ATL3_HUMAN
ID ATL3_HUMAN Reviewed; 1691 AA.
AC P82987; A1A566; A1A567; Q9ULI7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ADAMTS-like protein 3;
DE Short=ADAMTSL-3;
DE AltName: Full=Punctin-2;
DE Flags: Precursor;
GN Name=ADAMTSL3; Synonyms=KIAA1233;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-146 AND PHE-869.
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-766, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS VAL-290 AND LEU-661.
RX PubMed=14667842; DOI=10.1016/s0945-053x(03)00075-1;
RA Hall N.G., Klenotic P., Anand-Apte B., Apte S.S.;
RT "ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix related
RT to the ADAMTS family of metalloproteases.";
RL Matrix Biol. 22:501-510(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 669-1691.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17597111; DOI=10.1002/ijc.22882;
RA Koo B.H., Hurskainen T., Mielke K., Aung P.P., Casey G.,
RA Autio-Harmainen H., Apte S.S.;
RT "ADAMTSL3/punctin-2, a gene frequently mutated in colorectal tumors, is
RT widely expressed in normal and malignant epithelial cells, vascular
RT endothelial cells and other cell types, and its mRNA is reduced in colon
RT cancer.";
RL Int. J. Cancer 121:1710-1716(2007).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-330; HIS-587; CYS-855 AND GLU-1315.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- INTERACTION:
CC P82987; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10221726, EBI-3867333;
CC P82987; O76003: GLRX3; NbExp=3; IntAct=EBI-10221726, EBI-374781;
CC P82987; Q6A162: KRT40; NbExp=3; IntAct=EBI-10221726, EBI-10171697;
CC P82987; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10221726, EBI-11959885;
CC P82987; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-10221726, EBI-12012928;
CC P82987; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-10221726, EBI-10171774;
CC P82987; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10221726, EBI-11953334;
CC P82987; P0C7H8: KRTAP2-3; NbExp=3; IntAct=EBI-10221726, EBI-10196781;
CC P82987; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-10221726, EBI-14065470;
CC P82987; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-10221726, EBI-751260;
CC P82987; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-10221726, EBI-11987425;
CC P82987; Q99750: MDFI; NbExp=6; IntAct=EBI-10221726, EBI-724076;
CC P82987; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10221726, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:14667842}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P82987-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P82987-2; Sequence=VSP_037810;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the colon,
CC fallopian tube, skin, breast, prostate, epididymis, liver, pancreatic
CC islets and bile ducts, as well as by vascular endothelial cells, smooth
CC muscle cells, fibroblasts, cortical and ganglionic neurons and cardiac
CC myocytes. Also expressed by malignant epithelial cells in colon cancer,
CC as well as breast, prostate, renal and skin tumors. Expression is
CC significantly reduced in colon cancer compared to normal colon.
CC {ECO:0000269|PubMed:14667842, ECO:0000269|PubMed:17597111}.
CC -!- PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a
CC serine or a threonine residue found within the consensus sequence C1-
CC X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC the first and second cysteine residue of the repeat, respectively.
CC Fucosylated repeats can then be further glycosylated by the addition of
CC a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC Fucosylation mediates the efficient secretion of ADAMTS family members.
CC Can also be C-glycosylated with one or two mannose molecules on
CC tryptophan residues within the consensus sequence W-X-X-W of the TPRs,
CC and N-glycosylated. These other glycosylations can also facilitate
CC secretion (By similarity). {ECO:0000250}.
CC -!- CAUTION: Although strongly similar to members of the ADAMTS family it
CC lacks the metalloprotease and disintegrin-like domains which are
CC typical of that family. {ECO:0000305}.
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DR EMBL; AC087738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128389; AAI28390.1; -; mRNA.
DR EMBL; BC128390; AAI28391.1; -; mRNA.
DR EMBL; AF237652; AAK15041.1; -; mRNA.
DR EMBL; AB033059; BAA86547.1; -; mRNA.
DR CCDS; CCDS10326.1; -. [P82987-1]
DR CCDS; CCDS73773.1; -. [P82987-2]
DR RefSeq; NP_001288039.1; NM_001301110.1. [P82987-2]
DR RefSeq; NP_997400.2; NM_207517.2. [P82987-1]
DR AlphaFoldDB; P82987; -.
DR BioGRID; 121437; 14.
DR IntAct; P82987; 13.
DR STRING; 9606.ENSP00000286744; -.
DR GlyGen; P82987; 20 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; P82987; -.
DR PhosphoSitePlus; P82987; -.
DR BioMuta; ADAMTSL3; -.
DR DMDM; 308153648; -.
DR jPOST; P82987; -.
DR MassIVE; P82987; -.
DR PaxDb; P82987; -.
DR PeptideAtlas; P82987; -.
DR PRIDE; P82987; -.
DR ProteomicsDB; 57728; -. [P82987-1]
DR ProteomicsDB; 57729; -. [P82987-2]
DR Antibodypedia; 28207; 51 antibodies from 11 providers.
DR DNASU; 57188; -.
DR Ensembl; ENST00000286744.10; ENSP00000286744.5; ENSG00000156218.13. [P82987-1]
DR Ensembl; ENST00000567476.1; ENSP00000456313.1; ENSG00000156218.13. [P82987-2]
DR GeneID; 57188; -.
DR KEGG; hsa:57188; -.
DR MANE-Select; ENST00000286744.10; ENSP00000286744.5; NM_207517.3; NP_997400.2.
DR UCSC; uc002bjz.5; human. [P82987-1]
DR CTD; 57188; -.
DR DisGeNET; 57188; -.
DR GeneCards; ADAMTSL3; -.
DR HGNC; HGNC:14633; ADAMTSL3.
DR HPA; ENSG00000156218; Low tissue specificity.
DR MIM; 609199; gene.
DR neXtProt; NX_P82987; -.
DR OpenTargets; ENSG00000156218; -.
DR PharmGKB; PA134934525; -.
DR VEuPathDB; HostDB:ENSG00000156218; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158143; -.
DR HOGENOM; CLU_001717_1_0_1; -.
DR InParanoid; P82987; -.
DR OMA; MVFMHST; -.
DR OrthoDB; 38261at2759; -.
DR PhylomeDB; P82987; -.
DR TreeFam; TF351125; -.
DR PathwayCommons; P82987; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; P82987; -.
DR BioGRID-ORCS; 57188; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; ADAMTSL3; human.
DR GenomeRNAi; 57188; -.
DR Pharos; P82987; Tbio.
DR PRO; PR:P82987; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P82987; protein.
DR Bgee; ENSG00000156218; Expressed in calcaneal tendon and 151 other tissues.
DR Genevisible; P82987; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 2.20.100.10; -; 12.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00209; TSP1; 12.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF82895; SSF82895; 12.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1691
FT /note="ADAMTS-like protein 3"
FT /id="PRO_0000249684"
FT DOMAIN 75..124
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 418..468
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 478..535
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 564..626
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 703..760
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 763..818
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 819..881
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 896..992
FT /note="Ig-like C2-type 1"
FT DOMAIN 1185..1279
FT /note="Ig-like C2-type 2"
FT DOMAIN 1296..1378
FT /note="Ig-like C2-type 3"
FT DOMAIN 1424..1482
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1483..1545
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1597..1644
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1655..1691
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 1146..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..118
FT /evidence="ECO:0000250"
FT DISULFID 91..123
FT /evidence="ECO:0000250"
FT DISULFID 102..108
FT /evidence="ECO:0000250"
FT DISULFID 576..620
FT /evidence="ECO:0000250"
FT DISULFID 580..625
FT /evidence="ECO:0000250"
FT DISULFID 591..609
FT /evidence="ECO:0000250"
FT DISULFID 831..875
FT /evidence="ECO:0000250"
FT DISULFID 835..880
FT /evidence="ECO:0000250"
FT DISULFID 846..863
FT /evidence="ECO:0000250"
FT DISULFID 934..982
FT /evidence="ECO:0000250"
FT DISULFID 1215..1263
FT /evidence="ECO:0000250"
FT DISULFID 1321..1367
FT /evidence="ECO:0000250"
FT VAR_SEQ 1657..1691
FT /note="RDCTDTTHYCMFVKHLNLCSLDRYKQRCCQSCQEG -> STYTSQTATNKGA
FT ASHVKRDKPLEGS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037810"
FT VARIANT 146
FT /note="H -> R (in dbSNP:rs4483821)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027478"
FT VARIANT 290
FT /note="L -> V (in dbSNP:rs4144691)"
FT /evidence="ECO:0000269|PubMed:14667842"
FT /id="VAR_027479"
FT VARIANT 330
FT /note="V -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1439091253)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035809"
FT VARIANT 587
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs142860011)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035810"
FT VARIANT 661
FT /note="V -> L (in dbSNP:rs4842838)"
FT /evidence="ECO:0000269|PubMed:14667842"
FT /id="VAR_027480"
FT VARIANT 713
FT /note="G -> R (in dbSNP:rs34047645)"
FT /id="VAR_057365"
FT VARIANT 855
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs146769560)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035811"
FT VARIANT 855
FT /note="R -> H (in dbSNP:rs2277848)"
FT /id="VAR_027481"
FT VARIANT 869
FT /note="L -> F (in dbSNP:rs2277849)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027482"
FT VARIANT 1315
FT /note="A -> E (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035812"
FT VARIANT 1370
FT /note="T -> A (in dbSNP:rs17158450)"
FT /id="VAR_027483"
FT VARIANT 1558
FT /note="M -> T (in dbSNP:rs7175910)"
FT /id="VAR_027484"
FT VARIANT 1660
FT /note="T -> I (in dbSNP:rs950169)"
FT /id="VAR_027485"
FT VARIANT 1679
FT /note="R -> H (in dbSNP:rs11857906)"
FT /id="VAR_027486"
FT CONFLICT 265
FT /note="A -> V (in Ref. 3; AAK15041)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="S -> F (in Ref. 2; AAI28390)"
FT /evidence="ECO:0000305"
FT CONFLICT 1526
FT /note="A -> S (in Ref. 2; AAI28390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1691 AA; 188692 MW; 48C7281C737EA56E CRC64;
MASWTSPWWV LIGMVFMHSP LPQTTAEKSP GAYFLPEFAL SPQGSFLEDT TGEQFLTYRY
DDQTSRNTRS DEDKDGNWDA WGDWSDCSRT CGGGASYSLR RCLTGRNCEG QNIRYKTCSN
HDCPPDAEDF RAQQCSAYND VQYQGHYYEW LPRYNDPAAP CALKCHAQGQ NLVVELAPKV
LDGTRCNTDS LDMCISGICQ AVGCDRQLGS NAKEDNCGVC AGDGSTCRLV RGQSKSHVSP
EKREENVIAV PLGSRSVRIT VKGPAHLFIE SKTLQGSKGE HSFNSPGVFL VENTTVEFQR
GSERQTFKIP GPLMADFIFK TRYTAAKDSV VQFFFYQPIS HQWRQTDFFP CTVTCGGGYQ
LNSAECVDIR LKRVVPDHYC HYYPENVKPK PKLKECSMDP CPSSDGFKEI MPYDHFQPLP
RWEHNPWTAC SVSCGGGIQR RSFVCVEESM HGEILQVEEW KCMYAPKPKV MQTCNLFDCP
KWIAMEWSQC TVTCGRGLRY RVVLCINHRG EHVGGCNPQL KLHIKEECVI PIPCYKPKEK
SPVEAKLPWL KQAQELEETR IATEEPTFIP EPWSACSTTC GPGVQVREVK CRVLLTFTQT
ETELPEEECE GPKLPTERPC LLEACDESPA SRELDIPLPE DSETTYDWEY AGFTPCTATC
VGGHQEAIAV CLHIQTQQTV NDSLCDMVHR PPAMSQACNT EPCPPRWHVG SWGPCSATCG
VGIQTRDVYC LHPGETPAPP EECRDEKPHA LQACNQFDCP PGWHIEEWQQ CSRTCGGGTQ
NRRVTCRQLL TDGSFLNLSD ELCQGPKASS HKSCARTDCP PHLAVGDWSK CSVSCGVGIQ
RRKQVCQRLA AKGRRIPLSE MMCRDLPGLP LVRSCQMPEC SKIKSEMKTK LGEQGPQILS
VQRVYIQTRE EKRINLTIGS RAYLLPNTSV IIKCPVRRFQ KSLIQWEKDG RCLQNSKRLG
ITKSGSLKIH GLAAPDIGVY RCIAGSAQET VVLKLIGTDN RLIARPALRE PMREYPGMDH
SEANSLGVTW HKMRQMWNNK NDLYLDDDHI SNQPFLRALL GHCSNSAGST NSWELKNKQF
EAAVKQGAYS MDTAQFDELI RNMSQLMETG EVSDDLASQL IYQLVAELAK AQPTHMQWRG
IQEETPPAAQ LRGETGSVSQ SSHAKNSGKL TFKPKGPVLM RQSQPPSISF NKTINSRIGN
TVYITKRTEV INILCDLITP SEATYTWTKD GTLLQPSVKI ILDGTGKIQI QNPTRKEQGI
YECSVANHLG SDVESSSVLY AEAPVILSVE RNITKPEHNH LSVVVGGIVE AALGANVTIR
CPVKGVPQPN ITWLKRGGSL SGNVSLLFNG SLLLQNVSLE NEGTYVCIAT NALGKAVATS
VLHLLERRWP ESRIVFLQGH KKYILQATNT RTNSNDPTGE PPPQEPFWEP GNWSHCSATC
GHLGARIQRP QCVMANGQEV SEALCDHLQK PLAGFEPCNI RDCPARWFTS VWSQCSVSCG
EGYHSRQVTC KRTKANGTVQ VVSPRACAPK DRPLGRKPCF GHPCVQWEPG NRCPGRCMGR
AVRMQQRHTA CQHNSSDSNC DDRKRPTLRR NCTSGACDVC WHTGPWKPCT AACGRGFQSR
KVDCIHTRSC KPVAKRHCVQ KKKPISWRHC LGPSCDRDCT DTTHYCMFVK HLNLCSLDRY
KQRCCQSCQE G
