LAMC3_HUMAN
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 03-AUG-2022, entry version 186.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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, non-
RT 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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 GLY-544;
RP 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., Choi M.,
RA 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 is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Gamma-3 is a
CC subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and
CC 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 the
CC reproductive tracts.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC 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 by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD36991.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q9Y6N6; -.
DR SMR; Q9Y6N6; -.
DR BioGRID; 115603; 49.
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 GlyGen; Q9Y6N6; 8 sites.
DR iPTMnet; Q9Y6N6; -.
DR PhosphoSitePlus; Q9Y6N6; -.
DR BioMuta; LAMC3; -.
DR DMDM; 308153586; -.
DR EPD; Q9Y6N6; -.
DR jPOST; Q9Y6N6; -.
DR MassIVE; Q9Y6N6; -.
DR MaxQB; Q9Y6N6; -.
DR PaxDb; Q9Y6N6; -.
DR PeptideAtlas; Q9Y6N6; -.
DR PRIDE; Q9Y6N6; -.
DR ProteomicsDB; 86743; -.
DR Antibodypedia; 45184; 143 antibodies from 23 providers.
DR DNASU; 10319; -.
DR Ensembl; ENST00000361069.9; ENSP00000354360.4; ENSG00000050555.19.
DR GeneID; 10319; -.
DR KEGG; hsa:10319; -.
DR MANE-Select; ENST00000361069.9; ENSP00000354360.4; NM_006059.4; NP_006050.3.
DR UCSC; uc004caa.2; human.
DR CTD; 10319; -.
DR DisGeNET; 10319; -.
DR GeneCards; LAMC3; -.
DR HGNC; HGNC:6494; LAMC3.
DR HPA; ENSG00000050555; Tissue enhanced (placenta).
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 VEuPathDB; HostDB:ENSG00000050555; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000161559; -.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; Q9Y6N6; -.
DR OMA; TCVQLAD; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; Q9Y6N6; -.
DR TreeFam; TF352481; -.
DR PathwayCommons; Q9Y6N6; -.
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 SignaLink; Q9Y6N6; -.
DR BioGRID-ORCS; 10319; 15 hits in 1066 CRISPR screens.
DR ChiTaRS; LAMC3; human.
DR GeneWiki; LAMC3; -.
DR GenomeRNAi; 10319; -.
DR Pharos; Q9Y6N6; Tbio.
DR PRO; PR:Q9Y6N6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y6N6; protein.
DR Bgee; ENSG00000050555; Expressed in endocervix and 123 other tissues.
DR ExpressionAtlas; Q9Y6N6; baseline and differential.
DR Genevisible; Q9Y6N6; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 10.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
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; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1575
FT /note="Laminin subunit gamma-3"
FT /id="PRO_0000017079"
FT DOMAIN 31..270
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 271..326
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 327..382
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 383..429
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 430..479
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 480..489
FT /note="Laminin EGF-like 5; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 499..672
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 673..706
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 707..754
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 755..809
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 810..865
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 866..916
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 917..964
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 965..1013
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1014..1575
FT /note="Domain II and I"
FT REGION 1378..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1073..1134
FT /evidence="ECO:0000255"
FT COILED 1201..1228
FT /evidence="ECO:0000255"
FT COILED 1410..1492
FT /evidence="ECO:0000255"
FT COILED 1523..1567
FT /evidence="ECO:0000255"
FT MOTIF 1059..1061
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 273..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 292..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 304..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 327..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 329..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 355..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 367..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 383..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 385..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 403..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 415..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 430..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 432..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 450..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 462..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 707..715
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 709..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 724..733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 736..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 755..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 757..774
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 777..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 789..807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 810..824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 812..831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 834..843
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 846..863
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 866..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 868..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 889..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 901..914
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 917..929
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 919..936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 938..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 950..962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 965..977
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 967..983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 985..994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 997..1010
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT VARIANT 350
FT /note="G -> R (in OCCM; dbSNP:rs571785750)"
FT /evidence="ECO:0000269|PubMed:21572413"
FT /id="VAR_066404"
FT VARIANT 522
FT /note="P -> S (in dbSNP:rs869457)"
FT /evidence="ECO:0000269|PubMed:10225960"
FT /id="VAR_056145"
FT VARIANT 544
FT /note="E -> G (in dbSNP:rs10901333)"
FT /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT /id="VAR_056146"
FT VARIANT 770
FT /note="R -> G (in dbSNP:rs3739510)"
FT /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT /id="VAR_056147"
FT VARIANT 1082
FT /note="S -> G (in dbSNP:rs2275140)"
FT /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT /id="VAR_056148"
FT VARIANT 1264
FT /note="R -> W (in dbSNP:rs11244275)"
FT /id="VAR_056149"
FT CONFLICT 957
FT /note="F -> S (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="E -> Y (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="D -> Y (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="A -> T (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1157
FT /note="T -> I (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="K -> MARSRLTATFASQ (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1313
FT /note="E -> G (in Ref. 1; AAD36991)"
FT /evidence="ECO:0000305"
FT CONFLICT 1433
FT /note="T -> M (in Ref. 3; BAD92124)"
FT /evidence="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
