ID   ATS10_HUMAN             Reviewed;        1103 AA.
AC   Q9H324; M0QZE4;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10;
DE            Short=ADAM-TS 10;
DE            Short=ADAM-TS10;
DE            Short=ADAMTS-10;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAMTS10;
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=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-1103 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   VARIANT SER-134.
RX   PubMed=15355968; DOI=10.1074/jbc.m409036200;
RA   Somerville R.P.T., Jungers K.A., Apte S.S.;
RT   "Discovery and characterization of a novel, widely expressed
RT   metalloprotease, ADAMTS10, and its proteolytic activation.";
RL   J. Biol. Chem. 279:51208-51217(2004).
RN   [3]
RP   INVOLVEMENT IN WMS1.
RX   PubMed=15368195; DOI=10.1086/425231;
RA   Dagoneau N., Benoist-Lasselin C., Huber C., Faivre L., Megarbane A.,
RA   Alswaid A., Dollfus H., Alembik Y., Munnich A., Legeai-Mallet L.,
RA   Cormier-Daire V.;
RT   "ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome.";
RL   Am. J. Hum. Genet. 75:801-806(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FBN1.
RX   PubMed=21402694; DOI=10.1074/jbc.m111.231571;
RA   Kutz W.E., Wang L.W., Bader H.L., Majors A.K., Iwata K., Traboulsi E.I.,
RA   Sakai L.Y., Keene D.R., Apte S.S.;
RT   "ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in
RT   extracellular matrix of cultured fibroblasts.";
RL   J. Biol. Chem. 286:17156-17167(2011).
RN   [5]
RP   VARIANT WMS1 THR-25, AND CHARACTERIZATION OF VARIANT WMS1 THR-25.
RX   PubMed=18567016; DOI=10.1002/humu.20797;
RA   Kutz W.E., Wang L.W., Dagoneau N., Odrcic K.J., Cormier-Daire V.,
RA   Traboulsi E.I., Apte S.S.;
RT   "Functional analysis of an ADAMTS10 signal peptide mutation in Weill-
RT   Marchesani syndrome demonstrates a long-range effect on secretion of the
RT   full-length enzyme.";
RL   Hum. Mutat. 29:1425-1434(2008).
CC   -!- FUNCTION: Metalloprotease that participate in microfibrils assembly.
CC       Microfibrils are extracellular matrix components occurring
CC       independently or along with elastin in the formation of elastic
CC       tissues. {ECO:0000269|PubMed:21402694}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with FBN1; this interaction promotes microfibrils
CC       assembly. {ECO:0000269|PubMed:21402694}.
CC   -!- INTERACTION:
CC       Q9H324; P28301: Lox; Xeno; NbExp=3; IntAct=EBI-7096115, EBI-642911;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:21402694}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H324-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H324-2; Sequence=VSP_054707;
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
CC       {ECO:0000269|PubMed:15355968}.
CC   -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC       a tight interaction with the extracellular matrix. {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 1 (WMS1) [MIM:277600]: A rare
CC       connective tissue disorder characterized by short stature,
CC       brachydactyly, joint stiffness, and eye abnormalities including
CC       microspherophakia, ectopia lentis, severe myopia and glaucoma.
CC       {ECO:0000269|PubMed:15368195, ECO:0000269|PubMed:18567016}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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DR   EMBL; AC092315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF163762; AAG35563.1; -; mRNA.
DR   CCDS; CCDS12206.1; -. [Q9H324-1]
DR   CCDS; CCDS62529.1; -. [Q9H324-2]
DR   RefSeq; NP_001269281.1; NM_001282352.1. [Q9H324-2]
DR   RefSeq; NP_112219.3; NM_030957.3.
DR   AlphaFoldDB; Q9H324; -.
DR   SMR; Q9H324; -.
DR   BioGRID; 123586; 13.
DR   IntAct; Q9H324; 12.
DR   MINT; Q9H324; -.
DR   STRING; 9606.ENSP00000471851; -.
DR   MEROPS; M12.235; -.
DR   GlyCosmos; Q9H324; 6 sites, No reported glycans.
DR   GlyGen; Q9H324; 6 sites.
DR   iPTMnet; Q9H324; -.
DR   PhosphoSitePlus; Q9H324; -.
DR   BioMuta; ADAMTS10; -.
DR   DMDM; 148887344; -.
DR   MassIVE; Q9H324; -.
DR   PaxDb; 9606-ENSP00000270328; -.
DR   PeptideAtlas; Q9H324; -.
DR   Antibodypedia; 51079; 193 antibodies from 29 providers.
DR   DNASU; 81794; -.
DR   Ensembl; ENST00000595838.5; ENSP00000470501.1; ENSG00000142303.14. [Q9H324-2]
DR   GeneID; 81794; -.
DR   KEGG; hsa:81794; -.
DR   UCSC; uc002mki.3; human. [Q9H324-1]
DR   AGR; HGNC:13201; -.
DR   CTD; 81794; -.
DR   DisGeNET; 81794; -.
DR   GeneCards; ADAMTS10; -.
DR   GeneReviews; ADAMTS10; -.
DR   HGNC; HGNC:13201; ADAMTS10.
DR   HPA; ENSG00000142303; Low tissue specificity.
DR   MalaCards; ADAMTS10; -.
DR   MIM; 277600; phenotype.
DR   MIM; 608990; gene.
DR   neXtProt; NX_Q9H324; -.
DR   OpenTargets; ENSG00000142303; -.
DR   Orphanet; 3449; Weill-Marchesani syndrome.
DR   PharmGKB; PA24537; -.
DR   VEuPathDB; HostDB:ENSG00000142303; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158404; -.
DR   HOGENOM; CLU_554988_0_0_1; -.
DR   InParanoid; Q9H324; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; Q9H324; -.
DR   TreeFam; TF313537; -.
DR   PathwayCommons; Q9H324; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q9H324; -.
DR   BioGRID-ORCS; 81794; 19 hits in 1146 CRISPR screens.
DR   ChiTaRS; ADAMTS10; human.
DR   GeneWiki; ADAMTS10; -.
DR   GenomeRNAi; 81794; -.
DR   Pharos; Q9H324; Tbio.
DR   PRO; PR:Q9H324; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9H324; Protein.
DR   Bgee; ENSG00000142303; Expressed in descending thoracic aorta and 179 other cell types or tissues.
DR   ExpressionAtlas; Q9H324; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0001527; C:microfibril; IDA:UniProtKB.
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   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:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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; 5.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9H324; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues; Disease variant;
KW   Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..233
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029184"
FT   CHAIN           234..1103
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 10"
FT                   /id="PRO_0000029185"
FT   DOMAIN          239..457
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          460..546
FT                   /note="Disintegrin"
FT   DOMAIN          547..602
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          825..883
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          884..945
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          947..1001
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1003..1058
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1065..1103
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          213..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..828
FT                   /note="Spacer"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        90
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        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        795
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        892
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        315..376
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        370..452
FT                   /evidence="ECO:0000250"
FT   DISULFID        409..436
FT                   /evidence="ECO:0000250"
FT   DISULFID        479..501
FT                   /evidence="ECO:0000250"
FT   DISULFID        490..508
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..531
FT                   /evidence="ECO:0000250"
FT   DISULFID        521..536
FT                   /evidence="ECO:0000250"
FT   DISULFID        559..596
FT                   /evidence="ECO:0000250"
FT   DISULFID        563..601
FT                   /evidence="ECO:0000250"
FT   DISULFID        574..586
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..637
FT                   /note="MAPACQILRWALALGLGLMFEVTHAFRSQDEFLSSLESYEIAFPTRVDHNGA
FT                   LLAFSPPPPRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREG
FT                   LAWQRAARPHCLYAGHLQGQASTSHVAISTCGGLHGLIVADEEEYLIEPLHGGPKGSRS
FT                   PEESGPHVVYKRSSLRHPHLDTACGVRDEKPWKGRPWWLRTLKPPPARPLGNETERGQP
FT                   GLKRSVSRERYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILV
FT                   TRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVNHSGHGNAIPENGVANHDTAVLITR
FT                   YDICIYKNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTFGMNHDGVG
FT                   NSCGARGQDPAKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLNNRPPRQDFVYP
FT                   TVAPGQAYDADEQCRFQHGVKSRQCKYGEVCSELWCLSKSNRCITNSIPAAEGTLCQTH
FT                   TIDKGWCYKRVCVPFGSRPEGVDGAWGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGG
FT                   KYCLGERRRHRSCNTDDCPPGSQDFREVQCSEFDSIPFRGKFYKWKTYRGGGVK -> M
FT                   GPTSVLRAGLTPSCLPPPSGATNGSVSPLGRAQRVWTEPGGRGLHGATAAGPVAAACPL
FT                   LAVTATAPGQPSGASTVWVREGGTAPATRMTVPLAPRTSEKCSVLNLTASLSVGNSTSG
FT                   KRTGE (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054707"
FT   VARIANT         25
FT                   /note="A -> T (in WMS1; shows consistent and significantly
FT                   diminished protein secretion)"
FT                   /evidence="ECO:0000269|PubMed:18567016"
FT                   /id="VAR_054439"
FT   VARIANT         119
FT                   /note="R -> Q (in dbSNP:rs3814291)"
FT                   /id="VAR_054440"
FT   VARIANT         134
FT                   /note="T -> S (in dbSNP:rs7255721)"
FT                   /evidence="ECO:0000269|PubMed:15355968"
FT                   /id="VAR_054441"
FT   CONFLICT        385..386
FT                   /note="AT -> PQ (in Ref. 2; AAG35563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="S -> N (in Ref. 2; AAG35563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        643
FT                   /note="C -> S (in Ref. 2; AAG35563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1101
FT                   /note="H -> Q (in Ref. 2; AAG35563)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1103 AA;  120874 MW;  D7558271C303A87C CRC64;
     MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPP
     PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG HVSVEYWTRE GLAWQRAARP
     HCLYAGHLQG QASTSHVAIS TCGGLHGLIV ADEEEYLIEP LHGGPKGSRS PEESGPHVVY
     KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY
     VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT
     LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT
     LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM
     AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR
     FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG
     SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD
     CPPGSQDFRE VQCSEFDSIP FRGKFYKWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD
     GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPASPGAG
     YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ
     GPDQVQSLEA LGPINASLIV MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ
     CAGGSQVQAV ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSLCSRSC
     DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA LDWSECTPSC
     GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR RCPPARWVAG EWGECSAQCG
     VGQRQRSVRC TSHTGQASHE CTEALRPPTT QQCEAKCDSP TPGDGPEECK DVNKVAYCPL
     VLKFQFCSRA YFRQMCCKTC HGH
//