DR EMBL; AF164486; AAD46653.2; -; mRNA.
DR RefSeq; NP_064472.2; NM_020087.2.
DR AlphaFoldDB; Q9R172; -.
DR SMR; Q9R172; -.
DR STRING; 10116.ENSRNOP00000037570; -.
DR GlyGen; Q9R172; 3 sites.
DR PaxDb; Q9R172; -.
DR GeneID; 56761; -.
DR KEGG; rno:56761; -.
DR UCSC; RGD:620761; rat.
DR CTD; 4854; -.
DR RGD; 620761; Notch3.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q9R172; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; Q9R172; -.
DR Reactome; R-RNO-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-RNO-9017802; Noncanonical activation of NOTCH3.
DR PRO; PR:Q9R172; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0072104; P:glomerular capillary formation; ISO:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
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; IPR022331; Notch_3.
DR InterPro; IPR024600; Notch_C.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00008; EGF; 19.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF12661; hEGF; 4.
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; PR01986; NOTCH3.
DR SMART; SM00248; ANK; 6.
DR SMART; SM01334; DUF3454; 1.
DR SMART; SM00181; EGF; 34.
DR SMART; SM00179; EGF_CA; 30.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57184; SSF57184; 5.
DR SUPFAM; SSF90193; SSF90193; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 18.
DR PROSITE; PS00022; EGF_1; 33.
DR PROSITE; PS01186; EGF_2; 26.
DR PROSITE; PS50026; EGF_3; 34.
DR PROSITE; PS01187; EGF_CA; 16.
DR PROSITE; PS50258; LNR; 3.
PE 2: Evidence at transcript level;
KW Activator; ANK repeat; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Methylation; Notch signaling pathway; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..2319
FT /note="Neurogenic locus notch homolog protein 3"
FT /id="PRO_0000007698"
FT CHAIN 1631..2319
FT /note="Notch 3 extracellular truncation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007699"
FT CHAIN 1664..2319
FT /note="Notch 3 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007700"
FT TOPO_DOM 41..1645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1646..1666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1667..2319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..79
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 80..120
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 121..158
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 160..197
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 199..236
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 238..274
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 276..314
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 316..352
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 353..391
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 393..431
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 433..469
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 471..507
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 509..545
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 547..582
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 584..620
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 622..657
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 659..695
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 697..732
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 736..772
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 773..810
FT /note="EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 812..849
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 851..887
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 889..924
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 926..962
FT /note="EGF-like 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 964..1000
FT /note="EGF-like 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1002..1036
FT /note="EGF-like 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1038..1084
FT /note="EGF-like 27"
FT /evidence="ECO:0000305"
FT DOMAIN 1086..1122
FT /note="EGF-like 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1124..1160
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1162..1205
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1207..1246
FT /note="EGF-like 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1248..1289
FT /note="EGF-like 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1291..1327
FT /note="EGF-like 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1337..1375
FT /note="EGF-like 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1389..1429
FT /note="LNR 1"
FT REPEAT 1430..1467
FT /note="LNR 2"
FT REPEAT 1469..1507
FT /note="LNR 3"
FT REPEAT 1840..1869
FT /note="ANK 1"
FT REPEAT 1873..1903
FT /note="ANK 2"
FT REPEAT 1907..1936
FT /note="ANK 3"
FT REPEAT 1940..1969
FT /note="ANK 4"
FT REPEAT 1973..2002
FT /note="ANK 5"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2197..2319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2295..2310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1573..1574
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250"
FT MOD_RES 2175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM47"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..56
FT /evidence="ECO:0000250"
FT DISULFID 50..67
FT /evidence="ECO:0000250"
FT DISULFID 69..78
FT /evidence="ECO:0000250"
FT DISULFID 84..95
FT /evidence="ECO:0000250"
FT DISULFID 89..108
FT /evidence="ECO:0000250"
FT DISULFID 110..119
FT /evidence="ECO:0000250"
FT DISULFID 125..136
FT /evidence="ECO:0000250"
FT DISULFID 130..146
FT /evidence="ECO:0000250"
FT DISULFID 148..157
FT /evidence="ECO:0000250"
FT DISULFID 164..176
FT /evidence="ECO:0000250"
FT DISULFID 170..185
FT /evidence="ECO:0000250"
FT DISULFID 187..196
FT /evidence="ECO:0000250"
FT DISULFID 203..214
FT /evidence="ECO:0000250"
FT DISULFID 208..224
FT /evidence="ECO:0000250"
FT DISULFID 226..235
FT /evidence="ECO:0000250"
FT DISULFID 242..253
FT /evidence="ECO:0000250"
FT DISULFID 247..262
FT /evidence="ECO:0000250"
FT DISULFID 264..273
FT /evidence="ECO:0000250"
FT DISULFID 280..293
FT /evidence="ECO:0000250"
FT DISULFID 287..302
FT /evidence="ECO:0000250"
FT DISULFID 304..313
FT /evidence="ECO:0000250"
FT DISULFID 320..331
FT /evidence="ECO:0000250"
FT DISULFID 325..340
FT /evidence="ECO:0000250"
FT DISULFID 342..351
FT /evidence="ECO:0000250"
FT DISULFID 357..368
FT /evidence="ECO:0000250"
FT DISULFID 362..379
FT /evidence="ECO:0000250"
FT DISULFID 381..390
FT /evidence="ECO:0000250"
FT DISULFID 397..410
FT /evidence="ECO:0000250"
FT DISULFID 404..419
FT /evidence="ECO:0000250"
FT DISULFID 421..430
FT /evidence="ECO:0000250"
FT DISULFID 437..448
FT /evidence="ECO:0000250"
FT DISULFID 442..457
FT /evidence="ECO:0000250"
FT DISULFID 459..468
FT /evidence="ECO:0000250"
FT DISULFID 475..486
FT /evidence="ECO:0000250"
FT DISULFID 480..495
FT /evidence="ECO:0000250"
FT DISULFID 497..506
FT /evidence="ECO:0000250"
FT DISULFID 513..524
FT /evidence="ECO:0000250"
FT DISULFID 518..533
FT /evidence="ECO:0000250"
FT DISULFID 535..544
FT /evidence="ECO:0000250"
FT DISULFID 551..561
FT /evidence="ECO:0000250"
FT DISULFID 556..570
FT /evidence="ECO:0000250"
FT DISULFID 572..581
FT /evidence="ECO:0000250"
FT DISULFID 588..599
FT /evidence="ECO:0000250"
FT DISULFID 593..608
FT /evidence="ECO:0000250"
FT DISULFID 610..619
FT /evidence="ECO:0000250"
FT DISULFID 626..636
FT /evidence="ECO:0000250"
FT DISULFID 631..645
FT /evidence="ECO:0000250"
FT DISULFID 647..656
FT /evidence="ECO:0000250"
FT DISULFID 663..674
FT /evidence="ECO:0000250"
FT DISULFID 668..683
FT /evidence="ECO:0000250"
FT DISULFID 685..694
FT /evidence="ECO:0000250"
FT DISULFID 701..711
FT /evidence="ECO:0000250"
FT DISULFID 706..720
FT /evidence="ECO:0000250"
FT DISULFID 722..731
FT /evidence="ECO:0000250"
FT DISULFID 740..751
FT /evidence="ECO:0000250"
FT DISULFID 745..760
FT /evidence="ECO:0000250"
FT DISULFID 762..771
FT /evidence="ECO:0000250"
FT DISULFID 777..788
FT /evidence="ECO:0000250"
FT DISULFID 782..798
FT /evidence="ECO:0000250"
FT DISULFID 800..809
FT /evidence="ECO:0000250"
FT DISULFID 816..828
FT /evidence="ECO:0000250"
FT DISULFID 822..837
FT /evidence="ECO:0000250"
FT DISULFID 839..848
FT /evidence="ECO:0000250"
FT DISULFID 855..866
FT /evidence="ECO:0000250"
FT DISULFID 860..875
FT /evidence="ECO:0000250"
FT DISULFID 877..886
FT /evidence="ECO:0000250"
FT DISULFID 893..903
FT /evidence="ECO:0000250"
FT DISULFID 898..912
FT /evidence="ECO:0000250"
FT DISULFID 914..923
FT /evidence="ECO:0000250"
FT DISULFID 930..941
FT /evidence="ECO:0000250"
FT DISULFID 935..950
FT /evidence="ECO:0000250"
FT DISULFID 952..961
FT /evidence="ECO:0000250"
FT DISULFID 968..979
FT /evidence="ECO:0000250"
FT DISULFID 973..988
FT /evidence="ECO:0000250"
FT DISULFID 990..999
FT /evidence="ECO:0000250"
FT DISULFID 1006..1017
FT /evidence="ECO:0000250"
FT DISULFID 1011..1024
FT /evidence="ECO:0000250"
FT DISULFID 1026..1035
FT /evidence="ECO:0000250"
FT DISULFID 1042..1063
FT /evidence="ECO:0000305"
FT DISULFID 1057..1072
FT /evidence="ECO:0000250"
FT DISULFID 1074..1083
FT /evidence="ECO:0000250"
FT DISULFID 1090..1101
FT /evidence="ECO:0000250"
FT DISULFID 1095..1110
FT /evidence="ECO:0000250"
FT DISULFID 1112..1121
FT /evidence="ECO:0000250"
FT DISULFID 1128..1139
FT /evidence="ECO:0000250"
FT DISULFID 1133..1148
FT /evidence="ECO:0000250"
FT DISULFID 1150..1159
FT /evidence="ECO:0000250"
FT DISULFID 1166..1184
FT /evidence="ECO:0000250"
FT DISULFID 1178..1193
FT /evidence="ECO:0000250"
FT DISULFID 1195..1204
FT /evidence="ECO:0000250"
FT DISULFID 1211..1224
FT /evidence="ECO:0000250"
FT DISULFID 1216..1234
FT /evidence="ECO:0000250"
FT DISULFID 1236..1245
FT /evidence="ECO:0000250"
FT DISULFID 1252..1263
FT /evidence="ECO:0000250"
FT DISULFID 1257..1277
FT /evidence="ECO:0000250"
FT DISULFID 1279..1288
FT /evidence="ECO:0000250"
FT DISULFID 1295..1306
FT /evidence="ECO:0000250"
FT DISULFID 1300..1315
FT /evidence="ECO:0000250"
FT DISULFID 1317..1326
FT /evidence="ECO:0000250"
FT DISULFID 1341..1352
FT /evidence="ECO:0000250"
FT DISULFID 1346..1363
FT /evidence="ECO:0000250"
FT DISULFID 1365..1374
FT /evidence="ECO:0000250"
FT DISULFID 1389..1412
FT /evidence="ECO:0000250"
FT DISULFID 1394..1407
FT /evidence="ECO:0000250"
FT DISULFID 1403..1419
FT /evidence="ECO:0000250"
FT DISULFID 1430..1453
FT /evidence="ECO:0000250"
FT DISULFID 1435..1448
FT /evidence="ECO:0000250"
FT DISULFID 1444..1460
FT /evidence="ECO:0000250"
FT DISULFID 1469..1495
FT /evidence="ECO:0000250"
FT DISULFID 1477..1490
FT /evidence="ECO:0000250"
FT DISULFID 1486..1502
FT /evidence="ECO:0000250"
SQ SEQUENCE 2319 AA; 244301 MW; 243BCA02D7C3283D CRC64;
MGPGARGRRR RRRLMALPPP PPPMRALPLL LLLLAGLGAA APPCLDGSPC ANGGRCTHQQ
PSREAACLCL PGWVGERCQL EDPCHSGPCA GRGVCQSSVV AGVARFSCRC LRGFRGPDCS
LPDPCFSSPC AHGAPCSVGS DGRYACACPP GYQGRNCRSD IDECRAGASC RHGGTCINTP
GSFHCLCPLG YTGLLCENPI VPCAPSPCRN GGTCRQSSDV TYDCACLPGF EGQNCEVNVD
DCPGHRCLNG GTCVDGVNTY NCQCPPEWTG QFCTEDVDEC QLQPNACHNG GTCFNLLGGH
SCVCVNGWTG ESCSQNIDDC ATAVCFHGAT CHDRVASFYC ACPMGKTGLL CHLDDACVSN
PCHEDAICDT NPVSGRAICT CPPGFTGGAC DQDVDECSIG ANPCEHLGRC VNTQGSFLCQ
CGRGYTGPRC ETDVNECLSG PCRNQATCLD RIGQFTCICM AGFTGTFCEV DIDECQSSPC
VNGGVCKDRV NGFSCTCPSG FSGSTCQLDV DECASTPCRN GAKCVDQPDG YECRCAEGFE
GTLCERNVDD CSPDPCHHGR CVDGIASFSC ACAPGYTGIR CESQVDECRS QPCRYGGKCL
DLVDKYLCRC PPGTTGVNCE VNIDDCASNP CTFGVCRDGI NRYDCVCQPG FTGPLCNVEI
NECASSPCGE GGSCVDGENG FHCLCPPGSL PPLCLPANHP CAHKPCSHGV CHDAPGGFQC
VCDPGWSGPR CSQSLAPDAC ESQPCQAGGT CTSDGIGFHC TCAPGFQGHQ CEVLSPCTPS
LCEHGGHCES DPDQLTVCSC PPGWQGPRCQ QDVDECAGAS PCGPHGTCTN LPGSFRCICH
GGYTGPFCDQ DIDDCDPNPC LNGGSCQDGV GSFSCSCLSG FAGPRCARDV DECLSSPCGP
GTCTDHVASF TCTCPPGYGG FHCETDLLDC SPSSCFNGGT CVDGVNSFSC LCRPGYTGTH
CQYKVDPCFS RPCLHGGICN PTHSGFECTC REGFTGNQCQ NPVDWCSQAP CQNGGRCVQT
GAYCICPPEW SGPLCDIPSL PCTEAAAHMG VRLEQLCQAG GQCIDKDHSH YCVCPEGRMG
SHCEQEVDPC TAQPCQHGGT CRGYMGGYVC ECPTGYSGDS CEDDVDECAS QPCQNGGSCI
DLVAHYLCSC PPGTLGVLCE INEDDCGPGP SLDSGLRCLH NGTCVDLVGG FRCNCPPGYT
GLHCEADINE CRPGTCHAAH TRDCLQDPGG HFRCICLPGF TGPRCQTALF PCESQPCQHG
GQCRPSLGRG GGLTFTCHCV QPFWGLRCER VARSCRELQC PVGIPCQQTA RGPRCACPPG
LSGPSCRVSR ASPSGATNTS CAATPCLHGG SCLPVQSVPF FRCVCAPGWG GPRCETPSAA
PEVPEEPRCP RAACQAKRGD QNCDRECNSP GCGWDGGDCS LNVDDPWRQC EALQCWRLFN
NSRCDPACSS PACLYDNFDC YSGGRDRTCN PVYKKYCADH FADGRCDQGC NTEECGWDGL
DCASEVPALL ARGVLVLTVL LPPEELLRSS ADFLQRLSAI LRTSLRFRLD ARGQAMVFPY
HRPSPGSESR VRRELGPEVI GSVVMLEIDN RLCLKSAEND HCFPDAQSAA DYLGALSAVE
RLDFPYPLRD VRGEPLEPPE QSVPLLPLLV AGAVFLLVIF VLGVMVARRK REHSTLWFPE
GFALHKDIAA GHKGRREPVG QDALGMKNMT KGESLMGEVA TDWNDSECPE AKRLKVEEPG
MGAEEPVDCR QWTQHHLVAA DIRVAPAMAL TPPQGDADAD GMDVNVRGPD GFTPLMLASF
CGGALEPMPA EEDEADDTSA SIISDLICQG AQLGARTDRT GETALHLAAR YARADAAKRL
LDAGADTNAQ DHSGRTPLHT AVTADAQGVF QILIRNRSTD LDARMADGST ALILAARLAV
EGMVEELIAS HADVNAVDEL GKSALHWAAA VNNVEATLAL LKNGANKDMQ DSKEETPLFL
AAREGSYEAA KLLLDHFANR EITDHLDRLP RDVAQERLHQ DIVRLLDQPS GPRSPSGPHG
LGPLLCPPGA FLPGLKAVQS GTKKSRRPPG KTGLGPQGTR GRGKKLTLAC PGPLADSSVT
LSPVDSLDSP RPFGGPPASP GGFPLEGPYA TTATTVSLAQ LGASRAGPLG RQPPGGCVLS
LGLLNPVAVP LDWARLPPPA PPGPSFLLPL APGSQLLNPA TPVSPHERPP PYLAAPGHGE
EYPAAGTHSS PTKARFLRVP SEHPYLTPSP ESPEHWASPS PPSLSDWSDS TPSPATATSA
TAAGALPAQP HPISVPSLPQ SQTQLGPQPE VTPKRQVMA
