ID   ATS6_HUMAN              Reviewed;        1117 AA.
AC   Q9UKP5; Q59EX6; Q5IR87; Q5IR88; Q5IR89; Q68DL1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 6;
DE            Short=ADAM-TS 6;
DE            Short=ADAM-TS6;
DE            Short=ADAMTS-6;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAMTS6;
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 2).
RX   PubMed=10464288; DOI=10.1074/jbc.274.36.25555;
RA   Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.;
RT   "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc
RT   metalloproteases.";
RL   J. Biol. Chem. 274:25555-25563(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND INDUCTION.
RX   PubMed=16129570; DOI=10.1016/j.gene.2005.06.011;
RA   Bevitt D.J., Li Z., Lindrop J.L., Barker M.D., Clarke M.P., McKie N.;
RT   "Analysis of full length ADAMTS6 transcript reveals alternative splicing
RT   and a role for the 5' untranslated region in translational control.";
RL   Gene 359:99-110(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1117 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 804-1117 (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   INDUCTION.
RX   PubMed=12697333; DOI=10.1016/s0167-4781(03)00047-2;
RA   Bevitt D.J., Mohamed J., Catterall J.B., Li Z., Arris C.E., Hiscott P.,
RA   Sheridan C., Langton K.P., Barker M.D., Clarke M.P., McKie N.;
RT   "Expression of ADAMTS metalloproteinases in the retinal pigment epithelium
RT   derived cell line ARPE-19: transcriptional regulation by TNFalpha.";
RL   Biochim. Biophys. Acta 1626:83-91(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Variant 2;
CC         IsoId=Q9UKP5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Variant 1;
CC         IsoId=Q9UKP5-2; Sequence=VSP_037095, VSP_037098, VSP_037099;
CC       Name=3; Synonyms=Variant 3;
CC         IsoId=Q9UKP5-3; Sequence=VSP_037096, VSP_037097;
CC       Name=4; Synonyms=Variant 4;
CC         IsoId=Q9UKP5-4; Sequence=VSP_037093, VSP_037094;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in placenta and barely
CC       detectable in a number of other tissues.
CC   -!- INDUCTION: Isoform 1 and isoform 2 expressions are up-regulated by TNF
CC       in retinal pigment epithelial cells. {ECO:0000269|PubMed:12697333,
CC       ECO:0000269|PubMed:16129570}.
CC   -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC       a tight interaction with the extracellular matrix.
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   -!- MISCELLANEOUS: [Isoform 2]: Contains critical point mutations in the
CC       region encoding the catalytic domain as well as 2 point mutations
CC       compared with genomic sequence. May either be a rare polymorphism or
CC       may have arisen through a combination of aberrant RNA editing and point
CC       mutation/sequencing error. {ECO:0000305}.
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DR   EMBL; AF140674; AAD56357.1; -; mRNA.
DR   EMBL; AY692424; AAW47397.1; -; mRNA.
DR   EMBL; AY692425; AAW47398.1; -; mRNA.
DR   EMBL; AY692426; AAW47399.1; -; mRNA.
DR   EMBL; AC008847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC099505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB209685; BAD92922.1; -; mRNA.
DR   EMBL; CR749356; CAH18209.1; -; mRNA.
DR   CCDS; CCDS3983.2; -. [Q9UKP5-1]
DR   RefSeq; NP_922932.2; NM_197941.3. [Q9UKP5-1]
DR   RefSeq; XP_011541415.1; XM_011543113.2. [Q9UKP5-1]
DR   RefSeq; XP_011541416.1; XM_011543114.2. [Q9UKP5-1]
DR   AlphaFoldDB; Q9UKP5; -.
DR   SMR; Q9UKP5; -.
DR   BioGRID; 116345; 8.
DR   IntAct; Q9UKP5; 2.
DR   MINT; Q9UKP5; -.
DR   STRING; 9606.ENSP00000370443; -.
DR   BindingDB; Q9UKP5; -.
DR   MEROPS; M12.230; -.
DR   GlyCosmos; Q9UKP5; 6 sites, No reported glycans.
DR   GlyGen; Q9UKP5; 6 sites.
DR   iPTMnet; Q9UKP5; -.
DR   PhosphoSitePlus; Q9UKP5; -.
DR   BioMuta; ADAMTS6; -.
DR   DMDM; 229462816; -.
DR   MassIVE; Q9UKP5; -.
DR   PaxDb; 9606-ENSP00000370443; -.
DR   PeptideAtlas; Q9UKP5; -.
DR   ProteomicsDB; 84830; -. [Q9UKP5-2]
DR   Antibodypedia; 11532; 79 antibodies from 17 providers.
DR   DNASU; 11174; -.
DR   Ensembl; ENST00000381052.8; ENSP00000424377.1; ENSG00000049192.15. [Q9UKP5-4]
DR   Ensembl; ENST00000381055.8; ENSP00000370443.3; ENSG00000049192.15. [Q9UKP5-1]
DR   GeneID; 11174; -.
DR   KEGG; hsa:11174; -.
DR   MANE-Select; ENST00000381055.8; ENSP00000370443.3; NM_197941.4; NP_922932.2.
DR   UCSC; uc003jtp.4; human. [Q9UKP5-1]
DR   AGR; HGNC:222; -.
DR   CTD; 11174; -.
DR   DisGeNET; 11174; -.
DR   GeneCards; ADAMTS6; -.
DR   HGNC; HGNC:222; ADAMTS6.
DR   HPA; ENSG00000049192; Tissue enhanced (placenta).
DR   MIM; 605008; gene.
DR   neXtProt; NX_Q9UKP5; -.
DR   OpenTargets; ENSG00000049192; -.
DR   PharmGKB; PA24550; -.
DR   VEuPathDB; HostDB:ENSG00000049192; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   eggNOG; KOG4597; Eukaryota.
DR   GeneTree; ENSGT00940000156571; -.
DR   HOGENOM; CLU_000660_1_1_1; -.
DR   InParanoid; Q9UKP5; -.
DR   OMA; GPEWRHD; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; Q9UKP5; -.
DR   TreeFam; TF313537; -.
DR   PathwayCommons; Q9UKP5; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q9UKP5; -.
DR   BioGRID-ORCS; 11174; 6 hits in 1079 CRISPR screens.
DR   ChiTaRS; ADAMTS6; human.
DR   GenomeRNAi; 11174; -.
DR   Pharos; Q9UKP5; Tbio.
DR   PRO; PR:Q9UKP5; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UKP5; Protein.
DR   Bgee; ENSG00000049192; Expressed in tibia and 127 other cell types or tissues.
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:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR   GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
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   PANTHER; PTHR13723:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9UKP5; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029174"
FT   CHAIN           245..1117
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 6"
FT                   /id="PRO_0000029175"
FT   DOMAIN          250..468
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          495..557
FT                   /note="Disintegrin"
FT   DOMAIN          558..613
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          840..900
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          902..960
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          962..1007
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1018..1073
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1079..1117
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          717..843
FT                   /note="Spacer"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        724
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        956
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        326..387
FT                   /evidence="ECO:0000250"
FT   DISULFID        362..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..463
FT                   /evidence="ECO:0000250"
FT   DISULFID        420..447
FT                   /evidence="ECO:0000250"
FT   DISULFID        490..512
FT                   /evidence="ECO:0000250"
FT   DISULFID        501..519
FT                   /evidence="ECO:0000250"
FT   DISULFID        507..542
FT                   /evidence="ECO:0000250"
FT   DISULFID        532..547
FT                   /evidence="ECO:0000250"
FT   DISULFID        570..607
FT                   /evidence="ECO:0000250"
FT   DISULFID        574..612
FT                   /evidence="ECO:0000250"
FT   DISULFID        585..597
FT                   /evidence="ECO:0000250"
FT   DISULFID        911..954
FT                   /evidence="ECO:0000250"
FT   DISULFID        915..959
FT                   /evidence="ECO:0000250"
FT   DISULFID        926..943
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         283..292
FT                   /note="AKLYRDSSLG -> RLPNFTVIPA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16129570"
FT                   /id="VSP_037093"
FT   VAR_SEQ         293..1117
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16129570"
FT                   /id="VSP_037094"
FT   VAR_SEQ         422..504
FT                   /note="TKGHEAAKLMAAHITANTNPFSWSACSRDYITSFLDSGRGTCLDNEPPKRDF
FT                   LYPAVAPGQVYDADEQCRFQYGATSRQCKYG -> RKVMKQQNYGSSHYCEYQSFFLVC
FT                   LQSRFHHQLFR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10464288"
FT                   /id="VSP_037095"
FT   VAR_SEQ         457..468
FT                   /note="DSGRGTCLDNEP -> EFLKLGDSISGS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16129570"
FT                   /id="VSP_037096"
FT   VAR_SEQ         469..1117
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16129570"
FT                   /id="VSP_037097"
FT   VAR_SEQ         860..908
FT                   /note="VQRQEVVCKRLDDNSIVQNNYCDPDSKPPENQRACNTEPCPPEWFIGDW ->
FT                   KMPTRQPTQRARWRTKHILSYALCLLKKLIGNISCRFASSCNLAKETLL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10464288"
FT                   /id="VSP_037098"
FT   VAR_SEQ         909..1117
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10464288"
FT                   /id="VSP_037099"
FT   CONFLICT        4
FT                   /note="L -> S (in Ref. 2; AAW47399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="D -> G (in Ref. 2; AAW47398)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="S -> P (in Ref. 2; AAW47398)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="Y -> H (in Ref. 2; AAW47397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="G -> V (in Ref. 1; AAD56357)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        426
FT                   /note="E -> G (in Ref. 1; AAD56357 and 2; AAW47397)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        588..589
FT                   /note="PA -> LK (in Ref. 4; BAD92922)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="D -> G (in Ref. 1; AAD56357)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1117 AA;  125273 MW;  5901E86BC82A9A87 CRC64;
     MEILWKTLTW ILSLIMASSE FHSDHRLSYS SQEEFLTYLE HYQLTIPIRV DQNGAFLSFT
     VKNDKHSRRR RSMDPIDPQQ AVSKLFFKLS AYGKHFHLNL TLNTDFVSKH FTVEYWGKDG
     PQWKHDFLDN CHYTGYLQDQ RSTTKVALSN CVGLHGVIAT EDEEYFIEPL KNTTEDSKHF
     SYENGHPHVI YKKSALQQRH LYDHSHCGVS DFTRSGKPWW LNDTSTVSYS LPINNTHIHH
     RQKRSVSIER FVETLVVADK MMVGYHGRKD IEHYILSVMN IVAKLYRDSS LGNVVNIIVA
     RLIVLTEDQP NLEINHHADK SLDSFCKWQK SILSHQSDGN TIPENGIAHH DNAVLITRYD
     ICTYKNKPCG TLGLASVAGM CEPERSCSIN EDIGLGSAFT IAHEIGHNFG MNHDGIGNSC
     GTKGHEAAKL MAAHITANTN PFSWSACSRD YITSFLDSGR GTCLDNEPPK RDFLYPAVAP
     GQVYDADEQC RFQYGATSRQ CKYGEVCREL WCLSKSNRCV TNSIPAAEGT LCQTGNIEKG
     WCYQGDCVPF GTWPQSIDGG WGPWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE
     RKRYRSCNTD PCPLGSRDFR EKQCADFDNM PFRGKYYNWK PYTGGGVKPC ALNCLAEGYN
     FYTERAPAVI DGTQCNADSL DICINGECKH VGCDNILGSD AREDRCRVCG GDGSTCDAIE
     GFFNDSLPRG GYMEVVQIPR GSVHIEVREV AMSKNYIALK SEGDDYYING AWTIDWPRKF
     DVAGTAFHYK RPTDEPESLE ALGPTSENLI VMVLLQEQNL GIRYKFNVPI TRTGSGDNEV
     GFTWNHQPWS ECSATCAGGV QRQEVVCKRL DDNSIVQNNY CDPDSKPPEN QRACNTEPCP
     PEWFIGDWLE CSKTCDGGMR TRAVLCIRKI GPSEEETLDY SGCLTHRPVE KEPCNNQSCP
     PQWVALDWSE CTPKCGPGFK HRIVLCKSSD LSKTFPAAQC PEESKPPVRI RCSLGRCPPP
     RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG QASSDCLETV RPPSMQQCES KCDSTPISNT
     EECKDVNKVA YCPLVLKFKF CSRAYFRQMC CKTCQGH
//