GenomeNet

Database: UniProt
Entry: P15215
LinkDB: P15215
Original site: P15215 
ID   LAMC1_DROME             Reviewed;        1639 AA.
AC   P15215; Q24373; Q5BI30; Q9VT18;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   13-FEB-2019, entry version 182.
DE   RecName: Full=Laminin subunit gamma-1;
DE   AltName: Full=Laminin B2 chain;
DE   Flags: Precursor;
GN   Name=LanB2; Synonyms=LAMC1, LAMG1; ORFNames=CG3322;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Oregon-R;
RX   PubMed=2912972;
RA   Chi H.-C., Hui C.-F.;
RT   "Primary structure of the Drosophila laminin B2 chain and comparison
RT   with human, mouse, and Drosophila laminin B1 and B2 chains.";
RL   J. Biol. Chem. 264:1543-1550(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=2808533; DOI=10.1083/jcb.109.5.2441;
RA   Montell D.J., Goodman C.S.;
RT   "Drosophila laminin: sequence of B2 subunit and expression of all
RT   three subunits during embryogenesis.";
RL   J. Cell Biol. 109:2441-2453(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S, and Oregon-R;
RX   PubMed=1840513; DOI=10.1089/dna.1991.10.451;
RA   Chi H.-C., Juminaga D., Wang S.Y., Hui C.-F.;
RT   "Structure of the Drosophila gene for the laminin B2 chain.";
RL   DNA Cell Biol. 10:451-466(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 344-1639.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=3405777; DOI=10.1093/nar/16.14.7205;
RA   Chi H.-C., Hui C.-F.;
RT   "cDNA and amino acid sequences of Drosophila laminin B2 chain.";
RL   Nucleic Acids Res. 16:7205-7206(1988).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI and IV are globular.
DR   EMBL; M58417; AAA28665.1; -; Genomic_DNA.
DR   EMBL; M25063; AAA28664.1; -; mRNA.
DR   EMBL; AE014296; AAF50238.1; -; Genomic_DNA.
DR   EMBL; BT021394; AAX33542.1; -; mRNA.
DR   PIR; A31483; MMFFB2.
DR   RefSeq; NP_001287009.1; NM_001300080.1.
DR   RefSeq; NP_524006.1; NM_079282.2.
DR   UniGene; Dm.2551; -.
DR   ProteinModelPortal; P15215; -.
DR   SMR; P15215; -.
DR   BioGrid; 64509; 14.
DR   DIP; DIP-21994N; -.
DR   IntAct; P15215; 12.
DR   STRING; 7227.FBpp0076111; -.
DR   PaxDb; P15215; -.
DR   PRIDE; P15215; -.
DR   EnsemblMetazoa; FBtr0076382; FBpp0076111; FBgn0267348.
DR   EnsemblMetazoa; FBtr0345031; FBpp0311281; FBgn0267348.
DR   GeneID; 39118; -.
DR   KEGG; dme:Dmel_CG3322; -.
DR   CTD; 39118; -.
DR   FlyBase; FBgn0267348; LanB2.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410XRDC; LUCA.
DR   HOGENOM; HOG000264193; -.
DR   InParanoid; P15215; -.
DR   KO; K05635; -.
DR   OMA; FYSATCR; -.
DR   OrthoDB; 156553at2759; -.
DR   PhylomeDB; P15215; -.
DR   Reactome; R-DME-3000157; Laminin interactions.
DR   GenomeRNAi; 39118; -.
DR   PRO; PR:P15215; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0267348; Expressed in 35 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila).
DR   ExpressionAtlas; P15215; baseline and differential.
DR   Genevisible; P15215; DM.
DR   GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR   GO; GO:0070831; P:basement membrane assembly; IMP:FlyBase.
DR   GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR   GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:FlyBase.
DR   GO; GO:0085029; P:extracellular matrix assembly; IMP:FlyBase.
DR   GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 11.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 11.
DR   PROSITE; PS50027; EGF_LAM_2; 11.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   2: Evidence at transcript level;
KW   Basement membrane; Cell adhesion; Coiled coil; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34   1639       Laminin subunit gamma-1.
FT                                /FTId=PRO_0000017081.
FT   DOMAIN       63    298       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      299    358       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      359    413       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      414    460       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      461    513       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      514    523       Laminin EGF-like 5; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      533    709       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN      710    743       Laminin EGF-like 5; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      744    792       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      793    846       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      847    901       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      902    955       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      956   1003       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1004   1049       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1050   1609       Domain II and I.
FT   COILED     1087   1109       {ECO:0000255}.
FT   COILED     1144   1247       {ECO:0000255}.
FT   COILED     1306   1627       {ECO:0000255}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    376    376       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    862    862       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    965    965       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1070   1070       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1156   1156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1394   1394       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1479   1479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1584   1584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    299    308       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    301    322       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    324    333       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    336    356       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    359    368       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    361    384       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    387    396       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    399    411       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    414    426       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    416    432       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    434    443       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    446    458       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    461    475       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    463    482       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    484    493       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    496    511       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    712    721       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    724    741       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    744    753       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    746    760       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    762    771       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    774    790       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    793    801       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    795    811       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    814    823       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    826    844       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    847    861       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    849    868       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    871    880       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    883    899       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    902    919       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    904    926       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    928    937       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    940    953       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    956    968       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    958    975       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    977    986       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    989   1001       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1004   1016       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1006   1022       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1024   1033       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1036   1047       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1050   1050       Interchain. {ECO:0000305}.
FT   DISULFID   1053   1053       Interchain. {ECO:0000305}.
FT   DISULFID   1631   1631       Interchain. {ECO:0000305}.
FT   VARIANT     831    831       F -> Y.
FT   VARIANT     892    892       L -> P (in strain: Oregon-R).
FT   CONFLICT   1026   1027       DN -> EY (in Ref. 1). {ECO:0000305}.
SQ   SEQUENCE   1639 AA;  182339 MW;  8F510AC6933A52BC CRC64;
     MKRSRWSHSG SSTARLLLIG VLFASCSTAI LGAQRPPINS AGGHELRGTT FMPALECYDP
     YGRPQKCLPE FINAAYQLQI ESTNTCGEQN DNHFCIQTMN QNHKNCEFCK YNDHNPSFLT
     DLHDPQSPTW WQSETMFEGI QHPNYVNLTL HLGKSYDITY VRILFRSPRP ESFTIYKRTS
     ESGPWIPYQF YSATCRDTYS LPDSRAIRKG EGEAHALCTS EYSDISPLRD GEIAFSTLEG
     RPSGINFERS GELQEWVTAT DIRITLDRLN TFGDELFGDS QVLKSYFYAI SDIAVGARCK
     CNGHASKCVP STGMHGERTL VCECRHNTDG PDCDRCLPLY NDLKWKRSTS TEVNECKACN
     CNGLADKCFF DANLFNRTGH GGHCLDCREN RDGPNCERCK ENFYMRDDGY CVNCACDPVG
     SRSLQCNSHG KCQCKPGVTG DKCDRCDNNY YQFGPHGCQQ CGCDSGGSHQ NTPACDTETG
     ICFCKENVEG RRCNECKPGF FNLDKNNRFG CTPCFCYGHT SECMTAPGYS IVSVTSNFNK
     FKERWTAADL NQREVDIKYN QYSRSIGTTA QGNEHVYFQA PDRFLGDQRA SYNRDLKFKL
     QLVGQVANTG VSDVILEGAG SRISLPIFAQ GNGIPDQGVK EYTFRLHEHH DYQWQPSQSA
     RGFLSILSNL TAIKIRATYS VQGEAILDDV ELQTAHRGAA GHPATWIEQC TCPEGYLGQF
     CESCAPGYRH SPARGGPFMP CIPCDCHGHA DICDSETGRC ICQHNTHGDN CDQCAKGFYG
     NALGGTPNDC KRCPCPNDGA CLQINEDTVI CTECPKGYFG SRCEQCSDGF FGDPTGLLGE
     VQTCKSCDCN GNVDPNAVGN CNRTTGECLK CIHNTAGEHC DQCLSGHFGD PLALPHGRCD
     RCSCYEAGTE QDEQSITRCD QVTGQCQCKP NVIGRDCGEC QPGYFNIRSG NGCENCLCDP
     VGSYNSTCDR YSGQCHCRPG VMGQRCDQCE NYFYGFSSEG CKPCECDESG SKGFQCDQNG
     QCPCNDNVEG RRCDRCKENK YDRHRGCIDC PDCYNLVQDA ADLHRAKLFN LSQTLDEIAR
     TPVTNDDEFE AKLKAVQEKV AVLAQDARDN SGDGGQTYAE VIDDLHKHLD SVREHLVSAD
     KFQADANGEI DRARQNYTIL DQITENAKKE LQQALDLLND EGAQALARAK EKSVEFGQQS
     EQISDISREA RALADKLESE AQFDLKNAKD AKDAVEKAHQ LAKSAIDLQL KIGTELRSEV
     GLELSHVKQS LGTVVQTSKE ALRKANEVYD TALTLLNDVN RQTQPEIDIS QLKKDAVAAN
     ERADELLKQI TELSNSNGEL FADFETEQEL TEALLKRAEQ QQLEDIELLE RAKAAHDKAT
     KAVEQGDNTL KEANNTYEKL AGFQSDVQRS SESAEKALQT VPNIEKEIQN AESLISQAEE
     ALDGANKNAN EAKKNAQEAQ LKYAEQASKD AELIRRKANE TKVAARNLRE EADQLNHRVK
     LTEMDIFKLE ESSTKDDNLV DDAKRKVGQA KADTQEAQKQ IEKANADLTA IKDELENLKD
     INTGDLDRLE NRLATVEGEI NRVNLTGRIE KYREQRTIQK NLIDKYDAEL RELKDEVQNI
     GLISKALPDS CFSRNRLEP
//
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