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Database: UniProt/SWISS-PROT
Entry: ACE_MOUSE
LinkDB: ACE_MOUSE
Original site: ACE_MOUSE 
ID   ACE_MOUSE               Reviewed;        1312 AA.
AC   P09470; P22967; Q6GTS2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 3.
DT   25-OCT-2017, entry version 171.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            Short=ACE;
DE            EC=3.2.1.-;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   AltName: CD_antigen=CD143;
DE   Contains:
DE     RecName: Full=Angiotensin-converting enzyme, soluble form;
DE   Flags: Precursor;
GN   Name=Ace; Synonyms=Dcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
RX   PubMed=2545691;
RA   Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A.;
RT   "Mouse angiotensin-converting enzyme is a protein composed of two
RT   homologous domains.";
RL   J. Biol. Chem. 264:11945-11951(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2164636; DOI=10.1128/MCB.10.8.4294;
RA   Howard T.E., Shai S.-Y., Langford K.G., Martin B.M., Bernstein K.E.;
RT   "Transcription of testicular angiotensin-converting enzyme (ACE) is
RT   initiated within the 12th intron of the somatic ACE gene.";
RL   Mol. Cell. Biol. 10:4294-4302(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-332 (ISOFORM SOMATIC), AND PARTIAL
RP   PROTEIN SEQUENCE.
RX   PubMed=2841312;
RA   Bernstein K.E., Martin B.M., Bernstein E.A., Linton J., Striker L.,
RA   Striker G.;
RT   "The isolation of angiotensin-converting enzyme cDNA.";
RL   J. Biol. Chem. 263:11021-11024(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 35-54.
RC   TISSUE=Kidney;
RX   PubMed=2835538; DOI=10.1038/ki.1988.48;
RA   Bernstein K.E., Martin B.M., Striker L., Striker G.;
RT   "Partial protein sequence of mouse and bovine kidney angiotensin
RT   converting enzyme.";
RL   Kidney Int. 33:652-655(1988).
RN   [6]
RP   FUNCTION.
RX   PubMed=7753170; DOI=10.1038/375146a0;
RA   Krege J.H., John S.W., Langenbach L.L., Hodgin J.B., Hagaman J.R.,
RA   Bachman E.S., Jennette J.C., O'Brien D.A., Smithies O.;
RT   "Male-female differences in fertility and blood pressure in ACE-
RT   deficient mice.";
RL   Nature 375:146-148(1995).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8642790;
RA   Esther C.R. Jr., Howard T.E., Marino E.M., Goddard J.M.,
RA   Capecchi M.R., Bernstein K.E.;
RT   "Mice lacking angiotensin-converting enzyme have low blood pressure,
RT   renal pathology, and reduced male fertility.";
RL   Lab. Invest. 74:953-965(1996).
RN   [8]
RP   FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF HIS-993; GLU-994 AND
RP   HIS-997.
RX   PubMed=15665832; DOI=10.1038/nm1179;
RA   Kondoh G., Tojo H., Nakatani Y., Komazawa N., Murata C., Yamagata K.,
RA   Maeda Y., Kinoshita T., Okabe M., Taguchi R., Takeda J.;
RT   "Angiotensin-converting enzyme is a GPI-anchored protein releasing
RT   factor crucial for fertilization.";
RL   Nat. Med. 11:160-166(2005).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23535237; DOI=10.1152/ajpcell.00364.2012;
RA   Xiao L., Haack K.K., Zucker I.H.;
RT   "Angiotensin II regulates ACE and ACE2 in neurons through p38 mitogen-
RT   activated protein kinase and extracellular signal-regulated kinase 1/2
RT   signaling.";
RL   Am. J. Physiol. 304:C1073-C1079(2013).
CC   -!- FUNCTION: Converts angiotensin I to angiotensin II by release of
CC       the terminal His-Leu, this results in an increase of the
CC       vasoconstrictor activity of angiotensin. Also able to inactivate
CC       bradykinin, a potent vasodilator. Has also a glycosidase activity
CC       which releases GPI-anchored proteins from the membrane by cleaving
CC       the mannose linkage in the GPI moiety. This GPIase activity seems
CC       to be crucial for the egg-binding ability of the sperm.
CC       {ECO:0000269|PubMed:15665832, ECO:0000269|PubMed:7753170,
CC       ECO:0000269|PubMed:8642790}.
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
CC       oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
CC       Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
CC       with increase in vasoconstrictor activity, but no action on
CC       angiotensin II.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only
CC       binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC       Note=Binds 3 chloride ions per subunit. {ECO:0000250};
CC   -!- ENZYME REGULATION: Peptidase activity is specifically inhibited by
CC       lisinopril, captopril and enalaprilat. In contrast, GPIase
CC       activity is nearly insensitive to captopril.
CC       {ECO:0000269|PubMed:15665832}.
CC   -!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
CC       Secreted {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:23535237}.
CC       Cytoplasm {ECO:0000269|PubMed:23535237}. Note=Detected in both
CC       cell membrane and cytoplasm in neurons.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Somatic;
CC         IsoId=P09470-1; Sequence=Displayed;
CC       Name=Testis-specific; Synonyms=ACE-T;
CC         IsoId=P09470-2, P22967-1;
CC         Sequence=VSP_037638, VSP_037639;
CC   -!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
CC       spermatocytes, adult testis.
CC   -!- INDUCTION: Expression is thought to be subject to hormonal
CC       regulation by androgens.
CC   -!- PTM: Phosphorylated by CK2 on Ser-1305; which allows membrane
CC       retention. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Low blood pressure, elevated serum
CC       potassium, anemia, and renal defects. Male mice have reduced
CC       fertility. {ECO:0000269|PubMed:8642790}.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
DR   EMBL; J04946; AAA37147.1; -; mRNA.
DR   EMBL; J04947; AAA37148.1; -; mRNA.
DR   EMBL; M55333; AAA37149.1; -; mRNA.
DR   EMBL; M61094; AAA37150.1; -; Genomic_DNA.
DR   EMBL; BC040404; AAH40404.1; -; mRNA.
DR   EMBL; J03940; AAA37146.1; -; mRNA.
DR   CCDS; CCDS25543.1; -. [P09470-1]
DR   CCDS; CCDS25544.1; -. [P09470-2]
DR   PIR; A34171; A34171.
DR   PIR; A35655; A35655.
DR   RefSeq; NP_033728.1; NM_009598.2. [P09470-2]
DR   RefSeq; NP_997507.1; NM_207624.5. [P09470-1]
DR   UniGene; Mm.754; -.
DR   ProteinModelPortal; P09470; -.
DR   SMR; P09470; -.
DR   BioGrid; 197920; 1.
DR   IntAct; P09470; 3.
DR   MINT; MINT-4086662; -.
DR   STRING; 10090.ENSMUSP00000001963; -.
DR   BindingDB; P09470; -.
DR   ChEMBL; CHEMBL2994; -.
DR   MEROPS; M02.001; -.
DR   iPTMnet; P09470; -.
DR   PhosphoSitePlus; P09470; -.
DR   PaxDb; P09470; -.
DR   PeptideAtlas; P09470; -.
DR   PRIDE; P09470; -.
DR   Ensembl; ENSMUST00000001963; ENSMUSP00000001963; ENSMUSG00000020681. [P09470-1]
DR   Ensembl; ENSMUST00000001964; ENSMUSP00000001964; ENSMUSG00000020681. [P09470-2]
DR   GeneID; 11421; -.
DR   KEGG; mmu:11421; -.
DR   UCSC; uc007lxu.2; mouse. [P09470-1]
DR   UCSC; uc007lxw.2; mouse. [P09470-2]
DR   CTD; 1636; -.
DR   MGI; MGI:87874; Ace.
DR   eggNOG; KOG3690; Eukaryota.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   GeneTree; ENSGT00520000055576; -.
DR   HOGENOM; HOG000007838; -.
DR   HOVERGEN; HBG000264; -.
DR   InParanoid; P09470; -.
DR   KO; K01283; -.
DR   OMA; VTMEQLF; -.
DR   OrthoDB; EOG091G033S; -.
DR   PhylomeDB; P09470; -.
DR   TreeFam; TF312861; -.
DR   Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   PRO; PR:P09470; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020681; -.
DR   ExpressionAtlas; P09470; baseline and differential.
DR   Genevisible; P09470; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISO:MGI.
DR   GO; GO:0031711; F:bradykinin receptor binding; ISO:MGI.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR   GO; GO:0008144; F:drug binding; ISO:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR   GO; GO:0008238; F:exopeptidase activity; ISO:MGI.
DR   GO; GO:0070573; F:metallodipeptidase activity; ISO:MGI.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR   GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; ISO:MGI.
DR   GO; GO:0050482; P:arachidonic acid secretion; ISO:MGI.
DR   GO; GO:0071838; P:cell proliferation in bone marrow; IMP:BHF-UCL.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:1903597; P:negative regulation of gap junction assembly; IMP:BHF-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0032091; P:negative regulation of protein binding; IMP:BHF-UCL.
DR   GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR   GO; GO:0043171; P:peptide catabolic process; ISO:MGI.
DR   GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; IMP:BHF-UCL.
DR   GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IMP:BHF-UCL.
DR   GO; GO:0032092; P:positive regulation of protein binding; IMP:BHF-UCL.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IDA:BHF-UCL.
DR   GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   CDD; cd06461; M2_ACE; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 2.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carboxypeptidase; Cell membrane;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     34       {ECO:0000269|PubMed:2835538}.
FT   CHAIN        35   1312       Angiotensin-converting enzyme.
FT                                /FTId=PRO_0000028539.
FT   CHAIN        35   1237       Angiotensin-converting enzyme, soluble
FT                                form.
FT                                /FTId=PRO_0000028540.
FT   PROPEP     1238   1312       Removed in secreted form. {ECO:0000250}.
FT                                /FTId=PRO_0000028541.
FT   TOPO_DOM     35   1264       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1265   1281       Helical. {ECO:0000255}.
FT   TOPO_DOM   1282   1312       Cytoplasmic. {ECO:0000255}.
FT   REGION       35    635       Peptidase M2 1.
FT   REGION      636   1237       Peptidase M2 2.
FT   ACT_SITE    396    396       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   ACT_SITE    994    994       2.
FT   METAL       395    395       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       399    399       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       423    423       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       993    993       Zinc 2; catalytic.
FT   METAL       997    997       Zinc 2; catalytic.
FT   METAL      1021   1021       Zinc 2; catalytic. {ECO:0000250}.
FT   BINDING     236    236       Chloride 1. {ECO:0000250}.
FT   BINDING     534    534       Chloride 1. {ECO:0000250}.
FT   BINDING     796    796       Chloride 2. {ECO:0000250}.
FT   BINDING     834    834       Chloride 3. {ECO:0000250}.
FT   BINDING    1095   1095       Chloride 2. {ECO:0000250}.
FT   BINDING    1099   1099       Chloride 2. {ECO:0000250}.
FT   BINDING    1132   1132       Chloride 3. {ECO:0000250}.
FT   MOD_RES    1305   1305       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD     59     59       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16944957}.
FT   CARBOHYD    165    165       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    323    323       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    682    682       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    700    700       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000250}.
FT   CARBOHYD    719    719       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000250}.
FT   CARBOHYD    765    765       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    947    947       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1196   1196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    162    170       {ECO:0000250}.
FT   DISULFID    762    768       {ECO:0000250}.
FT   DISULFID    962    980       {ECO:0000250}.
FT   DISULFID   1148   1160       {ECO:0000250}.
FT   VAR_SEQ       1    580       Missing (in isoform Testis-specific).
FT                                {ECO:0000303|PubMed:2164636}.
FT                                /FTId=VSP_037638.
FT   VAR_SEQ     581    646       GCSRPWQEVLKDLVGSDALDAKALLEYFQPVSQWLEEQNQR
FT                                NGEVLGWPENQWRPPLPDNYPEGID -> MGQGWATPGLPS
FT                                FLFLLLCCGHHLLVLSQVATDHVTANQGITNQATTRSQTTT
FT                                HQATIDQTTQIPN (in isoform Testis-
FT                                specific). {ECO:0000303|PubMed:2164636}.
FT                                /FTId=VSP_037639.
FT   MUTAGEN     993    993       H->K: Abolishes peptidase activity but no
FT                                effect on GPIase activity; when
FT                                associated with K-997.
FT                                {ECO:0000269|PubMed:15665832}.
FT   MUTAGEN     994    994       E->D: Abolishes peptidase activity but no
FT                                effect on GPIase activity.
FT                                {ECO:0000269|PubMed:15665832}.
FT   MUTAGEN     997    997       H->K: Abolishes peptidase activity but no
FT                                effect on GPIase activity; when
FT                                associated with K-993.
FT                                {ECO:0000269|PubMed:15665832}.
FT   CONFLICT    568    568       A -> T (in Ref. 1; AAA37147).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1312 AA;  150918 MW;  7DF9F5BE91762DFF CRC64;
     MGAASGQRGR WPLSPPLLML SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG AQLFAESYNS
     SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE VWGKKAKELY ESIWQNFTDS
     KLRRIIGSIR TLGPANLPLA QRQQYNSLLS NMSRIYSTGK VCFPNKTATC WSLDPELTNI
     LASSRSYAKL LFAWEGWHDA VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS
     FEESLEHIYH QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD
     MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE SMLEKPTDGR
     EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV QYYLQYKDLH VSLRRGANPG
     FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN DIESDINYLL KMALEKIAFL PFGYLVDQWR
     WGVFSGRTPP SRYNFDWWYL RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV
     LQFQFHQALC KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD
     AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD EAKADRFVEE
     YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN HTLKYGTRAK TFDVSNFQNS
     SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL DMETTYSLSN ICYTNGTCMP LEPDLTNMMA
     TSRKYEELLW AWKSWRDKVG RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE
     QDLEKLYQEL QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV
     APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM LEKPTDGREV
     VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY FMQYKDLPVT FREGANPGFH
     EAIGDIMALS VSTPKHLYSL NLLSTEGSGY EYDINFLMKM ALDKIAFIPF SYLIDQWRWR
     VFDGSITKEN YNQEWWSLRL KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ
     FQFHEALCRA AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS
     AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF LGLYLEPQQA
     RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG PQFGSEVELR HS
//
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