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Database: UniProt
Entry: P07898
LinkDB: P07898
Original site: P07898 
ID   PGCA_CHICK              Reviewed;        2109 AA.
AC   P07898; Q90810; Q90820; Q90991; Q91047;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   26-NOV-2014, entry version 136.
DE   RecName: Full=Aggrecan core protein;
DE   AltName: Full=Cartilage-specific proteoglycan core protein;
DE            Short=CSPCP;
DE   Flags: Precursor;
GN   Name=ACAN; Synonyms=AGC1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=White leghorn; TISSUE=Embryo;
RX   PubMed=8226878;
RA   Li H., Schwartz N.B., Vertel B.M.;
RT   "cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core
RT   protein and identification of a stop codon in the aggrecan gene
RT   associated with the chondrodystrophy, nanomelia.";
RL   J. Biol. Chem. 268:23504-23511(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Cartilage;
RX   PubMed=1339285;
RA   Chandrasekaran L., Tanzer M.L.;
RT   "Molecular cloning of chicken aggrecan. Structural analyses.";
RL   Biochem. J. 288:903-910(1992).
RN   [3]
RP   ERRATUM.
RX   PubMed=8280087;
RA   Chandrasekaran L., Tanzer M.L.;
RL   Biochem. J. 296:885-887(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1042-1559 (ISOFORMS 1/2).
RC   TISSUE=Embryo;
RX   PubMed=1694853;
RA   Krueger R.C. Jr., Fields T.A., Mensch J.R. Jr., Schwartz N.B.;
RT   "Chick cartilage chondroitin sulfate proteoglycan core protein. II.
RT   Nucleotide sequence of cDNA clone and localization of the S103L
RT   epitope.";
RL   J. Biol. Chem. 265:12088-12097(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1492-1610.
RC   STRAIN=White leghorn; TISSUE=Chondrocyte;
RX   PubMed=7827752; DOI=10.1016/0945-053X(94)90195-3;
RA   Primorac D., Stover M.L., Clark S.H., Rowe D.W.;
RT   "Molecular basis of nanomelia, a heritable chondrodystrophy of
RT   chicken.";
RL   Matrix Biol. 14:297-305(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2109 (ISOFORM 2).
RX   PubMed=3460082; DOI=10.1073/pnas.83.14.5081;
RA   Sai S., Tanaka T., Kosher R.A., Tanzer M.L.;
RT   "Cloning and sequence analysis of a partial cDNA for chicken cartilage
RT   proteoglycan core protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:5081-5085(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1894-2109.
RX   PubMed=3170613;
RA   Tanaka T., Har-El R., Tanzer M.L.;
RT   "Partial structure of the gene for chicken cartilage proteoglycan core
RT   protein.";
RL   J. Biol. Chem. 263:15831-15835(1988).
RN   [8]
RP   PROTEIN SEQUENCE OF 718-736; 998-1023 AND 1247-1275, AND GLYCOSYLATION
RP   AT THR-728; SER-1006; SER-1010; SER-1016; SER-1249; SER-1253;
RP   SER-1259; SER-1263 AND SER-1269.
RX   PubMed=2365711;
RA   Krueger R.C. Jr., Fields T.A., Hildreth J. IV, Schwartz N.B.;
RT   "Chick cartilage chondroitin sulfate proteoglycan core protein. I.
RT   Generation and characterization of peptides and specificity for
RT   glycosaminoglycan attachment.";
RL   J. Biol. Chem. 265:12075-12087(1990).
CC   -!- FUNCTION: This proteoglycan is a major component of extracellular
CC       matrix of cartilagenous tissues. A major function of this protein
CC       is to resist compression in cartilage. It binds avidly to
CC       hyaluronic acid via an N-terminal globular region. May play a
CC       regulatory role in the matrix assembly of the cartilage.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P07898-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P07898-2; Sequence=VSP_003073;
CC   -!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus
CC       of the proteoglycan, while another globular region, G3, makes up
CC       the C-terminus. G1 contains Link domains and thus consists of
CC       three disulfide-bonded loop structures designated as the A, B, B'
CC       motifs. G2 is similar to G1. The keratan sulfate (KS) and the
CC       chondroitin sulfate (CS) attachment domains lie between G2 and G3.
CC   -!- PTM: Contains mostly chondroitin sulfate, but also keratan sulfate
CC       chains, N-linked and O-linked oligosaccharides.
CC       {ECO:0000269|PubMed:2365711}.
CC   -!- DISEASE: Note=Defects in ACAN are the cause of nanomelia, a lethal
CC       connective tissue disorder affecting cartilage development
CC       (chondrodystrophy) characterized by shortened and malformed limbs.
CC       Aggrecan is truncated at its C-terminus in the CS-2 binding domain
CC       and is not anymore secreted from the chondrocytes.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00040}.
CC   -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 Link domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00323}.
CC   -!- SIMILARITY: Contains 1 Sushi (CCP/SCR) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00302}.
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DR   EMBL; L21913; AAB19128.1; -; mRNA.
DR   EMBL; M88101; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M38187; AAA48731.1; -; mRNA.
DR   EMBL; S74657; AAC60751.1; -; Genomic_DNA.
DR   EMBL; S74656; AAC60751.1; JOINED; Genomic_DNA.
DR   EMBL; M13993; AAA48720.1; -; mRNA.
DR   EMBL; J04028; AAA48719.1; -; Genomic_DNA.
DR   PIR; I50421; I50421.
DR   UniGene; Gga.3977; -.
DR   ProteinModelPortal; P07898; -.
DR   SMR; P07898; 1897-2020.
DR   PaxDb; P07898; -.
DR   eggNOG; NOG12793; -.
DR   HOGENOM; HOG000168421; -.
DR   HOVERGEN; HBG007982; -.
DR   InParanoid; P07898; -.
DR   PhylomeDB; P07898; -.
DR   PRO; PR:P07898; -.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 5.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 4.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00445; LINK; 4.
DR   SUPFAM; SSF56436; SSF56436; 5.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 4.
DR   PROSITE; PS50963; LINK_2; 4.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Immunoglobulin domain; Lectin;
KW   Metal-binding; Proteoglycan; Reference proteome; Repeat; Secreted;
KW   Signal; Sushi.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17   2109       Aggrecan core protein.
FT                                /FTId=PRO_0000017504.
FT   DOMAIN       34    143       Ig-like V-type.
FT   DOMAIN      149    244       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      250    347       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      520    615       Link 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      621    717       Link 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   REPEAT     1363   1382       1.
FT   REPEAT     1383   1402       2.
FT   REPEAT     1403   1422       3.
FT   REPEAT     1423   1442       4.
FT   REPEAT     1443   1462       5.
FT   REPEAT     1463   1482       6.
FT   REPEAT     1483   1502       7.
FT   REPEAT     1503   1522       8.
FT   REPEAT     1523   1542       9.
FT   REPEAT     1543   1562       10.
FT   REPEAT     1563   1582       11.
FT   REPEAT     1583   1602       12.
FT   REPEAT     1603   1622       13.
FT   REPEAT     1623   1642       14.
FT   REPEAT     1643   1662       15.
FT   REPEAT     1663   1682       16.
FT   REPEAT     1683   1702       17.
FT   REPEAT     1703   1722       18.
FT   REPEAT     1723   1742       19.
FT   DOMAIN     1855   1892       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1901   2019       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     2022   2082       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION       48    137       G1-A.
FT   REGION      148    243       G1-B.
FT   REGION      249    346       G1-B'.
FT   REGION      519    613       G2-B.
FT   REGION      620    715       G2-B'.
FT   REGION      718    803       KS.
FT   REGION      805   1264       CS-1.
FT   REGION     1265   1742       CS-2.
FT   REGION     1363   1742       19 X 20 AA tandem repeats of E-[TA]-S-T-
FT                                [ADHIFSRVT]-[YQLRH]-E-[IVTAG]-[SR]-[GS]-
FT                                E-[SAT]-[SP]-[AG]-[FYL]-P-[EA]-[TIV]-
FT                                [SRTG]-[IVT].
FT   REGION     1893   2109       G3.
FT   METAL      1958   1958       Calcium 1. {ECO:0000250}.
FT   METAL      1962   1962       Calcium 1. {ECO:0000250}.
FT   METAL      1962   1962       Calcium 3. {ECO:0000250}.
FT   METAL      1982   1982       Calcium 2. {ECO:0000250}.
FT   METAL      1984   1984       Calcium 2. {ECO:0000250}.
FT   METAL      1985   1985       Calcium 1. {ECO:0000250}.
FT   METAL      1991   1991       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1991   1991       Calcium 2. {ECO:0000250}.
FT   METAL      1992   1992       Calcium 1. {ECO:0000250}.
FT   METAL      1992   1992       Calcium 3. {ECO:0000250}.
FT   METAL      2005   2005       Calcium 2. {ECO:0000250}.
FT   METAL      2006   2006       Calcium 2. {ECO:0000250}.
FT   METAL      2006   2006       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   SITE       1001   1001       Not glycosylated.
FT   CARBOHYD     76     76       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    388    388       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    439    439       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    644    644       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    700    700       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    728    728       O-linked (Xyl...) (keratan sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD    765    765       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    801    801       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1006   1006       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1010   1010       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1016   1016       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1020   1020       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000305}.
FT   CARBOHYD   1249   1249       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1253   1253       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1259   1259       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1263   1263       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1269   1269       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000269|PubMed:2365711}.
FT   CARBOHYD   1273   1273       O-linked (Xyl...) (chondroitin sulfate).
FT                                {ECO:0000305}.
FT   DISULFID     51    129       {ECO:0000250}.
FT   DISULFID    171    242       {ECO:0000250}.
FT   DISULFID    195    216       {ECO:0000250}.
FT   DISULFID    269    345       {ECO:0000250}.
FT   DISULFID    293    314       {ECO:0000250}.
FT   DISULFID    542    613       {ECO:0000250}.
FT   DISULFID    566    587       {ECO:0000250}.
FT   DISULFID    640    715       {ECO:0000250}.
FT   DISULFID    664    685       {ECO:0000250}.
FT   DISULFID   1859   1870       {ECO:0000250}.
FT   DISULFID   1864   1879       {ECO:0000250}.
FT   DISULFID   1881   1890       {ECO:0000250}.
FT   DISULFID   1897   1908       {ECO:0000250}.
FT   DISULFID   1925   2017       {ECO:0000250}.
FT   DISULFID   1993   2009       {ECO:0000250}.
FT   DISULFID   2024   2067       {ECO:0000250}.
FT   DISULFID   2053   2080       {ECO:0000250}.
FT   VAR_SEQ    1856   1892       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1339285,
FT                                ECO:0000303|PubMed:3460082}.
FT                                /FTId=VSP_003073.
FT   CONFLICT    362    362       E -> D (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    601    601       G -> D (in Ref. 2). {ECO:0000305}.
FT   CONFLICT   1000   1000       P -> R (in Ref. 2; M88101).
FT                                {ECO:0000305}.
FT   CONFLICT   1029   1029       A -> P (in Ref. 2; M88101).
FT                                {ECO:0000305}.
FT   CONFLICT   1042   1043       VT -> PA (in Ref. 4; AAA48731).
FT                                {ECO:0000305}.
FT   CONFLICT   1251   1251       E -> D (in Ref. 2 and 8). {ECO:0000305}.
FT   CONFLICT   1587   1587       I -> T (in Ref. 5; AAC60751).
FT                                {ECO:0000305}.
FT   CONFLICT   1590   1590       I -> V (in Ref. 5; AAC60751).
FT                                {ECO:0000305}.
FT   CONFLICT   1594   1594       T -> S (in Ref. 5; AAC60751).
FT                                {ECO:0000305}.
FT   CONFLICT   1602   1610       IETSTVREI -> VLCRCSVLR (in Ref. 5;
FT                                AAC60751). {ECO:0000305}.
FT   CONFLICT   1603   1603       E -> A (in Ref. 2; M88101).
FT                                {ECO:0000305}.
FT   CONFLICT   1672   1672       S -> G (in Ref. 2; M88101).
FT                                {ECO:0000305}.
FT   CONFLICT   1796   1796       E -> G (in Ref. 2 and 6; AAA48720).
FT                                {ECO:0000305}.
FT   CONFLICT   1988   1988       F -> S (in Ref. 7; AAA48719).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2109 AA;  223493 MW;  7F824FD5B3A2ABDA CRC64;
     MTTLLLVFVC LQAITTAASA ELSDSSDGLE VKIPEQSPLR VVLGSSLNIP CYFNIPEEED
     TNALLTPRIK WSKLSNGTEI VLLVATGGKI RLNAEYREVI SLPNYPAIPT DATLEIKALR
     SNHTGIYRCE VMYGIEDRQD TIEVLVKGVV FHYRAISTRY TLNFERAKQA CIQNSAVIAT
     PEQLQAAYED GYEQCDAGWL ADQTVRYPIH LPRERCYGDK DEFPGVRTYG VRETDETYDV
     YCYAEQMQGK VFYATSPEKF TFQEAFDKCH SLGARLATTG ELYLAWKDGM DMCSAGWLAD
     RSVRYPISRA RPNCGGNLVG VRTVYLNPAN QTGYPHPSSR YDAICYSGDD FEALVPGLFT
     DEVGTELGSA FTIQTVTQTE VELPLPRNVT EEEARGSIAT LEPMEITATA TELYEAFTVL
     PDLFATSVTV ETASPREENV TREEITGIWA VPEEVTTSVS GTAFTTGMAE VSSVEEAIAV
     TATPGLESAS PFTIEDHLVQ VTAAPDVALL PRQPISPTGV VFHYRAATSR YAFSFIQAQQ
     ACLENNAVIA TPEQLQAAYE AGFDQCDAGW LRDQTVRYPI VNPRSNCVGD KESSPGVRSY
     GMRPASETYD VYCYIDRLKG EVFFATQPEQ FTFQEAQLYC ESQNATLASA GQLHAAWKQG
     LDRCYPGWLA DGSLRYPIVS PRPACGGDAP GVRTIYQHHN QTGFPDPLSR HHAFCFRALP
     SVVEEGVTSL FEEEVMVTQL IPGVEGIPSG EETTVETELS SEPENQTAQG TEVFPTDVSL
     LSARPSAFPP ATVIPEETST NASIPEVSGE FPESGEHPTS GEPSASGAPD TSGEPTSVGF
     ELSGEQSGIG ESGLPSVDLQ SSGFVPGESG LPSGDVSGLP SGIVDISGLP SAEEEVTVSV
     SRIPEVSGMP SGAESSGLHS GFSGEISGTE LISGLPSGEE SGLASGFPTI SLVDSTLVEV
     VTAAPGRQEE GKGSIGVSGE EELSGFPSAE WDSSGARGLP SGAETSGEQS GVPELSGEHS
     GVPGLSGEAF EVPELSGEHS GVTELSGEHS GLPELSGEPF GVPELSGFPS GLDISGEPSG
     APEVSGPVDV SGLTSGVDGS GEVSGVTFIS TSLQEVTTPS VAEAEAKEIL EISGLPSGET
     SGMVSGSLDV SGQPSGHIGF GGSASGVLEM SGFPGGAVES SGEASGVEVT SGLASGEESG
     LTSGFPTVSL VDTTLVEVVT QTSVAQEVGE GPSGMIEISG FLSGDRGVSG EGSGAVQSSG
     LPSGTGDFSG EPSGIPYFSG DISGATDLSG QPSAVTDISG EDSGLPEVTL VTSDLVEVVT
     RPTVSQELGG ETAVTFPYVF GPSGEGSASG DLSGGASAEG GIETSTAYEI SGESSAFPET
     SIETSTDQEI SGEASAYPEI SVETSTHLET SGETSAYPEI STETSTIQEV SGETSAFPEI
     STETSTIQEI SGETSAFPEI RIETSTFQEI SGETSAFPEI RIETSTSQEA RGETSAFPEI
     TIEASTVHET SGETSAFPEI SIETSTVHET SGETSAFPEI SIETSTVHEI SGESSAFPEI
     RIETSTSQEA RGETSAFPEI TIEASTIQEI SGETSAFPEI SIETSTVREI SGETSAFPEI
     RIETSTSQEA RGETSALPEI TIETSTVHET SGEASAFPEI SIETSTRQEA RSEASAYPEV
     SIEASTTQEV SGESSAFPEI SVETSTSQEA RGETSAFPEI GIETSTAHEG SGETPGLPAV
     STDTAATSLA SGEPSGAPEK ETPDTTSHLI TGVSGETSVP DAVISTSAPD VELAQEPRNT
     EETQLEIEPS TPAASGQETE TAAVLDNPHL PATATAALHP ASQEAVDALG PTTEDTDECH
     SSPCLNGATC VDGIDSFKCL CLPSYGGDLC EIDLANCEEG WIKFQGHCYR HFEERETWMD
     AESRCREHQA HLSSIITPEE QEFVNSHAQD YQWIGLSDRA VENDFRWSDG HSLQFENWRP
     NQPDNFFFAG EDCVVMIWHE QGEWNDVPCN YHLPFTCKKG TVACGDPPVV ENARTFGRKK
     DRYEINSLVR YQCDHGYIQR HVPTIRCQPN GHWEEPRISC TNPSSYQRRL YKRSPRSRLR
     PGVVHRPTH
//
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