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Database: UniProt/SWISS-PROT
Entry: CO4A2_CAEEL
LinkDB: CO4A2_CAEEL
Original site: CO4A2_CAEEL 
ID   CO4A2_CAEEL             Reviewed;        1758 AA.
AC   P17140; Q19098; Q19099;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Collagen alpha-2(IV) chain;
DE   AltName: Full=Lethal protein 2;
DE   Flags: Precursor;
GN   Name=let-2 {ECO:0000312|WormBase:F01G12.5a};
GN   Synonyms=clb-1 {ECO:0000312|WormBase:F01G12.5a};
GN   ORFNames=F01G12.5 {ECO:0000312|WormBase:F01G12.5a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2;
RX   PubMed=7691828; DOI=10.1083/jcb.123.1.255;
RA   Sibley M.H., Johnson J.J., Mello C.C., Kramer J.M.;
RT   "Genetic identification, sequence, and alternative splicing of the
RT   Caenorhabditis elegans alpha 2(IV) collagen gene.";
RL   J. Cell Biol. 123:255-264(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1495-1758.
RC   STRAIN=Bristol N2;
RX   PubMed=2793871; DOI=10.1016/s0021-9258(18)71530-5;
RA   Guo X., Kramer J.M.;
RT   "The two Caenorhabditis elegans basement membrane (type IV) collagen genes
RT   are located on separate chromosomes.";
RL   J. Biol. Chem. 264:17574-17582(1989).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS.
RX   PubMed=8045258; DOI=10.1002/j.1460-2075.1994.tb06629.x;
RA   Sibley M.H., Graham P.L., von Mende N., Kramer J.M.;
RT   "Mutations in the alpha 2(IV) basement membrane collagen gene of
RT   Caenorhabditis elegans produce phenotypes of differing severities.";
RL   EMBO J. 13:3278-3285(1994).
RN   [5]
RP   ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RX   PubMed=18230701; DOI=10.1101/gad.1620608;
RA   Ohno G., Hagiwara M., Kuroyanagi H.;
RT   "STAR family RNA-binding protein ASD-2 regulates developmental switching of
RT   mutually exclusive alternative splicing in vivo.";
RL   Genes Dev. 22:360-374(2008).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   GLY-1125; GLY-1286; GLY-1465 AND SER-1610.
RX   PubMed=19104038; DOI=10.1073/pnas.0804055106;
RA   Kubota Y., Ohkura K., Tamai K.K., Nagata K., Nishiwaki K.;
RT   "MIG-17/ADAMTS controls cell migration by recruiting nidogen to the
RT   basement membrane in C. elegans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:20804-20809(2008).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF GLY-877.
RX   PubMed=25080592; DOI=10.1523/jneurosci.5128-13.2014;
RA   Qin J., Liang J., Ding M.;
RT   "Perlecan antagonizes collagen IV and ADAMTS9/GON-1 in restricting the
RT   growth of presynaptic boutons.";
RL   J. Neurosci. 34:10311-10324(2014).
RN   [8]
RP   MUTAGENESIS OF GLU-479; PRO-587 AND SER-1610.
RX   PubMed=29440357; DOI=10.1534/genetics.118.300731;
RA   Gotenstein J.R., Koo C.C., Ho T.W., Chisholm A.D.;
RT   "Genetic Suppression of Basement Membrane Defects in Caenorhabditis elegans
RT   by Gain of Function in Extracellular Matrix and Cell-Matrix Attachment
RT   Genes.";
RL   Genetics 208:1499-1512(2018).
CC   -!- FUNCTION: Collagen type IV is specific for basement membranes
CC       (Probable). Together with fbl-1 and downstream of metalloprotease mig-
CC       17, recruits nidogen nid-1 to the gonad basement membrane thereby
CC       probably inducing basement membrane remodeling required for the
CC       directional migration of distal tip cells (PubMed:19104038). Required
CC       to restrict presynaptic growth at the neuromuscular junctions in late
CC       larval stage and in adult motor neurons (PubMed:25080592). Vital for
CC       embryonic development (PubMed:7691828, PubMed:8045258).
CC       {ECO:0000269|PubMed:19104038, ECO:0000269|PubMed:25080592,
CC       ECO:0000269|PubMed:7691828, ECO:0000269|PubMed:8045258, ECO:0000305}.
CC   -!- SUBUNIT: Trimers of two alpha 1(IV) and one alpha 2(IV) chain. Type IV
CC       collagen forms a mesh-like network linked through intermolecular
CC       interactions between 7S domains and between NC1 domains.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736,
CC       ECO:0000269|PubMed:19104038}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Exons 9 and 10 are mutually exclusive splicing exons. There
CC         is alternative usage of either exon 9 (isoform a) or exon 10 (isoform
CC         b). {ECO:0000305};
CC       Name=a {ECO:0000312|WormBase:F01G12.5a}; Synonyms=I
CC       {ECO:0000303|PubMed:7691828};
CC         IsoId=P17140-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F01G12.5b}; Synonyms=II
CC       {ECO:0000303|PubMed:7691828};
CC         IsoId=P17140-2; Sequence=VSP_001160;
CC   -!- TISSUE SPECIFICITY: Localizes to the basement membrane between distal
CC       tip cells and the germline. Localizes to the intestinal basement
CC       membrane. {ECO:0000269|PubMed:19104038}.
CC   -!- DEVELOPMENTAL STAGE: Alternatively spliced, in part by RNA-binding
CC       protein asd-2, to produce isoforms which are expressed at different
CC       developmental stages (PubMed:18230701). Isoform a: Predominantly
CC       expressed in embryos (PubMed:7691828, PubMed:18230701). Isoform b:
CC       Predominantly expressed in larvae and adults (PubMed:7691828,
CC       PubMed:18230701). {ECO:0000269|PubMed:18230701,
CC       ECO:0000269|PubMed:7691828}.
CC   -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC       (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC       in the long central triple-helical domain (which may cause flexibility
CC       in the triple helix), and a short N-terminal triple-helical 7S domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC       involved in inter- and intramolecular disulfide bonding. 12 of these,
CC       located in the NC1 domain, are conserved in all known type IV
CC       collagens. {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC       covalent bonds between Lys and Met residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA64312.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; Z22964; CAA80536.1; -; Genomic_DNA.
DR   EMBL; Z22964; CAA80537.1; -; Genomic_DNA.
DR   EMBL; U22327; AAA64312.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX284606; CCD68907.1; -; Genomic_DNA.
DR   EMBL; BX284606; CCD68906.1; -; Genomic_DNA.
DR   EMBL; J05066; AAA27989.1; -; Genomic_DNA.
DR   PIR; A34476; A34476.
DR   PIR; T29350; T29350.
DR   PIR; T29351; T29351.
DR   RefSeq; NP_510663.1; NM_078262.4.
DR   RefSeq; NP_510664.1; NM_078263.3.
DR   AlphaFoldDB; P17140; -.
DR   SMR; P17140; -.
DR   BioGRID; 46593; 2.
DR   STRING; 6239.F01G12.5b.1; -.
DR   GlyCosmos; P17140; 1 site, No reported glycans.
DR   EPD; P17140; -.
DR   PaxDb; 6239-F01G12-5b-1; -.
DR   PeptideAtlas; P17140; -.
DR   EnsemblMetazoa; F01G12.5a.1; F01G12.5a.1; WBGene00002280.
DR   EnsemblMetazoa; F01G12.5b.1; F01G12.5b.1; WBGene00002280.
DR   GeneID; 181708; -.
DR   UCSC; F01G12.5b.1; c. elegans. [P17140-1]
DR   AGR; WB:WBGene00002280; -.
DR   WormBase; F01G12.5a; CE04334; WBGene00002280; let-2.
DR   WormBase; F01G12.5b; CE04335; WBGene00002280; let-2.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000164076; -.
DR   HOGENOM; CLU_002023_1_0_1; -.
DR   InParanoid; P17140; -.
DR   OrthoDB; 2882192at2759; -.
DR   PhylomeDB; P17140; -.
DR   PRO; PR:P17140; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00002280; Expressed in larva and 3 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0005587; C:collagen type IV trimer; IMP:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IDA:WormBase.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IMP:UniProtKB.
DR   GO; GO:0016043; P:cellular component organization; NAS:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0035262; P:gonad morphogenesis; IGI:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:1903354; P:regulation of distal tip cell migration; IGI:UniProtKB.
DR   Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1065; COLLAGEN, TYPE IX, ALPHA 1A; 1.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 19.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Collagen; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1758
FT                   /note="Collagen alpha-2(IV) chain"
FT                   /id="PRO_0000005829"
FT   DOMAIN          1531..1754
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   REGION          27..42
FT                   /note="7S domain"
FT   REGION          42..1527
FT                   /note="Triple-helical region"
FT   REGION          47..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1316..1339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..389
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..733
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        248
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1546..1635
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1579..1632
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1591..1597
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1654..1750
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1688..1747
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   DISULFID        1700..1707
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   VAR_SEQ         229..264
FT                   /note="GDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDK -> GDIGAMGPAGPP
FT                   GPIASTMSKGTIIGPKGDLGEKGEK (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001160"
FT   MUTAGEN         48
FT                   /note="G->E: In MN114; 73% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         366
FT                   /note="A->T: In MN126; 100% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         479
FT                   /note="E->K: In ju1166; suppresses the lethal phenotypes of
FT                   the pxn-2 tm3464 mutant."
FT                   /evidence="ECO:0000269|PubMed:29440357"
FT   MUTAGEN         570
FT                   /note="G->E: In MN109; 37% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         587
FT                   /note="P->L: In ju1180; suppresses the lethal phenotypes of
FT                   the pxn-2 tm3464 mutant."
FT                   /evidence="ECO:0000269|PubMed:29440357"
FT   MUTAGEN         588
FT                   /note="G->R: In MN103 and MN151; 96% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         597
FT                   /note="G->R: In MN152; 50% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         690
FT                   /note="G->E: In MN129; 100% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         690
FT                   /note="G->R: In MN101; 100% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         737
FT                   /note="G->E: In MN143; 100% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         877
FT                   /note="G->R: In g30; temperature-sensitive mutant. At the
FT                   restrictive temperature, causes 90 percent lethality. At
FT                   the permissive temperature of 16 degrees Celsius, causes
FT                   the formation of ectopic presynaptic boutons on the ventral
FT                   cord axons."
FT                   /evidence="ECO:0000269|PubMed:25080592,
FT                   ECO:0000269|PubMed:8045258"
FT   MUTAGEN         904
FT                   /note="G->R: In E1470; 94% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1003
FT                   /note="G->E: In MN139; 20% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1125
FT                   /note="G->D: In g25; temperature-sensitive mutant. At the
FT                   restrictive temperature of 25 degrees Celsius, causes 96
FT                   percent embryonic lethality. At the permissive temperature
FT                   of 22.5 degrees Celsius, partially restores normal distal
FT                   tip cell migration in a mig-17 (k174) mutant background."
FT                   /evidence="ECO:0000269|PubMed:19104038,
FT                   ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1152
FT                   /note="G->D: In MN147; 7% lethal."
FT                   /evidence="ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1286
FT                   /note="G->D: In g37 and b246; 9% lethal. Moderate reduction
FT                   in basement membrane localization associated with a
FT                   moderate accumulation in muscle cell cytoplasm. At the
FT                   restrictive temperature of 25 degrees Celsius, causes a
FT                   reduction of nid-1 recruitment to the gonad basement
FT                   membrane. At the permissive temperature of 22.5 degrees
FT                   Celsius, partially restores normal distal tip cell
FT                   migration in a mig-17 (k174) mutant background."
FT                   /evidence="ECO:0000269|PubMed:19104038,
FT                   ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1465
FT                   /note="G->R: In k196; temperature-sensitive mutant. At the
FT                   restrictive temperature of 25 degrees Celsius, causes 85
FT                   percent larval lethality. Slight reduction in basement
FT                   membrane localization associated with a slight
FT                   intracellular accumulation in muscle and distal tip cells
FT                   (DTC). In a mig-17 (k174) mutant background, restores
FT                   normal DTC migration and nid-1 basement membrane
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:19104038,
FT                   ECO:0000269|PubMed:8045258"
FT   MUTAGEN         1610
FT                   /note="S->L: In k193; temperature-sensitive mutant. At both
FT                   the restrictive and permissive temperatures, causes 16-20
FT                   percent embryonic lethality. Slight reduction in basement
FT                   membrane localization associated with a slight
FT                   intracellular accumulation in muscle and distal tip cells
FT                   (DTC). In a mig-17 (k174) mutant background, restores
FT                   normal DTC migration and nid-1 basement membrane
FT                   localization. Enhances the lethality of the pxn-2 mutant
FT                   (ju432)."
FT                   /evidence="ECO:0000269|PubMed:19104038,
FT                   ECO:0000269|PubMed:29440357, ECO:0000269|PubMed:8045258"
FT   CONFLICT        1604
FT                   /note="E -> D (in Ref. 2; CCD68907/CCD68906)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1682
FT                   /note="P -> L (in Ref. 2; CCD68907/CCD68906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1758 AA;  167751 MW;  97EE3F3DBB2D2AC5 CRC64;
     MKQRAALGPV LRLAILALLA VSYVQSQATC RDCSNRGCFC VGEKGSMGAP GPQGPPGTQG
     IRGFPGPEGL AGPKGLKGAQ GPPGPVGIKG DRGAVGVPGF PGNDGGNGRP GEPGPPGAPG
     WDGCNGTDGA PGIPGRPGPP GMPGFPGPPG MDGLKGEPAI GYAGAPGEKG DGGMPGMPGL
     PGPSGRDGYP GEKGDRGDTG NAGPRGPPGE AGSPGNPGIG SIGPKGDPGD LGSVGPPGPP
     GPREFTGSGS IVGPRGNPGE KGDKGEPGEG GQRGYPGNGG LSGQPGLPGM KGEKGLSGPA
     GPRGKEGRPG NAGPPGFKGD RGLDGLGGIP GLPGQKGEAG YPGRDGPKGN SGPPGPPGGG
     TFNDGAPGPP GLPGRPGNPG PPGTDGYPGA PGPAGPIGNT GGPGLPGYPG NEGLPGPKGD
     KGDGGIPGAP GVSGPSGIPG LPGPKGEPGY RGTPGQSIPG LPGKDGKPGL DGAPGRKGEN
     GLPGVRGPPG DSLNGLPGAP GQRGAPGPNG YDGRDGVNGL PGAPGTKGDR GGTCSACAPG
     TKGEKGLPGY SGQPGPQGDR GLPGMPGPVG DAGDDGLPGP AGRPGSPGPP GQDGFPGLPG
     QKGEPTQLTL RPGPPGYPGL KGENGFPGQP GVDGLPGPSG PVGPPGAPGY PGEKGDAGLP
     GLSGKPGQDG LPGLPGNKGE AGYGQPGQPG FPGAKGDGGL PGLPGTPGLQ GMPGEPAPEN
     QVNPAPPGQP GLPGLPGTKG EGGYPGRPGE VGQPGFPGLP GMKGDSGLPG PPGLPGHPGV
     PGDKGFGGVP GLPGIPGPKG DVGNPGLPGL NGQKGEPGVG VPGQPGSPGF PGLKGDAGLP
     GLPGTPGLEG QRGFPGAPGL KGGDGLPGLS GQPGYPGEKG DAGLPGVPGR EGSPGFPGQD
     GLPGVPGMKG EDGLPGLPGV TGLKGDLGAP GQSGAPGLPG APGYPGMKGN AGIPGVPGFK
     GDGGLPGLPG LNGPKGEPGV PGMPGTPGMK GNGGLPGLPG RDGLSGVPGM KGDRGFNGLP
     GEKGEAGPAA RDGQKGDAGL PGQPGLRGPQ GPSGLPGVPG FKGETGLPGY GQPGQPGEKG
     LPGIPGKAGR QGAPGSPGQD GLPGFPGMKG ESGYPGQDGL PGRDGLPGVP GQKGDLGQSG
     QPGLSGAPGL DGQPGVPGIR GDKGQGGLPG IPGDRGMDGY PGQKGENGYP GQPGLPGLGG
     EKGFAGTPGF PGLKGSPGYP GQDGLPGIPG LKGDSGFPGQ PGQEGLPGLS GEKGMGGLPG
     MPGQPGQSIA GPVGPPGAPG LQGKDGFPGL PGQKGESGLS GLPGAPGLKG ESGMPGFPGA
     KGDLGANGIP GKRGEDGLPG VPGRDGQPGI PGLKGEVGGA GLPGQPGFPG IPGLKGEGGL
     PGFPGAKGEA GFPGTPGVPG YAGEKGDGGL PGLPGRDGLP GADGPVGPPG PSGPQNLVEP
     GEKGLPGLPG APGLRGEKGM PGLDGPPGND GPPGLPGQRG NDGYPGAPGL SGEKGMGGLP
     GFPGLDGQPG GPGAPGLPGA PGAAGPAYRD GFVLVKHSQT TEVPRCPEGQ TKLWDGYSLL
     YIEGNEKSHN QDLGHAGSCL QRFSTMPFLF CDFNNVCNYA SRNEKSYWLS TSEAIPMMPV
     NEREIEPYIS RCAVCEAPAN TIAVHSQTIQ IPNCPAGWSS LWIGYSFAMH TGAGAEGGGQ
     SPSSPGSCLE DFRATPFIEC NGARGSCHYF ANKFSFWLTT IDNDSEFKVP ESQTLKSGNL
     RTRVSRCQVC VKSTDGRH
//
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