GenomeNet

Database: UniProt
Entry: Q9R172
LinkDB: Q9R172
Original site: Q9R172 
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   16-JAN-2019, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   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
CC       Jagged1, Jagged2 and Delta1 to regulate cell-fate determination.
CC       Upon ligand activation through the released notch intracellular
CC       domain (NICD) it forms a transcriptional activator complex with
CC       RBPJ/RBPSUH and activates genes of the enhancer of split locus.
CC       Affects the implementation of differentiation, proliferation and
CC       apoptotic programs (By similarity). Acts instructively to control
CC       the cell fate determination of CNS multipotent progenitor cells,
CC       resulting in astroglial induction and neuron/oligodendrocyte
CC       suppression. {ECO:0000250, ECO:0000269|PubMed:11182080}.
CC   -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and a N-
CC       terminal fragment N(EC) which are probably linked by disulfide
CC       bonds. Interacts with MAML1, MAML2 and MAML3 which act as
CC       transcriptional coactivators for NOTCH3. Interacts with PSMA1 (By
CC       similarity). Interacts with HIF1AN (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q9UM47}; Single-pass type I membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Notch 3 intracellular domain: Nucleus.
CC       Note=Following proteolytical processing NICD is translocated to
CC       the nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in postnatal central nervous system
CC       (CNS) germinal zones and, in early postnatal life, within numerous
CC       cells throughout the CNS. It is more highly localized to
CC       ventricular germinal zones. {ECO:0000269|PubMed:11438922}.
CC   -!- DOMAIN: The EGF-like domains 10 and 11 are required for binding
CC       the ligands JAG1 and DLL1. {ECO:0000250|UniProtKB:Q9UM47}.
CC   -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
CC       which is proteolytically cleaved by a furin-like convertase in the
CC       trans-Golgi network before it reaches the plasma membrane to yield
CC       an active, ligand-accessible form. Cleavage results in a C-
CC       terminal fragment N(TM) and a N-terminal fragment N(EC). Following
CC       ligand binding, it is cleaved by TNF-alpha converting enzyme
CC       (TACE) to yield a membrane-associated intermediate fragment called
CC       notch extracellular truncation (NEXT). This fragment is then
CC       cleaved by presenilin dependent gamma-secretase to release a
CC       notch-derived peptide containing the intracellular domain (NICD)
CC       from the membrane (By similarity). {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}.
DR   EMBL; AF164486; AAD46653.2; -; mRNA.
DR   RefSeq; NP_064472.2; NM_020087.2.
DR   UniGene; Rn.228683; -.
DR   ProteinModelPortal; Q9R172; -.
DR   SMR; Q9R172; -.
DR   STRING; 10116.ENSRNOP00000037570; -.
DR   PaxDb; Q9R172; -.
DR   PRIDE; Q9R172; -.
DR   GeneID; 56761; -.
DR   KEGG; rno:56761; -.
DR   UCSC; RGD:620761; rat.
DR   CTD; 4854; -.
DR   RGD; 620761; Notch3.
DR   eggNOG; ENOG410KD9W; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   HOGENOM; HOG000234369; -.
DR   HOVERGEN; HBG052650; -.
DR   InParanoid; Q9R172; -.
DR   KO; K20995; -.
DR   OrthoDB; 7525at2759; -.
DR   PhylomeDB; Q9R172; -.
DR   PRO; PR:Q9R172; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:RGD.
DR   GO; GO:0050793; P:regulation of developmental process; IEA:InterPro.
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   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR024600; DUF3454_notch.
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; IPR000800; Notch_dom.
DR   InterPro; IPR010660; Notch_NOD_dom.
DR   InterPro; IPR011656; Notch_NODP_dom.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF11936; DUF3454; 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; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Methylation;
KW   Notch signaling pathway; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     40       {ECO:0000255}.
FT   CHAIN        41   2319       Neurogenic locus notch homolog protein 3.
FT                                /FTId=PRO_0000007698.
FT   CHAIN      1631   2319       Notch 3 extracellular truncation.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000007699.
FT   CHAIN      1664   2319       Notch 3 intracellular domain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000007700.
FT   TOPO_DOM     41   1645       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1646   1666       Helical. {ECO:0000255}.
FT   TOPO_DOM   1667   2319       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       41     79       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       80    120       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      121    158       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      160    197       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      199    236       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      238    274       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      276    314       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      316    352       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      353    391       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      393    431       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      433    469       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      471    507       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      509    545       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      547    582       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      584    620       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      622    657       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      659    695       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      697    732       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      736    772       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      773    810       EGF-like 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      812    849       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      851    887       EGF-like 22; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      889    924       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      926    962       EGF-like 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      964   1000       EGF-like 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1002   1036       EGF-like 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1038   1084       EGF-like 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1086   1122       EGF-like 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1124   1160       EGF-like 29; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1162   1205       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1207   1246       EGF-like 31. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1248   1289       EGF-like 32. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1291   1327       EGF-like 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1337   1375       EGF-like 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1389   1429       LNR 1.
FT   REPEAT     1430   1467       LNR 2.
FT   REPEAT     1469   1507       LNR 3.
FT   REPEAT     1840   1869       ANK 1.
FT   REPEAT     1873   1903       ANK 2.
FT   REPEAT     1907   1936       ANK 3.
FT   REPEAT     1940   1969       ANK 4.
FT   REPEAT     1973   2002       ANK 5.
FT   SITE       1573   1574       Cleavage; by furin-like protease.
FT                                {ECO:0000250}.
FT   MOD_RES    2175   2175       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9UM47}.
FT   CARBOHYD   1181   1181       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1338   1338       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1440   1440       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     44     56       {ECO:0000250}.
FT   DISULFID     50     67       {ECO:0000250}.
FT   DISULFID     69     78       {ECO:0000250}.
FT   DISULFID     84     95       {ECO:0000250}.
FT   DISULFID     89    108       {ECO:0000250}.
FT   DISULFID    110    119       {ECO:0000250}.
FT   DISULFID    125    136       {ECO:0000250}.
FT   DISULFID    130    146       {ECO:0000250}.
FT   DISULFID    148    157       {ECO:0000250}.
FT   DISULFID    164    176       {ECO:0000250}.
FT   DISULFID    170    185       {ECO:0000250}.
FT   DISULFID    187    196       {ECO:0000250}.
FT   DISULFID    203    214       {ECO:0000250}.
FT   DISULFID    208    224       {ECO:0000250}.
FT   DISULFID    226    235       {ECO:0000250}.
FT   DISULFID    242    253       {ECO:0000250}.
FT   DISULFID    247    262       {ECO:0000250}.
FT   DISULFID    264    273       {ECO:0000250}.
FT   DISULFID    280    293       {ECO:0000250}.
FT   DISULFID    287    302       {ECO:0000250}.
FT   DISULFID    304    313       {ECO:0000250}.
FT   DISULFID    320    331       {ECO:0000250}.
FT   DISULFID    325    340       {ECO:0000250}.
FT   DISULFID    342    351       {ECO:0000250}.
FT   DISULFID    357    368       {ECO:0000250}.
FT   DISULFID    362    379       {ECO:0000250}.
FT   DISULFID    381    390       {ECO:0000250}.
FT   DISULFID    397    410       {ECO:0000250}.
FT   DISULFID    404    419       {ECO:0000250}.
FT   DISULFID    421    430       {ECO:0000250}.
FT   DISULFID    437    448       {ECO:0000250}.
FT   DISULFID    442    457       {ECO:0000250}.
FT   DISULFID    459    468       {ECO:0000250}.
FT   DISULFID    475    486       {ECO:0000250}.
FT   DISULFID    480    495       {ECO:0000250}.
FT   DISULFID    497    506       {ECO:0000250}.
FT   DISULFID    513    524       {ECO:0000250}.
FT   DISULFID    518    533       {ECO:0000250}.
FT   DISULFID    535    544       {ECO:0000250}.
FT   DISULFID    551    561       {ECO:0000250}.
FT   DISULFID    556    570       {ECO:0000250}.
FT   DISULFID    572    581       {ECO:0000250}.
FT   DISULFID    588    599       {ECO:0000250}.
FT   DISULFID    593    608       {ECO:0000250}.
FT   DISULFID    610    619       {ECO:0000250}.
FT   DISULFID    626    636       {ECO:0000250}.
FT   DISULFID    631    645       {ECO:0000250}.
FT   DISULFID    647    656       {ECO:0000250}.
FT   DISULFID    663    674       {ECO:0000250}.
FT   DISULFID    668    683       {ECO:0000250}.
FT   DISULFID    685    694       {ECO:0000250}.
FT   DISULFID    701    711       {ECO:0000250}.
FT   DISULFID    706    720       {ECO:0000250}.
FT   DISULFID    722    731       {ECO:0000250}.
FT   DISULFID    740    751       {ECO:0000250}.
FT   DISULFID    745    760       {ECO:0000250}.
FT   DISULFID    762    771       {ECO:0000250}.
FT   DISULFID    777    788       {ECO:0000250}.
FT   DISULFID    782    798       {ECO:0000250}.
FT   DISULFID    800    809       {ECO:0000250}.
FT   DISULFID    816    828       {ECO:0000250}.
FT   DISULFID    822    837       {ECO:0000250}.
FT   DISULFID    839    848       {ECO:0000250}.
FT   DISULFID    855    866       {ECO:0000250}.
FT   DISULFID    860    875       {ECO:0000250}.
FT   DISULFID    877    886       {ECO:0000250}.
FT   DISULFID    893    903       {ECO:0000250}.
FT   DISULFID    898    912       {ECO:0000250}.
FT   DISULFID    914    923       {ECO:0000250}.
FT   DISULFID    930    941       {ECO:0000250}.
FT   DISULFID    935    950       {ECO:0000250}.
FT   DISULFID    952    961       {ECO:0000250}.
FT   DISULFID    968    979       {ECO:0000250}.
FT   DISULFID    973    988       {ECO:0000250}.
FT   DISULFID    990    999       {ECO:0000250}.
FT   DISULFID   1006   1017       {ECO:0000250}.
FT   DISULFID   1011   1024       {ECO:0000250}.
FT   DISULFID   1026   1035       {ECO:0000250}.
FT   DISULFID   1042   1063       {ECO:0000250}.
FT   DISULFID   1057   1072       {ECO:0000250}.
FT   DISULFID   1074   1083       {ECO:0000250}.
FT   DISULFID   1090   1101       {ECO:0000250}.
FT   DISULFID   1095   1110       {ECO:0000250}.
FT   DISULFID   1112   1121       {ECO:0000250}.
FT   DISULFID   1128   1139       {ECO:0000250}.
FT   DISULFID   1133   1148       {ECO:0000250}.
FT   DISULFID   1150   1159       {ECO:0000250}.
FT   DISULFID   1166   1184       {ECO:0000250}.
FT   DISULFID   1178   1193       {ECO:0000250}.
FT   DISULFID   1195   1204       {ECO:0000250}.
FT   DISULFID   1211   1224       {ECO:0000250}.
FT   DISULFID   1216   1234       {ECO:0000250}.
FT   DISULFID   1236   1245       {ECO:0000250}.
FT   DISULFID   1252   1263       {ECO:0000250}.
FT   DISULFID   1257   1277       {ECO:0000250}.
FT   DISULFID   1279   1288       {ECO:0000250}.
FT   DISULFID   1295   1306       {ECO:0000250}.
FT   DISULFID   1300   1315       {ECO:0000250}.
FT   DISULFID   1317   1326       {ECO:0000250}.
FT   DISULFID   1341   1352       {ECO:0000250}.
FT   DISULFID   1346   1363       {ECO:0000250}.
FT   DISULFID   1365   1374       {ECO:0000250}.
FT   DISULFID   1389   1412       {ECO:0000250}.
FT   DISULFID   1394   1407       {ECO:0000250}.
FT   DISULFID   1403   1419       {ECO:0000250}.
FT   DISULFID   1430   1453       {ECO:0000250}.
FT   DISULFID   1435   1448       {ECO:0000250}.
FT   DISULFID   1444   1460       {ECO:0000250}.
FT   DISULFID   1469   1495       {ECO:0000250}.
FT   DISULFID   1477   1490       {ECO:0000250}.
FT   DISULFID   1486   1502       {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
//
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