GenomeNet

Database: UniProt
Entry: Q9Y219
LinkDB: Q9Y219
Original site: Q9Y219 
ID   JAG2_HUMAN              Reviewed;        1238 AA.
AC   Q9Y219; Q9UE17; Q9UE99; Q9UNK8; Q9Y6P9; Q9Y6Q0;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   13-FEB-2019, entry version 189.
DE   RecName: Full=Protein jagged-2;
DE            Short=Jagged2;
DE            Short=hJ2;
DE   Flags: Precursor;
GN   Name=JAG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LYS-501.
RX   PubMed=9315665; DOI=10.1128/MCB.17.10.6057;
RA   Luo B., Aster J.C., Hasserjian R.P., Kuo F., Sklar J.;
RT   "Isolation and functional analysis of a cDNA for human Jagged2, a gene
RT   encoding a ligand for the Notch1 receptor.";
RL   Mol. Cell. Biol. 17:6057-6067(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LYS-501.
RC   TISSUE=Fetal brain;
RX   PubMed=10079256; DOI=10.1016/S0002-9440(10)65325-4;
RA   Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L.,
RA   Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.;
RT   "Human ligands of the Notch receptor.";
RL   Am. J. Pathol. 154:785-794(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT),
RP   AND VARIANT LYS-501.
RC   TISSUE=Bone marrow;
RX   PubMed=10662552; DOI=10.1006/geno.1999.6045;
RA   Deng Y., Madan A., Banta A.B., Friedman C., Trask B.J., Hood L.,
RA   Li L.;
RT   "Characterization, chromosomal localization, and the complete 30-kb
RT   DNA sequence of the human Jagged2 (JAG2) gene.";
RL   Genomics 63:133-138(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-1238 (ISOFORM LONG).
RC   TISSUE=Heart;
RX   PubMed=9486542; DOI=10.1016/S0925-4773(97)00146-9;
RA   Valsecchi C., Ghezzi C., Ballabio A., Rugarli E.I.;
RT   "JAGGED2: a putative Notch ligand expressed in the apical ectodermal
RT   ridge and in sites of epithelial-mesenchymal interactions.";
RL   Mech. Dev. 69:203-207(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. Involved in limb development (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q5VTD9:GFI1B; NbExp=2; IntAct=EBI-946223, EBI-946212;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9Y219-1; Sequence=Displayed;
CC       Name=Short; Synonyms=HJAG2.del-E6;
CC         IsoId=Q9Y219-2; Sequence=VSP_001395;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, placenta and skeletal
CC       muscle and to a lesser extent in pancreas. Very low expression in
CC       brain, lung, liver and kidney.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/JAG2ID41030ch14q32.html";
DR   EMBL; AF020201; AAB71189.1; -; mRNA.
DR   EMBL; AF003521; AAB61285.1; -; mRNA.
DR   EMBL; AF029778; AAB84215.1; -; mRNA.
DR   EMBL; AF029779; AAB84216.1; -; mRNA.
DR   EMBL; AF111170; AAD15562.1; -; Genomic_DNA.
DR   EMBL; Y14330; CAA74706.1; -; mRNA.
DR   CCDS; CCDS9998.1; -. [Q9Y219-1]
DR   CCDS; CCDS9999.1; -. [Q9Y219-2]
DR   RefSeq; NP_002217.3; NM_002226.4. [Q9Y219-1]
DR   RefSeq; NP_660142.1; NM_145159.2. [Q9Y219-2]
DR   UniGene; Hs.433445; -.
DR   PDB; 5MW5; X-ray; 2.70 A; A=27-309.
DR   PDB; 5MW7; X-ray; 2.80 A; A=27-348.
DR   PDB; 5MWF; X-ray; 2.80 A; A/B/C/D/E/F=27-309.
DR   PDBsum; 5MW5; -.
DR   PDBsum; 5MW7; -.
DR   PDBsum; 5MWF; -.
DR   ProteinModelPortal; Q9Y219; -.
DR   SMR; Q9Y219; -.
DR   BioGrid; 109918; 23.
DR   IntAct; Q9Y219; 9.
DR   STRING; 9606.ENSP00000328169; -.
DR   iPTMnet; Q9Y219; -.
DR   PhosphoSitePlus; Q9Y219; -.
DR   BioMuta; JAG2; -.
DR   DMDM; 116242598; -.
DR   EPD; Q9Y219; -.
DR   jPOST; Q9Y219; -.
DR   PaxDb; Q9Y219; -.
DR   PeptideAtlas; Q9Y219; -.
DR   PRIDE; Q9Y219; -.
DR   ProteomicsDB; 85595; -.
DR   ProteomicsDB; 85596; -. [Q9Y219-2]
DR   Ensembl; ENST00000331782; ENSP00000328169; ENSG00000184916. [Q9Y219-1]
DR   Ensembl; ENST00000347004; ENSP00000328566; ENSG00000184916. [Q9Y219-2]
DR   GeneID; 3714; -.
DR   KEGG; hsa:3714; -.
DR   UCSC; uc001yqg.4; human. [Q9Y219-1]
DR   CTD; 3714; -.
DR   DisGeNET; 3714; -.
DR   EuPathDB; HostDB:ENSG00000184916.8; -.
DR   GeneCards; JAG2; -.
DR   H-InvDB; HIX0037647; -.
DR   HGNC; HGNC:6189; JAG2.
DR   HPA; CAB025481; -.
DR   HPA; HPA030636; -.
DR   HPA; HPA050567; -.
DR   MIM; 602570; gene.
DR   neXtProt; NX_Q9Y219; -.
DR   OpenTargets; ENSG00000184916; -.
DR   PharmGKB; PA29987; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000160944; -.
DR   HOGENOM; HOG000113124; -.
DR   HOVERGEN; HBG031645; -.
DR   InParanoid; Q9Y219; -.
DR   KO; K21635; -.
DR   OMA; GVNCHIN; -.
DR   OrthoDB; 72177at2759; -.
DR   PhylomeDB; Q9Y219; -.
DR   TreeFam; TF351835; -.
DR   Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
DR   Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   SignaLink; Q9Y219; -.
DR   SIGNOR; Q9Y219; -.
DR   ChiTaRS; JAG2; human.
DR   GeneWiki; JAG2; -.
DR   GenomeRNAi; 3714; -.
DR   PMAP-CutDB; Q9Y219; -.
DR   PRO; PR:Q9Y219; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000184916; Expressed in 222 organ(s), highest expression level in epithelium of mammary gland.
DR   Genevisible; Q9Y219; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR   GO; GO:1990134; P:epithelial cell apoptotic process involved in palatal shelf morphogenesis; IEA:Ensembl.
DR   GO; GO:0042492; P:gamma-delta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045061; P:thymic T cell selection; IDA:UniProtKB.
DR   InterPro; IPR001774; DSL.
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; IPR033108; Jag2.
DR   InterPro; IPR026219; Jagged/Serrate.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR44097:SF1; PTHR44097:SF1; 1.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 10.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR02059; JAGGEDFAMILY.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 16.
DR   SMART; SM00179; EGF_CA; 14.
DR   SMART; SM00214; VWC; 1.
DR   SMART; SM00215; VWC_out; 1.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 16.
DR   PROSITE; PS01186; EGF_2; 12.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 8.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Complete proteome;
KW   Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Notch signaling pathway; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   1238       Protein jagged-2.
FT                                /FTId=PRO_0000007629.
FT   TOPO_DOM     27   1080       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1081   1101       Helical. {ECO:0000255}.
FT   TOPO_DOM   1102   1238       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      196    240       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      241    274       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      275    305       EGF-like 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      307    345       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      347    383       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      385    421       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      423    459       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      461    496       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      498    534       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      536    572       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      574    634       EGF-like 10; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      636    672       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      674    710       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      712    748       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      751    787       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      789    825       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      827    863       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      870    944       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   MOD_RES    1123   1123       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    570    570       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    619    619       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1058   1058       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    198    207       {ECO:0000250}.
FT   DISULFID    211    223       {ECO:0000250}.
FT   DISULFID    231    240       {ECO:0000250}.
FT   DISULFID    245    256       {ECO:0000250}.
FT   DISULFID    249    262       {ECO:0000250}.
FT   DISULFID    264    273       {ECO:0000250}.
FT   DISULFID    276    287       {ECO:0000250}.
FT   DISULFID    282    293       {ECO:0000250}.
FT   DISULFID    295    304       {ECO:0000250}.
FT   DISULFID    311    323       {ECO:0000250}.
FT   DISULFID    317    333       {ECO:0000250}.
FT   DISULFID    335    344       {ECO:0000250}.
FT   DISULFID    351    362       {ECO:0000250}.
FT   DISULFID    356    371       {ECO:0000250}.
FT   DISULFID    373    382       {ECO:0000250}.
FT   DISULFID    389    400       {ECO:0000250}.
FT   DISULFID    394    409       {ECO:0000250}.
FT   DISULFID    411    420       {ECO:0000250}.
FT   DISULFID    427    438       {ECO:0000250}.
FT   DISULFID    432    447       {ECO:0000250}.
FT   DISULFID    449    458       {ECO:0000250}.
FT   DISULFID    465    475       {ECO:0000250}.
FT   DISULFID    469    484       {ECO:0000250}.
FT   DISULFID    486    495       {ECO:0000250}.
FT   DISULFID    502    513       {ECO:0000250}.
FT   DISULFID    507    522       {ECO:0000250}.
FT   DISULFID    524    533       {ECO:0000250}.
FT   DISULFID    540    551       {ECO:0000250}.
FT   DISULFID    545    560       {ECO:0000250}.
FT   DISULFID    562    571       {ECO:0000250}.
FT   DISULFID    589    612       {ECO:0000255}.
FT   DISULFID    606    622       {ECO:0000255}.
FT   DISULFID    624    633       {ECO:0000250}.
FT   DISULFID    640    651       {ECO:0000250}.
FT   DISULFID    645    660       {ECO:0000250}.
FT   DISULFID    662    671       {ECO:0000250}.
FT   DISULFID    678    689       {ECO:0000250}.
FT   DISULFID    683    698       {ECO:0000250}.
FT   DISULFID    700    709       {ECO:0000250}.
FT   DISULFID    716    727       {ECO:0000250}.
FT   DISULFID    721    736       {ECO:0000250}.
FT   DISULFID    738    747       {ECO:0000250}.
FT   DISULFID    755    766       {ECO:0000250}.
FT   DISULFID    760    775       {ECO:0000250}.
FT   DISULFID    777    786       {ECO:0000250}.
FT   DISULFID    793    804       {ECO:0000250}.
FT   DISULFID    798    813       {ECO:0000250}.
FT   DISULFID    815    824       {ECO:0000250}.
FT   DISULFID    831    842       {ECO:0000250}.
FT   DISULFID    836    851       {ECO:0000250}.
FT   DISULFID    853    862       {ECO:0000250}.
FT   VAR_SEQ     424    461       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:10662552}.
FT                                /FTId=VSP_001395.
FT   VARIANT     501    501       E -> K (in dbSNP:rs1057744).
FT                                {ECO:0000269|PubMed:10079256,
FT                                ECO:0000269|PubMed:10662552,
FT                                ECO:0000269|PubMed:9315665}.
FT                                /FTId=VAR_028113.
FT   VARIANT     538    538       D -> N (in dbSNP:rs9972231).
FT                                /FTId=VAR_048986.
FT   CONFLICT      8     12       RLPRR -> AFPPA (in Ref. 1; AAB71189).
FT                                {ECO:0000305}.
FT   CONFLICT    119    119       A -> P (in Ref. 1; AAB71189).
FT                                {ECO:0000305}.
FT   CONFLICT    129    129       L -> F (in Ref. 1; AAB71189).
FT                                {ECO:0000305}.
FT   CONFLICT    384    384       L -> SA (in Ref. 4; CAA74706).
FT                                {ECO:0000305}.
FT   CONFLICT    424    426       ANE -> VND (in Ref. 1; AAB71189).
FT                                {ECO:0000305}.
FT   CONFLICT   1235   1235       A -> V (in Ref. 2; AAB61285).
FT                                {ECO:0000305}.
FT   STRAND       28     38       {ECO:0000244|PDB:5MW5}.
FT   STRAND       47     49       {ECO:0000244|PDB:5MW5}.
FT   STRAND       69     76       {ECO:0000244|PDB:5MW5}.
FT   STRAND       91     94       {ECO:0000244|PDB:5MW5}.
FT   STRAND       99    104       {ECO:0000244|PDB:5MW5}.
FT   STRAND      110    112       {ECO:0000244|PDB:5MW7}.
FT   HELIX       113    118       {ECO:0000244|PDB:5MW7}.
FT   STRAND      129    134       {ECO:0000244|PDB:5MW5}.
FT   STRAND      140    150       {ECO:0000244|PDB:5MW5}.
FT   HELIX       159    161       {ECO:0000244|PDB:5MW5}.
FT   STRAND      162    171       {ECO:0000244|PDB:5MW5}.
FT   STRAND      174    176       {ECO:0000244|PDB:5MW5}.
FT   STRAND      179    184       {ECO:0000244|PDB:5MW5}.
FT   STRAND      189    198       {ECO:0000244|PDB:5MW5}.
FT   STRAND      202    204       {ECO:0000244|PDB:5MW5}.
FT   STRAND      214    216       {ECO:0000244|PDB:5MW5}.
FT   STRAND      219    223       {ECO:0000244|PDB:5MW5}.
FT   STRAND      229    231       {ECO:0000244|PDB:5MW5}.
FT   STRAND      235    237       {ECO:0000244|PDB:5MW5}.
FT   STRAND      253    255       {ECO:0000244|PDB:5MW5}.
FT   STRAND      268    273       {ECO:0000244|PDB:5MW5}.
FT   STRAND      284    286       {ECO:0000244|PDB:5MW5}.
FT   TURN        301    304       {ECO:0000244|PDB:5MW5}.
FT   STRAND      306    314       {ECO:0000244|PDB:5MW7}.
FT   STRAND      323    325       {ECO:0000244|PDB:5MW7}.
FT   STRAND      331    333       {ECO:0000244|PDB:5MW7}.
SQ   SEQUENCE   1238 AA;  133367 MW;  23B4FCD7D2891EF7 CRC64;
     MRAQGRGRLP RRLLLLLALW VQAARPMGYF ELQLSALRNV NGELLSGACC DGDGRTTRAG
     GCGHDECDTY VRVCLKEYQA KVTPTGPCSY GHGATPVLGG NSFYLPPAGA AGDRARARAR
     AGGDQDPGLV VIPFQFAWPR SFTLIVEAWD WDNDTTPNEE LLIERVSHAG MINPEDRWKS
     LHFSGHVAHL ELQIRVRCDE NYYSATCNKF CRPRNDFFGH YTCDQYGNKA CMDGWMGKEC
     KEAVCKQGCN LLHGGCTVPG ECRCSYGWQG RFCDECVPYP GCVHGSCVEP WQCNCETNWG
     GLLCDKDLNY CGSHHPCTNG GTCINAEPDQ YRCTCPDGYS GRNCEKAEHA CTSNPCANGG
     SCHEVPSGFE CHCPSGWSGP TCALDIDECA SNPCAAGGTC VDQVDGFECI CPEQWVGATC
     QLDANECEGK PCLNAFSCKN LIGGYYCDCI PGWKGINCHI NVNDCRGQCQ HGGTCKDLVN
     GYQCVCPRGF GGRHCELERD ECASSPCHSG GLCEDLADGF HCHCPQGFSG PLCEVDVDLC
     EPSPCRNGAR CYNLEGDYYC ACPDDFGGKN CSVPREPCPG GACRVIDGCG SDAGPGMPGT
     AASGVCGPHG RCVSQPGGNF SCICDSGFTG TYCHENIDDC LGQPCRNGGT CIDEVDAFRC
     FCPSGWEGEL CDTNPNDCLP DPCHSRGRCY DLVNDFYCAC DDGWKGKTCH SREFQCDAYT
     CSNGGTCYDS GDTFRCACPP GWKGSTCAVA KNSSCLPNPC VNGGTCVGSG ASFSCICRDG
     WEGRTCTHNT NDCNPLPCYN GGICVDGVNW FRCECAPGFA GPDCRINIDE CQSSPCAYGA
     TCVDEINGYR CSCPPGRAGP RCQEVIGFGR SCWSRGTPFP HGSSWVEDCN SCRCLDGRRD
     CSKVWCGWKP CLLAGQPEAL SAQCPLGQRC LEKAPGQCLR PPCEAWGECG AEEPPSTPCL
     PRSGHLDNNC ARLTLHFNRD HVPQGTTVGA ICSGIRSLPA TRAVARDRLL VLLCDRASSG
     ASAVEVAVSF SPARDLPDSS LIQGAAHAIV AAITQRGNSS LLLAVTEVKV ETVVTGGSST
     GLLVPVLCGA FSVLWLACVV LCVWWTRKRR KERERSRLPR EESANNQWAP LNPIRNPIER
     PGGHKDVLYQ CKNFTPPPRR ADEALPGPAG HAAVREDEED EDLGRGEEDS LEAEKFLSHK
     FTKDPGRSPG RPAHWASGPK VDNRAVRSIN EARYAGKE
//
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