ID   ATS2_HUMAN              Reviewed;        1211 AA.
AC   O95450;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 221.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2;
DE            Short=ADAM-TS 2;
DE            Short=ADAM-TS2;
DE            Short=ADAMTS-2;
DE            EC=3.4.24.14;
DE   AltName: Full=Procollagen I N-proteinase;
DE            Short=PC I-NP;
DE   AltName: Full=Procollagen I/II amino propeptide-processing enzyme;
DE   AltName: Full=Procollagen N-endopeptidase;
DE            Short=pNPI;
DE   Flags: Precursor;
GN   Name=ADAMTS2; Synonyms=PCINP, PCPNI;
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] (ISOFORMS LPNPI AND SPNPI), AND INVOLVEMENT IN
RP   EDSDERMS.
RC   TISSUE=Skin;
RX   PubMed=10417273; DOI=10.1086/302504;
RA   Colige A., Sieron A.L., Li S.-W., Schwarze U., Petty E., Wertelecki W.,
RA   Wilcox W., Krakow D., Cohn D.H., Reardon W., Byers P.H., Lapiere C.M.,
RA   Prockop D.J., Nusgens B.V.;
RT   "Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are
RT   caused by mutations in the procollagen I N-proteinase gene.";
RL   Am. J. Hum. Genet. 65:308-317(1999).
RN   [2]
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   [3]
RP   FUNCTION.
RX   PubMed=31152061; DOI=10.1074/jbc.ra119.007806;
RA   Rosell-Garcia T., Paradela A., Bravo G., Dupont L., Bekhouche M.,
RA   Colige A., Rodriguez-Pascual F.;
RT   "Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and
RT   ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain.";
RL   J. Biol. Chem. 294:11087-11100(2019).
CC   -!- FUNCTION: Cleaves the propeptides of type I and II collagen prior to
CC       fibril assembly (By similarity). Does not act on type III collagen (By
CC       similarity). Cleaves lysyl oxidase LOX at a site downstream of its
CC       propeptide cleavage site to produce a short LOX form with reduced
CC       collagen-binding activity (PubMed:31152061).
CC       {ECO:0000250|UniProtKB:P79331, ECO:0000269|PubMed:31152061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-
CC         Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln.; EC=3.4.24.14;
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: May belong to a multimeric complex. Binds specifically to
CC       collagen type XIV (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=LpNPI;
CC         IsoId=O95450-1; Sequence=Displayed;
CC       Name=SpNPI;
CC         IsoId=O95450-2; Sequence=VSP_005497, VSP_005498;
CC   -!- TISSUE SPECIFICITY: Expressed at high level in skin, bone, tendon and
CC       aorta and at low levels in thymus and brain.
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   -!- DISEASE: Ehlers-Danlos syndrome, dermatosparaxis type (EDSDERMS)
CC       [MIM:225410]: A form of Ehlers-Danlos syndrome, a group of connective
CC       tissue disorders characterized by skin hyperextensibility, articular
CC       hypermobility, and tissue fragility. EDSDERMS is an autosomal recessive
CC       form characterized by extreme skin fragility and easy bruising, large
CC       fontanels, blue sclerae, puffy eyelids, micrognathia, umbilical hernia,
CC       and short fingers. Joint hypermobility becomes more important with age.
CC       {ECO:0000269|PubMed:10417273}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform SpNPI]: Has no significant N-procollagen
CC       peptidase activity. {ECO:0000305}.
CC   -!- CAUTION: Has sometimes been referred to as ADAMTS3. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ003125; CAA05880.1; -; mRNA.
DR   EMBL; AC008544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS34311.1; -. [O95450-2]
DR   CCDS; CCDS4444.1; -. [O95450-1]
DR   RefSeq; NP_055059.2; NM_014244.4. [O95450-1]
DR   RefSeq; NP_067610.1; NM_021599.3. [O95450-2]
DR   AlphaFoldDB; O95450; -.
DR   SMR; O95450; -.
DR   BioGRID; 114887; 54.
DR   IntAct; O95450; 16.
DR   STRING; 9606.ENSP00000251582; -.
DR   MEROPS; M12.301; -.
DR   GlyCosmos; O95450; 9 sites, 1 glycan.
DR   GlyGen; O95450; 11 sites, 2 O-linked glycans (3 sites).
DR   iPTMnet; O95450; -.
DR   PhosphoSitePlus; O95450; -.
DR   SwissPalm; O95450; -.
DR   BioMuta; ADAMTS2; -.
DR   jPOST; O95450; -.
DR   MassIVE; O95450; -.
DR   PaxDb; 9606-ENSP00000251582; -.
DR   PeptideAtlas; O95450; -.
DR   ProteomicsDB; 50883; -. [O95450-1]
DR   ProteomicsDB; 50884; -. [O95450-2]
DR   Antibodypedia; 17642; 203 antibodies from 29 providers.
DR   DNASU; 9509; -.
DR   Ensembl; ENST00000251582.12; ENSP00000251582.7; ENSG00000087116.17. [O95450-1]
DR   Ensembl; ENST00000274609.5; ENSP00000274609.5; ENSG00000087116.17. [O95450-2]
DR   GeneID; 9509; -.
DR   KEGG; hsa:9509; -.
DR   MANE-Select; ENST00000251582.12; ENSP00000251582.7; NM_014244.5; NP_055059.2.
DR   UCSC; uc003mjw.3; human. [O95450-1]
DR   AGR; HGNC:218; -.
DR   CTD; 9509; -.
DR   DisGeNET; 9509; -.
DR   GeneCards; ADAMTS2; -.
DR   HGNC; HGNC:218; ADAMTS2.
DR   HPA; ENSG00000087116; Low tissue specificity.
DR   MalaCards; ADAMTS2; -.
DR   MIM; 225410; phenotype.
DR   MIM; 604539; gene.
DR   neXtProt; NX_O95450; -.
DR   OpenTargets; ENSG00000087116; -.
DR   Orphanet; 1901; Dermatosparaxis Ehlers-Danlos syndrome.
DR   PharmGKB; PA24546; -.
DR   VEuPathDB; HostDB:ENSG00000087116; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000156647; -.
DR   HOGENOM; CLU_000660_4_1_1; -.
DR   InParanoid; O95450; -.
DR   OMA; ICPRNIS; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; O95450; -.
DR   TreeFam; TF313537; -.
DR   BRENDA; 3.4.24.14; 2681.
DR   PathwayCommons; O95450; -.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; O95450; -.
DR   BioGRID-ORCS; 9509; 16 hits in 1147 CRISPR screens.
DR   ChiTaRS; ADAMTS2; human.
DR   GeneWiki; ADAMTS2; -.
DR   GenomeRNAi; 9509; -.
DR   Pharos; O95450; Tbio.
DR   PRO; PR:O95450; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; O95450; Protein.
DR   Bgee; ENSG00000087116; Expressed in stromal cell of endometrium and 94 other cell types or tissues.
DR   ExpressionAtlas; O95450; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   GO; GO:0043588; P:skin development; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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; 4.
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; IPR013275; Pept_M12B_ADAM-TS2.
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:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 3.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01859; ADAMTS2.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 4.
DR   Genevisible; O95450; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Collagen degradation; Disulfide bond;
KW   Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..253
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029158"
FT   CHAIN           254..1211
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 2"
FT                   /id="PRO_0000029159"
FT   DOMAIN          266..470
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          480..560
FT                   /note="Disintegrin"
FT   DOMAIN          561..616
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          854..912
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          914..971
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          975..1029
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1059..1097
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          723..851
FT                   /note="Spacer"
FT   REGION          1170..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           691..693
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        949
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        993
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1031
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1098
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        343..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        386..465
FT                   /evidence="ECO:0000250"
FT   DISULFID        425..451
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..517
FT                   /evidence="ECO:0000250"
FT   DISULFID        503..526
FT                   /evidence="ECO:0000250"
FT   DISULFID        512..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        539..550
FT                   /evidence="ECO:0000250"
FT   DISULFID        573..610
FT                   /evidence="ECO:0000250"
FT   DISULFID        577..615
FT                   /evidence="ECO:0000250"
FT   DISULFID        588..600
FT                   /evidence="ECO:0000250"
FT   DISULFID        987..1023
FT                   /evidence="ECO:0000250"
FT   DISULFID        991..1028
FT                   /evidence="ECO:0000250"
FT   DISULFID        1002..1012
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         544..566
FT                   /note="HCFKGHCIWLTPDILKRDGSWGA -> FRPGAVAHACYPSTLGGQGRWIA
FT                   (in isoform SpNPI)"
FT                   /evidence="ECO:0000303|PubMed:10417273"
FT                   /id="VSP_005497"
FT   VAR_SEQ         567..1211
FT                   /note="Missing (in isoform SpNPI)"
FT                   /evidence="ECO:0000303|PubMed:10417273"
FT                   /id="VSP_005498"
FT   VARIANT         74
FT                   /note="V -> M (in dbSNP:rs2271211)"
FT                   /id="VAR_047927"
FT   VARIANT         241
FT                   /note="R -> H (in dbSNP:rs11750821)"
FT                   /id="VAR_047928"
FT   VARIANT         245
FT                   /note="V -> I (in dbSNP:rs398829)"
FT                   /id="VAR_020058"
FT   VARIANT         331
FT                   /note="E -> K (in dbSNP:rs17667857)"
FT                   /id="VAR_047929"
FT   VARIANT         665
FT                   /note="G -> R (in dbSNP:rs35372714)"
FT                   /id="VAR_047930"
FT   VARIANT         827
FT                   /note="R -> Q (in dbSNP:rs35445112)"
FT                   /id="VAR_047931"
FT   VARIANT         1177
FT                   /note="P -> S (in dbSNP:rs1054480)"
FT                   /id="VAR_020059"
FT   CONFLICT        1001
FT                   /note="L -> P (in Ref. 1; CAA05880)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1089
FT                   /note="C -> S (in Ref. 1; CAA05880)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1211 AA;  134755 MW;  6C4F2C2D46A1F925 CRC64;
     MDPPAGAARR LLCPALLLLL LLLPPPLLPP PPPPANARLA AAADPPGGPL GHGAERILAV
     PVRTDAQGRL VSHVVSAATS RAGVRARRAA PVRTPSFPGG NEEEPGSHLF YNVTVFGRDL
     HLRLRPNARL VAPGATMEWQ GEKGTTRVEP LLGSCLYVGD VAGLAEASSV ALSNCDGLAG
     LIRMEEEEFF IEPLEKGLAA QEAEQGRVHV VYRRPPTSPP LGGPQALDTG ASLDSLDSLS
     RALGVLEEHA NSSRRRARRH AADDDYNIEV LLGVDDSVVQ FHGKEHVQKY LLTLMNIVNE
     IYHDESLGAH INVVLVRIIL LSYGKSMSLI EIGNPSQSLE NVCRWAYLQQ KPDTGHDEYH
     DHAIFLTRQD FGPSGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG
     QGNRCGDEVR LGSIMAPLVQ AAFHRFHWSR CSQQELSRYL HSYDCLLDDP FAHDWPALPQ
     LPGLHYSMNE QCRFDFGLGY MMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTMCA
     PGKHCFKGHC IWLTPDILKR DGSWGAWSPF GSCSRTCGTG VKFRTRQCDN PHPANGGRTC
     SGLAYDFQLC SRQDCPDSLA DFREEQCRQW DLYFEHGDAQ HHWLPHEHRD AKERCHLYCE
     SRETGEVVSM KRMVHDGTRC SYKDAFSLCV RGDCRKVGCD GVIGSSKQED KCGVCGGDNS
     HCKVVKGTFT RSPKKHGYIK MFEIPAGARH LLIQEVDATS HHLAVKNLET GKFILNEEND
     VDASSKTFIA MGVEWEYRDE DGRETLQTMG PLHGTITVLV IPVGDTRVSL TYKYMIHEDS
     LNVDDNNVLE EDSVVYEWAL KKWSPCSKPC GGGSQFTKYG CRRRLDHKMV HRGFCAALSK
     PKAIRRACNP QECSQPVWVT GEWEPCSQTC GRTGMQVRSV RCIQPLHDNT TRSVHAKHCN
     DARPESRRAC SRELCPGRWR AGPWSQCSVT CGNGTQERPV LCRTADDSFG ICQEERPETA
     RTCRLGPCPR NISDPSKKSY VVQWLSRPDP DSPIRKISSK GHCQGDKSIF CRMEVLSRYC
     SIPGYNKLCC KSCNLYNNLT NVEGRIEPPP GKHNDIDVFM PTLPVPTVAM EVRPSPSTPL
     EVPLNASSTN ATEDHPETNA VDEPYKIHGL EDEVQPPNLI PRRPSPYEKT RNQRIQELID
     EMRKKEMLGK F
//