ATS17_HUMAN
ID ATS17_HUMAN Reviewed; 1095 AA.
AC Q8TE56; Q2I7G4; Q6ZN75;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17;
DE Short=ADAM-TS 17;
DE Short=ADAM-TS17;
DE Short=ADAMTS-17;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS17;
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] (ISOFORM 1), AND VARIANT SER-1094.
RX PubMed=11867212; DOI=10.1016/s0378-1119(01)00861-7;
RA Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.;
RT "Cloning, expression analysis, and structural characterization of seven
RT novel human ADAMTSs, a family of metalloproteinases with disintegrin and
RT thrombospondin-1 domains.";
RL Gene 283:49-62(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-566.
RA Tan J., Davila S., Hibberd M.L., Seielstad M.;
RT "Genetic variation in ADAMTS17 gene.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP VARIANTS LEU-216; THR-482 AND SER-1094, INVOLVEMENT IN WMS4, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=19836009; DOI=10.1016/j.ajhg.2009.09.011;
RA Morales J., Al-Sharif L., Khalil D.S., Shinwari J.M., Bavi P.,
RA Al-Mahrouqi R.A., Al-Rajhi A., Alkuraya F.S., Meyer B.F., Al Tassan N.;
RT "Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia,
RT ectopia lentis, glaucoma, spherophakia, and short stature.";
RL Am. J. Hum. Genet. 85:558-568(2009).
RN [6]
RP INVOLVEMENT IN WMS4.
RX PubMed=22486325; DOI=10.3109/13816810.2012.666708;
RA Khan A.O., Aldahmesh M.A., Al-Ghadeer H., Mohamed J.Y., Alkuraya F.S.;
RT "Familial spherophakia with short stature caused by a novel homozygous
RT ADAMTS17 mutation.";
RL Ophthalmic Genet. 33:235-239(2012).
RN [7]
RP INVOLVEMENT IN WMS4.
RX PubMed=24940034;
RA Shah M.H., Bhat V., Shetty J.S., Kumar A.;
RT "Whole exome sequencing identifies a novel splice-site mutation in ADAMTS17
RT in an Indian family with Weill-Marchesani syndrome.";
RL Mol. Vis. 20:790-796(2014).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist.;
CC Name=1; Synonyms=a;
CC IsoId=Q8TE56-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q8TE56-2; Sequence=VSP_040331, VSP_040332, VSP_040333;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at high
CC levels in the lung, brain, whole eye and retina. Isoform 1 shows a
CC weaker expression in the heart, kidney and skeletal muscle. Isoform 2
CC shows a weaker expression in the kidney, bone marrow and skeletal
CC muscle. Isoform 1 and isoform 2 are expressed at high levels in the
CC fetal heart, kidney, and whole eye, whereas a weak expression is seen
CC in the fetal liver. {ECO:0000269|PubMed:19836009}.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Weill-Marchesani syndrome 4 (WMS4) [MIM:613195]: An autosomal
CC recessive syndrome characterized by lenticular myopia, ectopia lentis,
CC glaucoma, spherophakia and short stature. Brachydactyly and decreased
CC joint flexibility are present in some patients.
CC {ECO:0000269|PubMed:19836009, ECO:0000269|PubMed:22486325,
CC ECO:0000269|PubMed:24940034}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AJ315735; CAC86016.1; -; mRNA.
DR EMBL; DQ217943; ABB70740.1; -; Genomic_DNA.
DR EMBL; AK131344; BAD18500.1; -; mRNA.
DR EMBL; AC015723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS10383.1; -. [Q8TE56-1]
DR RefSeq; NP_620688.2; NM_139057.3. [Q8TE56-1]
DR RefSeq; XP_016877473.1; XM_017021984.1. [Q8TE56-2]
DR AlphaFoldDB; Q8TE56; -.
DR SMR; Q8TE56; -.
DR BioGRID; 128083; 31.
DR IntAct; Q8TE56; 2.
DR STRING; 9606.ENSP00000268070; -.
DR MEROPS; M12.027; -.
DR GlyGen; Q8TE56; 7 sites.
DR iPTMnet; Q8TE56; -.
DR PhosphoSitePlus; Q8TE56; -.
DR BioMuta; ADAMTS17; -.
DR DMDM; 296434401; -.
DR jPOST; Q8TE56; -.
DR MassIVE; Q8TE56; -.
DR PaxDb; Q8TE56; -.
DR PeptideAtlas; Q8TE56; -.
DR PRIDE; Q8TE56; -.
DR ProteomicsDB; 74396; -. [Q8TE56-1]
DR ProteomicsDB; 74397; -. [Q8TE56-2]
DR Antibodypedia; 29223; 87 antibodies from 26 providers.
DR DNASU; 170691; -.
DR Ensembl; ENST00000268070.9; ENSP00000268070.4; ENSG00000140470.15. [Q8TE56-1]
DR GeneID; 170691; -.
DR KEGG; hsa:170691; -.
DR MANE-Select; ENST00000268070.9; ENSP00000268070.4; NM_139057.4; NP_620688.2.
DR UCSC; uc002bvv.2; human. [Q8TE56-1]
DR CTD; 170691; -.
DR DisGeNET; 170691; -.
DR GeneCards; ADAMTS17; -.
DR GeneReviews; ADAMTS17; -.
DR HGNC; HGNC:17109; ADAMTS17.
DR HPA; ENSG00000140470; Tissue enhanced (lymphoid).
DR MalaCards; ADAMTS17; -.
DR MIM; 607511; gene.
DR MIM; 613195; phenotype.
DR neXtProt; NX_Q8TE56; -.
DR OpenTargets; ENSG00000140470; -.
DR Orphanet; 363992; Ichthyosis-short stature-brachydactyly-microspherophakia syndrome.
DR PharmGKB; PA24543; -.
DR VEuPathDB; HostDB:ENSG00000140470; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158773; -.
DR HOGENOM; CLU_000660_8_0_1; -.
DR InParanoid; Q8TE56; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q8TE56; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; Q8TE56; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q8TE56; -.
DR BioGRID-ORCS; 170691; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; ADAMTS17; human.
DR GenomeRNAi; 170691; -.
DR Pharos; Q8TE56; Tbio.
DR PRO; PR:Q8TE56; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TE56; protein.
DR Bgee; ENSG00000140470; Expressed in thymus and 111 other tissues.
DR ExpressionAtlas; Q8TE56; baseline and differential.
DR Genevisible; Q8TE56; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Deafness;
KW Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..223
FT /evidence="ECO:0000250"
FT /id="PRO_0000029198"
FT CHAIN 224..1095
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 17"
FT /id="PRO_0000029199"
FT DOMAIN 232..452
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 453..542
FT /note="Disintegrin"
FT DOMAIN 543..598
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 800..860
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 861..922
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 925..968
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 972..1029
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1045..1084
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..779
FT /note="Spacer"
FT MOTIF 199..206
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..373
FT /evidence="ECO:0000250"
FT DISULFID 348..355
FT /evidence="ECO:0000250"
FT DISULFID 367..447
FT /evidence="ECO:0000250"
FT DISULFID 406..431
FT /evidence="ECO:0000250"
FT DISULFID 476..500
FT /evidence="ECO:0000250"
FT DISULFID 487..508
FT /evidence="ECO:0000250"
FT DISULFID 495..527
FT /evidence="ECO:0000250"
FT DISULFID 521..532
FT /evidence="ECO:0000250"
FT DISULFID 555..592
FT /evidence="ECO:0000250"
FT DISULFID 559..597
FT /evidence="ECO:0000250"
FT DISULFID 570..582
FT /evidence="ECO:0000250"
FT DISULFID 873..916
FT /evidence="ECO:0000250"
FT DISULFID 877..921
FT /evidence="ECO:0000250"
FT DISULFID 888..905
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040331"
FT VAR_SEQ 713..745
FT /note="ALKDSGKGSINSDWKIELPGEFQIAGTTVRYVR -> GYIEAAVIPAGARRI
FT RVVEDKPAHSFLGKTQMT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040332"
FT VAR_SEQ 746..1095
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040333"
FT VARIANT 216
FT /note="S -> L (in dbSNP:rs7496668)"
FT /evidence="ECO:0000269|PubMed:19836009"
FT /id="VAR_057081"
FT VARIANT 482
FT /note="M -> T (in dbSNP:rs28567966)"
FT /evidence="ECO:0000269|PubMed:19836009"
FT /id="VAR_057082"
FT VARIANT 566
FT /note="R -> T"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_064041"
FT VARIANT 1094
FT /note="N -> S (in dbSNP:rs2573652)"
FT /evidence="ECO:0000269|PubMed:11867212,
FT ECO:0000269|PubMed:19836009"
FT /id="VAR_060317"
FT CONFLICT 702
FT /note="V -> A (in Ref. 3; BAD18500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1095 AA; 121127 MW; A5D7A40484754D5D CRC64;
MCDGALLPPL VLPVLLLLVW GLDPGTAVGD AAADVEVVLP WRVRPDDVHL PPLPAAPGPR
RRRRPRTPPA APRARPGERA LLLHLPAFGR DLYLQLRRDL RFLSRGFEVE EAGAARRRGR
PAELCFYSGR VLGHPGSLVS LSACGAAGGL VGLIQLGQEQ VLIQPLNNSQ GPFSGREHLI
RRKWSLTPSP SAEAQRPEQL CKVLTEKKKP TWGRPSRDWR ERRNAIRLTS EHTVETLVVA
DADMVQYHGA EAAQRFILTV MNMVYNMFQH QSLGIKINIQ VTKLVLLRQR PAKLSIGHHG
ERSLESFCHW QNEEYGGARY LGNNQVPGGK DDPPLVDAAV FVTRTDFCVH KDEPCDTVGI
AYLGGVCSAK RKCVLAEDNG LNLAFTIAHE LGHNLGMNHD DDHSSCAGRS HIMSGEWVKG
RNPSDLSWSS CSRDDLENFL KSKVSTCLLV TDPRSQHTVR LPHKLPGMHY SANEQCQILF
GMNATFCRNM EHLMCAGLWC LVEGDTSCKT KLDPPLDGTE CGADKWCRAG ECVSKTPIPE
HVDGDWSPWG AWSMCSRTCG TGARFRQRKC DNPPPGPGGT HCPGASVEHA VCENLPCPKG
LPSFRDQQCQ AHDRLSPKKK GLLTAVVVDD KPCELYCSPL GKESPLLVAD RVLDGTPCGP
YETDLCVHGK CQKIGCDGII GSAAKEDRCG VCSGDGKTCH LVKGDFSHAR GTALKDSGKG
SINSDWKIEL PGEFQIAGTT VRYVRRGLWE KISAKGPTKL PLHLMVLLFH DQDYGIHYEY
TVPVNRTAEN QSEPEKPQDS LFIWTHSGWE GCSVQCGGGE RRTIVSCTRI VNKTTTLVND
SDCPQASRPE PQVRRCNLHP CQSRWVAGPW SPCSATCEKG FQHREVTCVY QLQNGTHVAT
RPLYCPGPRP AAVQSCEGQD CLSIWEASEW SQCSASCGKG VWKRTVACTN SQGKCDASTR
PRAEEACEDY SGCYEWKTGD WSTCSSTCGK GLQSRVVQCM HKVTGRHGSE CPALSKPAPY
RQCYQEVCND RINANTITSP RLAALTYKCT RDQWTVYCRV IREKNLCQDM RWYQRCCQTC
RDFYANKMRQ PPPNS
