GenomeNet

Database: UniProt
Entry: Q61072
LinkDB: Q61072
Original site: Q61072 
ID   ADAM9_MOUSE             Reviewed;         845 AA.
AC   Q61072; E9QPP2; Q60618; Q61853; Q80U94;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   16-JAN-2019, entry version 157.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
DE            Short=ADAM 9;
DE            EC=3.4.24.-;
DE   AltName: Full=Meltrin-gamma;
DE   AltName: Full=Metalloprotease/disintegrin/cysteine-rich protein 9;
DE   AltName: Full=Myeloma cell metalloproteinase;
DE   Flags: Precursor;
GN   Name=Adam9 {ECO:0000312|MGI:MGI:105376};
GN   Synonyms=Kiaa0021 {ECO:0000312|EMBL:BAC65470.1}, Mdc9, Mltng;
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].
RC   TISSUE=Lung;
RX   PubMed=8647900; DOI=10.1083/jcb.132.4.717;
RA   Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.;
RT   "MDC9, a widely expressed cellular disintegrin containing cytoplasmic
RT   SH3 ligand domains.";
RL   J. Cell Biol. 132:717-726(1996).
RN   [2] {ECO:0000312|EMBL:BAC65470.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC65470.1};
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; 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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 426-575.
RX   PubMed=7566181; DOI=10.1038/377652a0;
RA   Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.,
RA   Fujisawa-Sehara A.;
RT   "A metalloprotease-disintegrin participating in myoblast fusion.";
RL   Nature 377:652-656(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 432-478.
RC   STRAIN=BALB/cJ;
RX   PubMed=8146185; DOI=10.1073/pnas.91.7.2748;
RA   Weskamp G., Blobel C.P.;
RT   "A family of cellular proteins related to snake venom disintegrins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2748-2751(1994).
RN   [7]
RP   FUNCTION, PHOSPHORYLATION, ACTIVITY REGULATION, AND PROTEIN SEQUENCE
RP   OF 206-212.
RX   PubMed=9920899; DOI=10.1074/jbc.274.6.3531;
RA   Roghani M., Becherer J.D., Moss M.L., Atherton R.E.,
RA   Erdjument-Bromage H., Arribas J., Blackburn R.K., Weskamp G.,
RA   Tempst P., Blobel C.P.;
RT   "Metalloprotease-disintegrin MDC9: intracellular maturation and
RT   catalytic activity.";
RL   J. Biol. Chem. 274:3531-3540(1999).
RN   [8]
RP   INTERACTION WITH SH3GL2 AND SNX9.
RX   PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA   Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT   "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
RT   two SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL   J. Biol. Chem. 274:31693-31699(1999).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH ITGA6.
RX   PubMed=10825303;
RA   Nath D., Slocombe P.M., Webster A., Stephens P.E., Docherty A.J.,
RA   Murphy G.;
RT   "Meltrin gamma(ADAM-9) mediates cellular adhesion through
RT   alpha(6)beta(1)integrin, leading to a marked induction of fibroblast
RT   cell motility.";
RL   J. Cell Sci. 113:2319-2328(2000).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11839819; DOI=10.1128/MCB.22.5.1537-1544.2002;
RA   Weskamp G., Cai H., Brodie T.A., Higashyama S., Manova K., Ludwig T.,
RA   Blobel C.P.;
RT   "Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no
RT   evident major abnormalities during development or adult life.";
RL   Mol. Cell. Biol. 22:1537-1544(2002).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19409519; DOI=10.1016/j.ajhg.2009.04.005;
RA   Parry D.A., Toomes C., Bida L., Danciger M., Towns K.V., McKibbin M.,
RA   Jacobson S.G., Logan C.V., Ali M., Bond J., Chance R., Swendeman S.,
RA   Daniele L.L., Springell K., Adams M., Johnson C.A., Booth A.P.,
RA   Jafri H., Rashid Y., Banin E., Strom T.M., Farber D.B., Sharon D.,
RA   Blobel C.P., Pugh E.N. Jr., Pierce E.A., Inglehearn C.F.;
RT   "Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in
RT   humans and retinal degeneration in mice.";
RL   Am. J. Hum. Genet. 84:683-691(2009).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF GLU-348.
RX   PubMed=19273593; DOI=10.1128/MCB.01460-08;
RA   Guaiquil V., Swendeman S., Yoshida T., Chavala S., Campochiaro P.A.,
RA   Blobel C.P.;
RT   "ADAM9 is involved in pathological retinal neovascularization.";
RL   Mol. Cell. Biol. 29:2694-2703(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, 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   [14]
RP   MUTAGENESIS OF ARG-53; ARG-56; ARG-202 AND ARG-205, SUBCELLULAR
RP   LOCATION, AND ACTIVITY REGULATION.
RX   PubMed=25795784; DOI=10.1074/jbc.M114.624072;
RA   Wong E., Maretzky T., Peleg Y., Blobel C.P., Sagi I.;
RT   "The functional maturation of a disintegrin and metalloproteinase
RT   (ADAM) 9, 10, and 17 requires processing at a newly identified
RT   proprotein convertase (PC) cleavage site.";
RL   J. Biol. Chem. 290:12135-12146(2015).
CC   -!- FUNCTION: Cleaves and releases a number of molecules with
CC       important roles in tumorigenesis and angiogenesis, such as TEK,
CC       KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593). May mediate
CC       cell-cell, cell-matrix interactions and regulate the motility of
CC       cells via interactions with integrins (PubMed:10825303).
CC       {ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:19273593}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- ACTIVITY REGULATION: Synthesized as an inactive form which is
CC       proteolytically cleaved to generate an active enzyme. Processing
CC       at the upstream site is particularly important for activation of
CC       the proenzyme, whereas processing at the boundary between the pro-
CC       domain and the catalytic domain does not appear to be essential
CC       (PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors
CC       (PubMed:9920899). {ECO:0000269|PubMed:25795784,
CC       ECO:0000269|PubMed:9920899}.
CC   -!- SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic
CC       tail (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303).
CC       {ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:10825303}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784,
CC       ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC   -!- PTM: Proteolytically cleaved in the trans-Golgi network before it
CC       reaches the plasma membrane to generate a mature protein. The
CC       removal of the pro-domain occurs via cleavage at two different
CC       sites. Processed most likely by a pro-protein convertase such as
CC       furin, at the boundary between the pro-domain and the catalytic
CC       domain. An additional upstream cleavage pro-protein convertase
CC       site (Arg-56/Glu-57) has an important role in the activation of
CC       ADAM9. {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.
CC   -!- PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-
CC       13-acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice appear to develop normally,
CC       are viable and fertile, and do not have any major pathological
CC       phenotypes (PubMed:11839819). In adulthood, 20 months after birth,
CC       mice display progressive retinal degeneration, disorganized
CC       retinal layers and a degenerate retinal pigment epithelium
CC       (PubMed:19409519). {ECO:0000269|PubMed:11839819,
CC       ECO:0000269|PubMed:19409519}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65470.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; U41765; AAC52446.1; -; mRNA.
DR   EMBL; AK122188; BAC65470.1; ALT_INIT; mRNA.
DR   EMBL; AC156553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047156; AAH47156.1; -; mRNA.
DR   EMBL; D50412; BAA08913.1; -; mRNA.
DR   EMBL; U06145; AAA18424.1; -; mRNA.
DR   PIR; I48943; I48943.
DR   PIR; S60259; S60259.
DR   RefSeq; NP_031430.2; NM_007404.2.
DR   UniGene; Mm.28908; -.
DR   ProteinModelPortal; Q61072; -.
DR   SMR; Q61072; -.
DR   BioGrid; 197973; 1.
DR   IntAct; Q61072; 3.
DR   STRING; 10090.ENSMUSP00000081048; -.
DR   MEROPS; M12.209; -.
DR   iPTMnet; Q61072; -.
DR   PhosphoSitePlus; Q61072; -.
DR   EPD; Q61072; -.
DR   MaxQB; Q61072; -.
DR   PaxDb; Q61072; -.
DR   PRIDE; Q61072; -.
DR   Ensembl; ENSMUST00000084035; ENSMUSP00000081048; ENSMUSG00000031555.
DR   GeneID; 11502; -.
DR   KEGG; mmu:11502; -.
DR   UCSC; uc009lfk.2; mouse.
DR   CTD; 8754; -.
DR   MGI; MGI:105376; Adam9.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000156239; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q61072; -.
DR   KO; K06834; -.
DR   OrthoDB; 162519at2759; -.
DR   TreeFam; TF314733; -.
DR   BRENDA; 3.4.24.B9; 3474.
DR   PRO; PR:Q61072; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000031555; Expressed in 289 organ(s), highest expression level in endothelial cell of lymphatic vessel.
DR   ExpressionAtlas; Q61072; baseline and differential.
DR   Genevisible; Q61072; MM.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IMP:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:BHF-UCL.
DR   GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR   GO; GO:0042117; P:monocyte activation; ISO:MGI.
DR   GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; ISO:MGI.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISO:MGI.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:MGI.
DR   GO; GO:0034241; P:positive regulation of macrophage fusion; ISO:MGI.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR   GO; GO:0051384; P:response to glucocorticoid; IMP:BHF-UCL.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR   GO; GO:0010042; P:response to manganese ion; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
KW   Zymogen.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30    845       Disintegrin and metalloproteinase domain-
FT                                containing protein 9.
FT                                /FTId=PRO_0000029063.
FT   TOPO_DOM     30    697       Extracellular. {ECO:0000255}.
FT   TRANSMEM    698    718       Helical. {ECO:0000255}.
FT   TOPO_DOM    719    845       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      212    406       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      414    501       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      644    698       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    505    634       Cys-rich.
FT   ACT_SITE    348    348       {ECO:0000250|UniProtKB:P78536,
FT                                ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       347    347       Zinc; catalytic. {ECO:0000250}.
FT   METAL       351    351       Zinc; catalytic. {ECO:0000250}.
FT   METAL       357    357       Zinc; catalytic. {ECO:0000250}.
FT   SITE         56     57       Cleavage. {ECO:0000305|PubMed:25795784}.
FT   SITE        205    206       Cleavage; by furin-like protease.
FT                                {ECO:0000269|PubMed:9920899}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    154    154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    231    231       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    381    381       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    487    487       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    636    636       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    322    401       {ECO:0000250}.
FT   DISULFID    363    385       {ECO:0000250|UniProtKB:P78536}.
FT   DISULFID    365    370       {ECO:0000250}.
FT   DISULFID    473    493       {ECO:0000250}.
FT   DISULFID    644    656       {ECO:0000250}.
FT   DISULFID    650    662       {ECO:0000250}.
FT   DISULFID    664    673       {ECO:0000250}.
FT   MUTAGEN      53     53       R->A: Reduces the shedding activity; when
FT                                associated with A-56. Does not prevent
FT                                pro-domain processing between the
FT                                pro- and metalloprotease domain; when
FT                                associated with A-56.
FT                                {ECO:0000269|PubMed:25795784}.
FT   MUTAGEN      56     56       R->A: Reduces the shedding activity; when
FT                                associated with A-56. Does not prevent
FT                                pro-domain processing between the
FT                                pro- and metalloprotease domain; when
FT                                associated with A-56.
FT                                {ECO:0000269|PubMed:25795784}.
FT   MUTAGEN     202    202       R->A: Does not affect shedding activity;
FT                                when associated with A-205.
FT                                {ECO:0000269|PubMed:25795784}.
FT   MUTAGEN     205    205       R->A: Does not affect shedding activity;
FT                                when associated with A-203.
FT                                {ECO:0000269|PubMed:25795784}.
FT   MUTAGEN     348    348       E->A: Abolishes catalytic activity.
FT                                {ECO:0000269|PubMed:19273593}.
FT   CONFLICT    296    296       W -> R (in Ref. 1; AAC52446, 2; BAC65470
FT                                and 4; AAH47156). {ECO:0000305}.
SQ   SEQUENCE   845 AA;  92079 MW;  38C40F89D4A77725 CRC64;
     MGPRALSPLA SLRLRWLLAC GLLGPVLEAG RPDLEQTVHL SSYEIITPWR LTRERREALG
     PSSQQISYVI QAQGKQHIIH LERNTDLLPN DFVVYTYDKE GSLLSDHPNV QSHCHYRGYV
     EGVQNSAVAV SACFGLRGLL HLENASFGIE PLHNSSHFEH IFYPMDGIHQ EPLRCGVSNR
     DTEKEGTQGD EEEHPSVTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
     RLANYLDSMY IMLNIRIVLV GLEIWTDRNP INIIGGAGDV LGNFVQWREK FLITRWRHDS
     AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
     RECFCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGS CLLNIPKPDE AYSAPSCGNK
     LVDPGEECDC GTAKECEVDP CCEGSTCKLK SFAECAYGDC CKDCQFLPGG SMCRGKTSEC
     DVPEYCNGSS QFCPPDVFIQ NGYPCQNSKA YCYNGMCQYY DAQCQVIFGS KAKAAPRDCF
     IEVNSKGDRF GNCGFSGSEY KKCATGNALC GKLQCENVQD MPVFGIVPAI IQTPSRGTKC
     WGVDFQLGSD VPDPGMVNEG TKCDAGKICR NFQCVNASVL NYDCDIQGKC HGHGVCNSNK
     NCHCEDGWAP PHCDTKGYGG SVDSGPTYNA KSTALRDGLL VFFFLIVPLV AAAIFLFIKR
     DELRKTFRKK RSQMSDGRNQ ANVSRQPGDP SISRPPGGPN VSRPPGGPGV SRPPGGPGVS
     RPPGGPGVSR PPPGHGNRFP VPTYAAKQPA QFPSRPPPPQ PKISSQGNLI PARPAPAPPL
     YSSLT
//
DBGET integrated database retrieval system