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Database: UniProt
Entry: Q10651
LinkDB: Q10651
Original site: Q10651 
ID   A4_CAEEL                Reviewed;         686 AA.
AC   Q10651; Q18583; Q95ZX1;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   07-APR-2021, entry version 153.
DE   RecName: Full=Amyloid-beta-like protein {ECO:0000305};
DE   Flags: Precursor;
GN   Name=apl-1 {ECO:0000312|WormBase:C42D8.8a};
GN   ORFNames=C42D8.8 {ECO:0000312|WormBase:C42D8.8a};
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-686.
RC   STRAIN=Bristol N2;
RX   PubMed=8265668; DOI=10.1073/pnas.90.24.12045;
RA   Daigle I., Li C.;
RT   "apl-1, a Caenorhabditis elegans gene encoding a protein related to the
RT   human beta-amyloid protein precursor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:12045-12049(1993).
RN   [3]
RP   INTERACTION WITH FEH-1, AND DISRUPTION PHENOTYPE.
RX   PubMed=11896189;
RA   Zambrano N., Bimonte M., Arbucci S., Gianni D., Russo T., Bazzicalupo P.;
RT   "feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65
RT   and beta-amyloid precursor protein genes, are involved in the same pathway
RT   that controls nematode pharyngeal pumping.";
RL   J. Cell Sci. 115:1411-1422(2002).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND IDENTIFICATION BY MASS
RP   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).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF GLU-377.
RX   PubMed=17267616; DOI=10.1073/pnas.0603997104;
RA   Hornsten A., Lieberthal J., Fadia S., Malins R., Ha L., Xu X., Daigle I.,
RA   Markowitz M., O'Connor G., Plasterk R., Li C.;
RT   "APL-1, a Caenorhabditis elegans protein related to the human beta-amyloid
RT   precursor protein, is essential for viability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1971-1976(2007).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18262516; DOI=10.1016/j.ydbio.2007.12.044;
RA   Niwa R., Zhou F., Li C., Slack F.J.;
RT   "The expression of the Alzheimer's amyloid precursor protein-like gene is
RT   regulated by developmental timing microRNAs and their targets in
RT   Caenorhabditis elegans.";
RL   Dev. Biol. 315:418-425(2008).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=20862215; DOI=10.1371/journal.pone.0012790;
RA   Wiese M., Antebi A., Zheng H.;
RT   "Intracellular trafficking and synaptic function of APL-1 in Caenorhabditis
RT   elegans.";
RL   PLoS ONE 5:3307-3314(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=22466039; DOI=10.1534/genetics.112.138768;
RA   Ewald C.Y., Raps D.A., Li C.;
RT   "APL-1, the Alzheimer's Amyloid precursor protein in Caenorhabditis
RT   elegans, modulates multiple metabolic pathways throughout development.";
RL   Genetics 191:493-507(2012).
RN   [9]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=28933985; DOI=10.1080/15384101.2017.1344798;
RA   Metheetrairut C., Ahuja Y., Slack F.J.;
RT   "acn-1, a C. elegans homologue of ACE, genetically interacts with the let-7
RT   microRNA and other heterochronic genes.";
RL   Cell Cycle 16:1800-1809(2017).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 240-478 IN COMPLEX WITH HEPARIN
RP   ANALOG, AND MUTAGENESIS OF ASN-252; HIS-254; ASP-348; SER-368; ARG-374;
RP   GLU-377; LYS-378 AND HIS-382.
RX   PubMed=19906646; DOI=10.1074/jbc.m109.018432;
RA   Hoopes J.T., Liu X., Xu X., Demeler B., Folta-Stogniew E., Li C., Ha Y.;
RT   "Structural characterization of the E2 domain of APL-1, a Caenorhabditis
RT   elegans homolog of human amyloid precursor protein, and its heparin binding
RT   site.";
RL   J. Biol. Chem. 285:2165-2173(2010).
RN   [11]
RP   STRUCTURE BY NMR OF 135-197, DISULFIDE BONDS, AND LACK OF COPPER-BINDING.
RX   PubMed=24276282; DOI=10.1039/c3mt00258f;
RA   Leong S.L., Young T.R., Barnham K.J., Wedd A.G., Hinds M.G., Xiao Z.,
RA   Cappai R.;
RT   "Quantification of copper binding to amyloid precursor protein domain 2 and
RT   its Caenorhabditis elegans ortholog. Implications for biological
RT   function.";
RL   Metallomics 6:105-116(2014).
CC   -!- FUNCTION: Required for normal developmental progression throughout all
CC       life stages (PubMed:18262516, PubMed:22466039). Specifically required
CC       for the molt stage during all larval transitions and morphogenesis
CC       (PubMed:18262516, PubMed:17267616, PubMed:22466039). Acts with
CC       heterochronic genes, including members of the let-7 family, to regulate
CC       larval stage to adult transition (PubMed:18262516, PubMed:28933985).
CC       Acts synergistically with acn-1 in let-7 regulated postembryonic cell
CC       division of hypodermal seam cells (PubMed:28933985). Acts in multiple
CC       pathways to influence daf-12 and daf-16 activity to in turn regulate
CC       physiological and reproductive processes such as body size and egg-
CC       laying (PubMed:22466039). May play a role in neurotransmission
CC       (PubMed:20862215). {ECO:0000269|PubMed:17267616,
CC       ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:20862215,
CC       ECO:0000269|PubMed:22466039, ECO:0000269|PubMed:28933985}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic domain) with feh-1 (via PID 2
CC       domain). {ECO:0000269|PubMed:11896189}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Early endosome
CC       {ECO:0000269|PubMed:20862215}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q10651-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q10651-2; Sequence=VSP_000017;
CC   -!- TISSUE SPECIFICITY: Expressed in the head, pharynx, spermatheca,
CC       uterus, vulva, tail and ventral neurons (PubMed:18262516). Specifically
CC       expressed in nerve ring interneurons, the ventral cord, socket and
CC       amphids in the head, with strong expression in junctional cells,
CC       including the pharyngeal intestinal valve and uterine seam junction,
CC       and the excretory cell and weak expression in epidermal epithelial
CC       cells, including hyp7 cells, vulval cells, rectal valve cells,
CC       pharyngeal arcade cells and the tail hypodermis (PubMed:20862215).
CC       {ECO:0000269|PubMed:17267616, ECO:0000269|PubMed:20862215}.
CC   -!- DEVELOPMENTAL STAGE: Similar expression pattern in larval and adult
CC       cells with expression in neuronal, muscle, hypodermal and supporting
CC       cells (PubMed:17267616). Temporally expressed in seam cells from the
CC       middle of larval stage L4 and throughout adult stages (PubMed:18262516,
CC       PubMed:28933985). {ECO:0000269|PubMed:17267616,
CC       ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:28933985}.
CC   -!- DOMAIN: The NPXY motif mediates the interaction with clathrin.
CC       {ECO:0000255}.
CC   -!- PTM: Extracellular region is proteolytically cleaved.
CC       {ECO:0000269|PubMed:17267616}.
CC   -!- DISRUPTION PHENOTYPE: Larval lethality during the L1 stage, with the
CC       formation of vacuoles in syncytial hypoderm, organ morphology defects,
CC       and molting defects (PubMed:17267616, PubMed:20862215). RNAi-mediated
CC       knockdown results in a reduced body size, transparent appearance,
CC       sluggish movement and insensitivity to touch (PubMed:18262516,
CC       PubMed:20862215). Delayed development and a molting defect that begins
CC       at the L3 to L4 larval stage transition and continues through to
CC       transition from the L4 larval stage to the young adult stage
CC       (PubMed:20862215). Increased sensitivity to acetylcholine inhibition
CC       (PubMed:20862215). Increased pharyngeal pumping (PubMed:11896189). In a
CC       let-7 mutant background, partial suppression of the let-7 bursting
CC       vulva phenotype (PubMed:28933985). Double RNAi-mediated knockdown with
CC       acn-1 in a let-7 mutant background leads to complete suppression of the
CC       heterochronic seam cell defects (PubMed:28933985).
CC       {ECO:0000269|PubMed:11896189, ECO:0000269|PubMed:17267616,
CC       ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:20862215,
CC       ECO:0000269|PubMed:28933985}.
CC   -!- MISCELLANEOUS: Lacks conserved metal-binding sites and has only weak
CC       affinity for copper in vitro. {ECO:0000269|PubMed:24276282}.
CC   -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01217}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC46470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; FO080659; CCD65568.1; -; Genomic_DNA.
DR   EMBL; FO080659; CCD65569.1; -; Genomic_DNA.
DR   EMBL; U00240; AAC46470.1; ALT_INIT; mRNA.
DR   PIR; T15795; T15795.
DR   RefSeq; NP_508870.3; NM_076469.5. [Q10651-1]
DR   RefSeq; NP_508871.1; NM_076470.4. [Q10651-2]
DR   PDB; 2M05; NMR; -; A=135-197.
DR   PDB; 3K66; X-ray; 2.70 A; A=240-478.
DR   PDB; 3K6B; X-ray; 2.80 A; A=240-478.
DR   PDBsum; 2M05; -.
DR   PDBsum; 3K66; -.
DR   PDBsum; 3K6B; -.
DR   BMRB; Q10651; -.
DR   SMR; Q10651; -.
DR   BioGRID; 45718; 4.
DR   DIP; DIP-25431N; -.
DR   STRING; 6239.C42D8.8a; -.
DR   iPTMnet; Q10651; -.
DR   EPD; Q10651; -.
DR   PaxDb; Q10651; -.
DR   PeptideAtlas; Q10651; -.
DR   EnsemblMetazoa; C42D8.8a.1; C42D8.8a.1; WBGene00000149. [Q10651-1]
DR   EnsemblMetazoa; C42D8.8b.1; C42D8.8b.1; WBGene00000149. [Q10651-2]
DR   GeneID; 180783; -.
DR   KEGG; cel:CELE_C42D8.8; -.
DR   UCSC; C42D8.8a; c. elegans. [Q10651-1]
DR   CTD; 180783; -.
DR   WormBase; C42D8.8a; CE04209; WBGene00000149; apl-1. [Q10651-1]
DR   WormBase; C42D8.8b; CE27845; WBGene00000149; apl-1. [Q10651-2]
DR   eggNOG; KOG3540; Eukaryota.
DR   GeneTree; ENSGT00530000063252; -.
DR   InParanoid; Q10651; -.
DR   OMA; IIDEPAS; -.
DR   OrthoDB; 953529at2759; -.
DR   PhylomeDB; Q10651; -.
DR   Reactome; R-CEL-114608; Platelet degranulation.
DR   Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-CEL-416476; G alpha (q) signalling events.
DR   Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-CEL-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   EvolutionaryTrace; Q10651; -.
DR   PRO; PR:Q10651; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000149; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.770; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.1490.140; -; 1.
DR   Gene3D; 3.90.570.10; -; 1.
DR   InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR   InterPro; IPR008155; Amyloid_glyco.
DR   InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR   InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR   InterPro; IPR008154; Amyloid_glyco_extra.
DR   InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR   InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR   InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR   InterPro; IPR019543; APP_amyloid_C.
DR   InterPro; IPR019744; APP_CUBD_CS.
DR   InterPro; IPR036176; E2_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR23103; PTHR23103; 1.
DR   Pfam; PF10515; APP_amyloid; 1.
DR   Pfam; PF12924; APP_Cu_bd; 1.
DR   Pfam; PF12925; APP_E2; 1.
DR   Pfam; PF02177; APP_N; 1.
DR   PRINTS; PR00203; AMYLOIDA4.
DR   SMART; SM00006; A4_EXTRA; 1.
DR   SUPFAM; SSF109843; SSF109843; 1.
DR   SUPFAM; SSF56491; SSF56491; 1.
DR   SUPFAM; SSF89811; SSF89811; 1.
DR   PROSITE; PS00319; APP_CUBD; 1.
DR   PROSITE; PS51869; APP_E1; 1.
DR   PROSITE; PS51870; APP_E2; 1.
DR   PROSITE; PS00320; APP_INTRA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amyloid; Developmental protein;
KW   Differentiation; Disulfide bond; Endosome; Glycoprotein; Membrane;
KW   Neurogenesis; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..686
FT                   /note="Amyloid-beta-like protein"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000000201"
FT   TOPO_DOM        22..621
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..686
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..197
FT                   /note="E1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DOMAIN          240..440
FT                   /note="E2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT   REGION          32..125
FT                   /note="GFLD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          133..197
FT                   /note="CuBD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          252..255
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MOTIF           674..679
FT                   /note="YENPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P05067"
FT   COMPBIAS        205..228
FT                   /note="Asp-rich"
FT   BINDING         382
FT                   /note="Heparin"
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        76..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        101..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        135..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT                   ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT   DISULFID        146..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT                   ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT   DISULFID        160..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT                   ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT   VAR_SEQ         538..539
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000017"
FT   MUTAGEN         252
FT                   /note="N->A: Reduced heparin binding."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         254
FT                   /note="H->A: Reduced heparin binding."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         254
FT                   /note="H->P: Reduced heparin binding."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         348
FT                   /note="D->C: Results in destabilized protein structure;
FT                   when associated with C-368 and K-377."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         368
FT                   /note="S->C: Results in destabilized protein structure;
FT                   when associated with C-348 and K-377."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         374
FT                   /note="R->A: Reduced heparin binding; when associated with
FT                   A-378."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         377
FT                   /note="E->K: In yn32: Results in lethality and destabilized
FT                   protein structure."
FT                   /evidence="ECO:0000269|PubMed:17267616,
FT                   ECO:0000269|PubMed:19906646"
FT   MUTAGEN         378
FT                   /note="K->A: Reduced heparin binding; when associated with
FT                   A-374."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   MUTAGEN         382
FT                   /note="H->A: Moderately reduced heparin binding."
FT                   /evidence="ECO:0000269|PubMed:19906646"
FT   STRAND          136..141
FT                   /evidence="ECO:0007744|PDB:2M05"
FT   HELIX           149..162
FT                   /evidence="ECO:0007744|PDB:2M05"
FT   STRAND          172..178
FT                   /evidence="ECO:0007744|PDB:2M05"
FT   STRAND          187..195
FT                   /evidence="ECO:0007744|PDB:2M05"
FT   HELIX           243..246
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           253..292
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           294..358
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           362..393
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           395..399
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           402..421
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   TURN            422..425
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   HELIX           427..430
FT                   /evidence="ECO:0007744|PDB:3K66"
FT   TURN            431..433
FT                   /evidence="ECO:0007744|PDB:3K6B"
FT   HELIX           434..448
FT                   /evidence="ECO:0007744|PDB:3K66"
SQ   SEQUENCE   686 AA;  79435 MW;  A0816858FDD48608 CRC64;
     MTVGKLMIGL LIPILVATVY AEGSPAGSKR HEKFIPMVAF SCGYRNQYMT EEGSWKTDDE
     RYATCFSGKL DILKYCRKAY PSMNITNIVE YSHEVSISDW CREEGSPCKW THSVRPYHCI
     DGEFHSEALQ VPHDCQFSHV NSRDQCNDYQ HWKDEAGKQC KTKKSKGNKD MIVRSFAVLE
     PCALDMFTGV EFVCCPNDQT NKTDVQKTKE DEDDDDDEDD AYEDDYSEES DEKDEEEPSS
     QDPYFKIANW TNEHDDFKKA EMRMDEKHRK KVDKVMKEWG DLETRYNEQK AKDPKGAEKF
     KSQMNARFQK TVSSLEEEHK RMRKEIEAVH EERVQAMLNE KKRDATHDYR QALATHVNKP
     NKHSVLQSLK AYIRAEEKDR MHTLNRYRHL LKADSKEAAA YKPTVIHRLR YIDLRINGTL
     AMLRDFPDLE KYVRPIAVTY WKDYRDEVSP DISVEDSELT PIIHDDEFSK NAKLDVKAPT
     TTAKPVKETD NAKVLPTEAS DSEEEADEYY EDEDDEQVKK TPDMKKKVKV VDIKPKEIKV
     TIEEEKKAPK LVETSVQTDD EDDDEDSSSS TSSESDEDED KNIKELRVDI EPIIDEPASF
     YRHDKLIQSP EVERSASSVF QPYVLASAMF ITAICIIAFA ITNARRRRAM RGFIEVDVYT
     PEERHVAGMQ VNGYENPTYS FFDSKA
//
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