GenomeNet

Database: UniProt
Entry: O77469
LinkDB: O77469
Original site: O77469 
ID   FBLN1_CAEEL             Reviewed;         728 AA.
AC   O77469; O18026; O77474; Q20903; Q50JF9; Q5I5Q9; Q95NZ3; Q9TZS1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 3.
DT   13-FEB-2019, entry version 163.
DE   RecName: Full=Fibulin-1;
DE   Flags: Precursor;
GN   Name=fbl-1; Synonyms=fbln1; ORFNames=F56H11.1;
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 / MRNA] (ISOFORMS A AND B).
RC   STRAIN=CB1489;
RX   PubMed=9923656; DOI=10.1016/S0945-053X(98)90114-7;
RA   Barth J.L., Argraves K.M., Roark E.F., Little C.D., Argraves W.S.;
RT   "Identification of chicken and C. elegans fibulin-1 homologs and
RT   characterization of the C. elegans fibulin-1 gene.";
RL   Matrix Biol. 17:635-646(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-288 AND HIS-290.
RX   PubMed=15556863; DOI=10.1016/j.cub.2004.10.047;
RA   Kubota Y., Kuroki R., Nishiwaki K.;
RT   "A fibulin-1 homolog interacts with an ADAM protease that controls
RT   cell migration in C. elegans.";
RL   Curr. Biol. 14:2011-2018(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=16120639; DOI=10.1242/dev.02007;
RA   Muriel J.M., Dong C., Hutter H., Vogel B.E.;
RT   "Fibulin-1C and Fibulin-1D splice variants have distinct functions and
RT   assemble in a hemicentin-dependent manner.";
RL   Development 132:4223-4234(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15556862; DOI=10.1016/j.cub.2004.11.006;
RA   Hesselson D., Newman C., Kim K.W., Kimble J.;
RT   "GON-1 and fibulin have antagonistic roles in control of organ
RT   shape.";
RL   Curr. Biol. 14:2005-2010(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17043142; DOI=10.1083/jcb.200608061;
RA   Hesselson D., Kimble J.;
RT   "Growth control by EGF repeats of the C. elegans Fibulin-1C isoform.";
RL   J. Cell Biol. 175:217-223(2006).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   GLY-288 AND HIS-290.
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   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22298704; DOI=10.1534/genetics.111.133173;
RA   Kubota Y., Nagata K., Sugimoto A., Nishiwaki K.;
RT   "Tissue architecture in the Caenorhabditis elegans gonad depends on
RT   interactions among fibulin-1, type IV collagen and the ADAMTS
RT   extracellular protease.";
RL   Genetics 190:1379-1388(2012).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-624, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers.
CC       Plays a role in cell adhesion and migration along protein fibers
CC       within the extracellular matrix (ECM). Important for certain
CC       developmental processes and contributes to the supramolecular
CC       organization of ECM architecture, in particular to those of
CC       basement membranes. {ECO:0000269|PubMed:15556862,
CC       ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639,
CC       ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:19104038,
CC       ECO:0000269|PubMed:22298704}.
CC   -!- FUNCTION: Isoform a: Involved in regulating the shape and adhesion
CC       of cells in the developing pharynx, intestine, body-wall muscle
CC       and gonadal tissue (PubMed:16120639). During gonadogenesis,
CC       regulates the width of gonads and the migration of distal tip
CC       cells (DTC) (PubMed:15556862, PubMed:17043142, PubMed:22298704).
CC       Together with type IV collagen let-2 and downstream of
CC       metalloprotease mig-17, recruits nidogen nid-1 to the gonad
CC       basement membrane thereby inducing basement membrane remodeling
CC       required for the directional migration of DTCs (PubMed:15556863,
CC       PubMed:19104038). Acts antagonistically with metalloprotease gon-1
CC       to maintain optimal levels of type IV collagen emb-9 in the gonad
CC       basement membrane during gonadogenesis (PubMed:15556862,
CC       PubMed:17043142, PubMed:22298704). Required for larval development
CC       (PubMed:17043142). {ECO:0000269|PubMed:15556862,
CC       ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639,
CC       ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:19104038}.
CC   -!- FUNCTION: Isoform c: Involved in the assembly of the flexible
CC       hemicentin-containing tracks found joining the pharynx and body-
CC       wall-muscle basement membranes. {ECO:0000269|PubMed:16120639}.
CC   -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC       matrix components. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform a: Secreted, extracellular space,
CC       extracellular matrix, basement membrane
CC       {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863,
CC       ECO:0000269|PubMed:17043142}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=c; Synonyms=Fibulin-1D;
CC         IsoId=O77469-1; Sequence=Displayed;
CC       Name=a; Synonyms=C, Fibulin-1C;
CC         IsoId=O77469-2; Sequence=VSP_001388, VSP_001390;
CC       Name=b; Synonyms=D;
CC         IsoId=O77469-3; Sequence=VSP_001388;
CC   -!- TISSUE SPECIFICITY: Expressed in head muscle cells, anterior and
CC       posterior intestinal cells (PubMed:15556862). Isoform a: Expressed
CC       in male and hermaphrodite gonad, anterior and posterior intestine
CC       and pharyngeal basement membranes, body-wall muscle, GLR cells,
CC       uterine attachment and mechanosensory neurons (PubMed:15556863,
CC       PubMed:16120639, PubMed:17043142). Isoform c: Expressed on ALM/PLM
CC       mechanosensory neuron attachments, in flexible tracks connecting
CC       the pharyngeal, body-wall-muscle basement membranes and in uterine
CC       attachments (PubMed:16120639). {ECO:0000269|PubMed:15556862,
CC       ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639,
CC       ECO:0000269|PubMed:17043142}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from late embryonic stage onwards.
CC       {ECO:0000269|PubMed:16120639}.
CC   -!- DISRUPTION PHENOTYPE: Gonads have short and swollen arms.
CC       Pharyngeal defects. Movement is lethargic.
CC       {ECO:0000269|PubMed:16120639, ECO:0000269|PubMed:17043142,
CC       ECO:0000269|PubMed:22298704}.
CC   -!- MISCELLANEOUS: Although involved in the same pathway as gon-1 and
CC       mig-17, it is probably not cleaved by these metalloproteases.
CC       {ECO:0000305|PubMed:15556862}.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
DR   EMBL; AB212860; BAD98165.1; -; mRNA.
DR   EMBL; AY851363; AAW34127.1; -; mRNA.
DR   EMBL; AF051401; AAC28321.1; -; mRNA.
DR   EMBL; AF051402; AAC28322.1; -; mRNA.
DR   EMBL; AF051403; AAC28323.1; -; Genomic_DNA.
DR   EMBL; AF051403; AAC28324.1; -; Genomic_DNA.
DR   EMBL; AF070477; AAC24035.1; -; Genomic_DNA.
DR   EMBL; Z68749; CAA92962.2; -; Genomic_DNA.
DR   EMBL; Z68219; CAA92962.2; JOINED; Genomic_DNA.
DR   EMBL; Z68749; CAC35817.1; -; Genomic_DNA.
DR   EMBL; Z68219; CAC35817.1; JOINED; Genomic_DNA.
DR   EMBL; Z68749; CAC35818.1; -; Genomic_DNA.
DR   EMBL; Z68219; CAC35818.1; JOINED; Genomic_DNA.
DR   PIR; T22793; T22793.
DR   PIR; T42760; T42760.
DR   PIR; T42990; T42990.
DR   PIR; T43210; T43210.
DR   RefSeq; NP_001023236.1; NM_001028065.2. [O77469-2]
DR   RefSeq; NP_001023237.1; NM_001028066.4. [O77469-3]
DR   RefSeq; NP_501694.2; NM_069293.4. [O77469-1]
DR   UniGene; Cel.12816; -.
DR   ProteinModelPortal; O77469; -.
DR   SMR; O77469; -.
DR   BioGrid; 42893; 6.
DR   DIP; DIP-26629N; -.
DR   IntAct; O77469; 7.
DR   MINT; O77469; -.
DR   STRING; 6239.F56H11.1c; -.
DR   iPTMnet; O77469; -.
DR   PaxDb; O77469; -.
DR   PeptideAtlas; O77469; -.
DR   EnsemblMetazoa; F56H11.1a; F56H11.1a; WBGene00001403. [O77469-2]
DR   EnsemblMetazoa; F56H11.1b; F56H11.1b; WBGene00001403. [O77469-3]
DR   EnsemblMetazoa; F56H11.1c; F56H11.1c; WBGene00001403. [O77469-1]
DR   GeneID; 177788; -.
DR   KEGG; cel:CELE_F56H11.1; -.
DR   UCSC; F56H11.1a.1; c. elegans. [O77469-1]
DR   CTD; 177788; -.
DR   WormBase; F56H11.1a; CE26701; WBGene00001403; fbl-1. [O77469-2]
DR   WormBase; F56H11.1b; CE26702; WBGene00001403; fbl-1. [O77469-3]
DR   WormBase; F56H11.1c; CE38374; WBGene00001403; fbl-1. [O77469-1]
DR   eggNOG; ENOG410IR7F; Eukaryota.
DR   eggNOG; ENOG410Y194; LUCA.
DR   GeneTree; ENSGT00940000156642; -.
DR   HOGENOM; HOG000007079; -.
DR   InParanoid; O77469; -.
DR   KO; K17307; -.
DR   OMA; CHENQEC; -.
DR   PhylomeDB; O77469; -.
DR   PRO; PR:O77469; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001403; Expressed in 4 organ(s), highest expression level in material anatomical entity.
DR   ExpressionAtlas; O77469; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IMP:WormBase.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:WormBase.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR026823; cEGF.
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; IPR017048; Fibulin-1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 6.
DR   PIRSF; PIRSF036313; Fibulin-1; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 8.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 8.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Calcium; Complete proteome;
KW   Developmental protein; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    728       Fibulin-1.
FT                                /FTId=PRO_0000007567.
FT   DOMAIN       23     64       Anaphylatoxin-like 1.
FT   DOMAIN       65     96       Anaphylatoxin-like 2.
FT   DOMAIN       97    129       Anaphylatoxin-like 3.
FT   DOMAIN      155    194       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      195    280       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      281    344       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      343    389       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      390    429       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      430    473       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      474    514       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      515    559       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      560    610       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD    624    624       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17761667}.
FT   DISULFID     23     49       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     24     56       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     37     57       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     66     94       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     79     95       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     97    121       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     98    128       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    111    129       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    159    168       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    164    178       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    180    279       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    285    298       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    292    307       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    347    359       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    353    368       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    375    388       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    394    404       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    399    413       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    415    428       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    434    448       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    442    457       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    459    472       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    478    489       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    485    498       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    500    513       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    519    534       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    530    543       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    545    558       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    564    576       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    569    585       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     196    280       RNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRAN
FT                                RIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHG
FT                                HCV -> IDECATLMDDCLESQRCLNTPGSFKCIRTLSCGT
FT                                GYAMDSETERCR (in isoform a and isoform
FT                                b). {ECO:0000303|PubMed:15556863,
FT                                ECO:0000303|PubMed:16120639,
FT                                ECO:0000303|PubMed:9923656}.
FT                                /FTId=VSP_001388.
FT   VAR_SEQ     603    728       QIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTII
FT                                SPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIV
FT                                QLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSK
FT                                YPF -> RCNRQPSACGLPEECSKVPLFLTYQFISLARAVP
FT                                ISSHRPAITLFKVSAPNHADTEVNFELQLKTTIVGAPNVLP
FT                                AIRANFLLQKGEKRNSAVVTLRDSLDGPQTVKLQLLLRMSK
FT                                KGKNFNTYAANLIVDVAAHKRHNTVHPPLMKIR (in
FT                                isoform a). {ECO:0000303|PubMed:15556863,
FT                                ECO:0000303|PubMed:16120639,
FT                                ECO:0000303|PubMed:9923656}.
FT                                /FTId=VSP_001390.
FT   MUTAGEN     288    288       G->E: In k201/tk51; slight defect in
FT                                posterior DTC migration. In a let-2
FT                                (k196) mutant background, partially
FT                                prevents anterior DTC migration. Restores
FT                                normal DTC migration and nid-1 basement
FT                                membrane localization in a mig-17 (k174)
FT                                mutant background but not in a mig-17
FT                                (k174) and nid-1 (cg119) mutant
FT                                background. Restores nid-1 basement
FT                                membrane localization in a mig-17 (k174)
FT                                mutant background.
FT                                {ECO:0000269|PubMed:15556863,
FT                                ECO:0000269|PubMed:19104038}.
FT   MUTAGEN     290    290       H->Y: In k206; No defect in DTC
FT                                migration. In a let-2 (k196) mutant
FT                                background, partially prevents anterior
FT                                DTC migration. Restores normal DTC
FT                                migration and nid-1 basement membrane
FT                                localization in a mig-17 (k174) mutant
FT                                background but not in a mig-17 (k174) and
FT                                nid-1 (cg119) mutant background.
FT                                {ECO:0000269|PubMed:15556863,
FT                                ECO:0000269|PubMed:19104038}.
FT   CONFLICT    195    195       D -> DH (in Ref. 1; AAC24035).
FT                                {ECO:0000305}.
SQ   SEQUENCE   728 AA;  79321 MW;  DBD2484CC6FD53A9 CRC64;
     MRICFLLLAF LVAETFANEL TRCCAGGTRH FKNSNTCSSI KSEGTSMTCQ RAASICCLRS
     LLDNACDSGT DIAKEEESCP SNINILGGGL KKECCDCCLL AKDLLNRNEP CVAPVGFSAG
     CLRSFNKCCN GDIEITHASE IITGRPLNDP HVLHLGDRCA SSHCEHLCHD RGGEKVECSC
     RSGFDLAPDG MACVDRNECL TRQSPCTQSE DCVNTIGGYI CQRRISRLVP HRHRANRIGN
     APRRMRDDPY SRAGEYREAS QANTEFGCPM GWLFQHGHCV DVDECNLGSH DCGPLYQCRN
     TQGSYRCDAK KCGDGELQNP MTGECTSITC PNGYYPKNGM CNDIDECVTG HNCGAGEECV
     NTPGSFRCQQ KGNLCAHGYE VNGATGFCED VNECQQGVCG SMECINLPGT YKCKCGPGYE
     FNDAKKRCED VDECIKFAGH VCDLSAECIN TIGSFECKCK PGFQLASDGR RCEDVNECTT
     GIAACEQKCV NIPGSYQCIC DRGFALGPDG TKCEDIDECS IWAGSGNDLC MGGCINTKGS
     YLCQCPPGYK IQPDGRTCVD VDECAMGECA GSDKVCVNTL GSFKCHSIDC PTNYIHDSLN
     KNQIADGYSC IKVCSTEDTE CLGNHTREVL YQFRAVPSLK TIISPIEVSR IVTHMGVPFS
     VDYNLDYVGQ RHFRIVQERN IGIVQLVKPI SGPTVETIKV NIHTKSRTGV ILAFNEAIIE
     ISVSKYPF
//
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