GenomeNet

Database: UniProt
Entry: Q9Y6N6
LinkDB: Q9Y6N6
Original site: Q9Y6N6 
ID   LAMC3_HUMAN             Reviewed;        1575 AA.
AC   Q9Y6N6; B1APX9; B1APY0; Q59H72;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   10-APR-2019, entry version 168.
DE   RecName: Full=Laminin subunit gamma-3;
DE   AltName: Full=Laminin-12 subunit gamma;
DE   AltName: Full=Laminin-14 subunit gamma;
DE   AltName: Full=Laminin-15 subunit gamma;
DE   Flags: Precursor;
GN   Name=LAMC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-522; GLY-544; GLY-770 AND
RP   GLY-1082.
RC   TISSUE=Placenta;
RX   PubMed=10225960; DOI=10.1083/jcb.145.3.605;
RA   Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J.,
RA   Burgeson R.E., Champliaud M.-F.;
RT   "Characterization and expression of the laminin gamma3 chain: a novel,
RT   non-basement membrane-associated, laminin chain.";
RL   J. Cell Biol. 145:605-618(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, AND VARIANTS
RP   GLY-544; GLY-770 AND GLY-1082.
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   VARIANT OCCM ARG-350.
RX   PubMed=21572413; DOI=10.1038/ng.836;
RA   Barak T., Kwan K.Y., Louvi A., Demirbilek V., Saygi S., Tuysuz B.,
RA   Choi M., Boyaci H., Doerschner K., Zhu Y., Kaymakcalan H., Yilmaz S.,
RA   Bakircioglu M., Caglayan A.O., Ozturk A.K., Yasuno K., Brunken W.J.,
RA   Atalar E., Yalcinkaya C., Dincer A., Bronen R.A., Mane S., Ozcelik T.,
RA   Lifton R.P., Sestan N., Bilguvar K., Gunel M.;
RT   "Recessive LAMC3 mutations cause malformations of occipital cortical
RT   development.";
RL   Nat. Genet. 43:590-594(2011).
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. Gamma-3 is a subunit of laminin-12 (laminin-213), laminin-14
CC       (laminin-423) and laminin-15 (laminin-523).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Broadly expressed in: skin, heart, lung, and
CC       the reproductive tracts.
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: Domain IV is globular.
CC   -!- DISEASE: Cortical malformations occipital (OCCM) [MIM:614115]: A
CC       disease in which affected individuals develop seizures, sometimes
CC       associated with transient visual changes. Brain MRI shows both
CC       pachygyria and polymicrogyria restricted to the lateral occipital
CC       lobes. {ECO:0000269|PubMed:21572413}. Note=The disease is caused
CC       by mutations affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD36991.1; Type=Frameshift; Positions=598, 609; Evidence={ECO:0000305};
DR   EMBL; AF041835; AAD36991.1; ALT_FRAME; mRNA.
DR   EMBL; AL355872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL583807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB208887; BAD92124.1; -; mRNA.
DR   CCDS; CCDS6938.1; -.
DR   RefSeq; NP_006050.3; NM_006059.3.
DR   UniGene; Hs.201805; -.
DR   ProteinModelPortal; Q9Y6N6; -.
DR   SMR; Q9Y6N6; -.
DR   BioGrid; 115603; 20.
DR   ComplexPortal; CPX-1781; Laminin-213 complex.
DR   ComplexPortal; CPX-1782; Laminin-423 complex.
DR   ComplexPortal; CPX-1784; Laminin-523 complex.
DR   IntAct; Q9Y6N6; 30.
DR   MINT; Q9Y6N6; -.
DR   STRING; 9606.ENSP00000354360; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   iPTMnet; Q9Y6N6; -.
DR   PhosphoSitePlus; Q9Y6N6; -.
DR   BioMuta; LAMC3; -.
DR   DMDM; 308153586; -.
DR   EPD; Q9Y6N6; -.
DR   jPOST; Q9Y6N6; -.
DR   MaxQB; Q9Y6N6; -.
DR   PaxDb; Q9Y6N6; -.
DR   PeptideAtlas; Q9Y6N6; -.
DR   PRIDE; Q9Y6N6; -.
DR   ProteomicsDB; 86743; -.
DR   DNASU; 10319; -.
DR   Ensembl; ENST00000361069; ENSP00000354360; ENSG00000050555.
DR   GeneID; 10319; -.
DR   KEGG; hsa:10319; -.
DR   UCSC; uc004caa.2; human.
DR   CTD; 10319; -.
DR   DisGeNET; 10319; -.
DR   EuPathDB; HostDB:ENSG00000050555.17; -.
DR   GeneCards; LAMC3; -.
DR   H-InvDB; HIX0008477; -.
DR   HGNC; HGNC:6494; LAMC3.
DR   HPA; HPA022814; -.
DR   MalaCards; LAMC3; -.
DR   MIM; 604349; gene.
DR   MIM; 614115; phenotype.
DR   neXtProt; NX_Q9Y6N6; -.
DR   OpenTargets; ENSG00000050555; -.
DR   Orphanet; 280640; Occipital pachygyria and polymicrogyria.
DR   PharmGKB; PA30282; -.
DR   eggNOG; ENOG410IP68; Eukaryota.
DR   eggNOG; ENOG4111F9V; LUCA.
DR   GeneTree; ENSGT00940000161559; -.
DR   HOGENOM; HOG000019301; -.
DR   HOVERGEN; HBG100808; -.
DR   InParanoid; Q9Y6N6; -.
DR   KO; K06247; -.
DR   OMA; TCIQLAD; -.
DR   OrthoDB; 156553at2759; -.
DR   PhylomeDB; Q9Y6N6; -.
DR   TreeFam; TF352481; -.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   ChiTaRS; LAMC3; human.
DR   GeneWiki; LAMC3; -.
DR   GenomeRNAi; 10319; -.
DR   PRO; PR:Q9Y6N6; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000050555; Expressed in 123 organ(s), highest expression level in placenta.
DR   ExpressionAtlas; Q9Y6N6; baseline and differential.
DR   Genevisible; Q9Y6N6; HS.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0000904; P:cell morphogenesis involved in differentiation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
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; 7.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 10.
DR   PROSITE; PS50027; EGF_LAM_2; 10.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Coiled coil; Complete proteome;
KW   Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   1575       Laminin subunit gamma-3.
FT                                /FTId=PRO_0000017079.
FT   DOMAIN       31    270       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      271    326       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      327    382       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      383    429       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      430    479       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      480    489       Laminin EGF-like 5; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      499    672       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN      673    706       Laminin EGF-like 5; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      707    754       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      755    809       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      810    865       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      866    916       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      917    964       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      965   1013       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   REGION     1014   1575       Domain II and I.
FT   COILED     1073   1134       {ECO:0000255}.
FT   COILED     1201   1228       {ECO:0000255}.
FT   COILED     1410   1492       {ECO:0000255}.
FT   COILED     1523   1567       {ECO:0000255}.
FT   MOTIF      1059   1061       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD     87     87       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    119    119       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    328    328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    837    837       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    980    980       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1185   1185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    280       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    273    290       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    292    301       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    304    324       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    327    336       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    329    352       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    355    364       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    367    380       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    383    395       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    385    401       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    403    412       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    415    427       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    430    441       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    432    448       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    450    459       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    462    477       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    707    715       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    709    722       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    724    733       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    736    752       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    755    763       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    757    774       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    777    786       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    789    807       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    810    824       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    812    831       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    834    843       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    846    863       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    866    880       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    868    887       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    889    898       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    901    914       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    917    929       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    919    936       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    938    947       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    950    962       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    965    977       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    967    983       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    985    994       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    997   1010       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   VARIANT     350    350       G -> R (in OCCM; dbSNP:rs571785750).
FT                                {ECO:0000269|PubMed:21572413}.
FT                                /FTId=VAR_066404.
FT   VARIANT     522    522       P -> S (in dbSNP:rs869457).
FT                                {ECO:0000269|PubMed:10225960}.
FT                                /FTId=VAR_056145.
FT   VARIANT     544    544       E -> G (in dbSNP:rs10901333).
FT                                {ECO:0000269|PubMed:10225960,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_056146.
FT   VARIANT     770    770       R -> G (in dbSNP:rs3739510).
FT                                {ECO:0000269|PubMed:10225960,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_056147.
FT   VARIANT    1082   1082       S -> G (in dbSNP:rs2275140).
FT                                {ECO:0000269|PubMed:10225960,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_056148.
FT   VARIANT    1264   1264       R -> W (in dbSNP:rs11244275).
FT                                /FTId=VAR_056149.
FT   CONFLICT    957    957       F -> S (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT    979    979       E -> Y (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT    999    999       D -> Y (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT   1024   1024       A -> T (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT   1157   1157       T -> I (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT   1309   1309       K -> MARSRLTATFASQ (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT   1313   1313       E -> G (in Ref. 1; AAD36991).
FT                                {ECO:0000305}.
FT   CONFLICT   1433   1433       T -> M (in Ref. 3; BAD92124).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1575 AA;  171227 MW;  D09DAFB3A900E1BD CRC64;
     MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA SHTCGSPPED
     FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES TWWQSPSMAF GVQYPTSVNI
     TLRLGKAYEI TYVRLKFHTS RPESFAIYKR SRADGPWEPY QFYSASCQKT YGRPEGQYLR
     PGEDERVAFC TSEFSDISPL SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR
     LNTFGDDIFK DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD
     CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG RCHHCRDHTA
     GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT CACKPTVTGW KCDRCLPGFH
     SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC
     FCYGHSKVCA STAQFQVHHI LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL
     TAPEKFLGDQ RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP
     REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF LTEVRLTSAR
     PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP YASCVPCTCN QHGTCDPNTG
     ICVCSHHTEG PSCERCLPGF YGNPFAGQAD DCQPCPCPGQ SACTTIPESR EVVCTHCPPG
     QRGRRCEVCD DGFFGDPLGL FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG
     DHCEHCQEGF YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR
     CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC QLGFFGFSIK
     GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN FFLTADGTHC QQCPSCYALV
     KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL DILLGEAPRG DVYQGHHLLP GAREAFLEQM
     MSLEGAVKAA REQLQRLNKG ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE
     IPQEGPSQPT KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA
     LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL ALLASPGALP
     QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT LRQTEPLTKL HQEARAALTQ
     ASSSVQAATV TVMGARTLLA DLEGMKLQFP RPKDQAALQR KADSVSDRLL ADTRKKTKQA
     ERMLGNAAPL SSSAKKKGRE AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA
     SQQVLASEAR RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA
     PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL AEIRADKQNL
     EAILHSLPEN CASWQ
//
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