ID   ATS1_MOUSE              Reviewed;         968 AA.
AC   P97857; E9QMN9; O54768;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   24-JAN-2024, entry version 194.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1;
DE            Short=ADAM-TS 1;
DE            Short=ADAM-TS1;
DE            Short=ADAMTS-1;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=Adamts1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9441751; DOI=10.1006/geno.1997.5064;
RA   Kuno K., Lizasa H., Ohno S., Matsushima K.;
RT   "The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1
RT   gene encoding an ADAM family protein with TSP motifs.";
RL   Genomics 46:466-471(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8995297; DOI=10.1074/jbc.272.1.556;
RA   Kuno K., Kanada N., Nakashima E., Fujiki F., Ichimura F., Matsushima K.;
RT   "Molecular cloning of a gene encoding a new type of metalloproteinase-
RT   disintegrin family protein with thrombospondin motifs as an inflammation
RT   associated gene.";
RL   J. Biol. Chem. 272:556-562(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb, and Mammary gland;
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   [5]
RP   CHARACTERIZATION, AND MUTAGENESIS OF GLU-403.
RX   PubMed=10373500; DOI=10.1074/jbc.274.26.18821;
RA   Kuno K., Terashima Y., Matsushima K.;
RT   "ADAMTS-1 is an active metalloproteinase associated with the extracellular
RT   matrix.";
RL   J. Biol. Chem. 274:18821-18826(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=10930576; DOI=10.1016/s0014-5793(00)01854-8;
RA   Kuno K., Okada Y., Kawashima H., Nakamura H., Miyasaka M., Ohno H.,
RA   Matsushima K.;
RT   "ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan.";
RL   FEBS Lett. 478:241-245(2000).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10781075; DOI=10.1073/pnas.080073497;
RA   Robker R.L., Russell D.L., Espey L.L., Lydon J.P., O'Malley B.W.,
RA   Richards J.S.;
RT   "Progesterone-regulated genes in the ovulation process: ADAMTS-1 and
RT   cathepsin L proteases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4689-4694(2000).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23233679; DOI=10.1074/jbc.m112.429647;
RA   Stupka N., Kintakas C., White J.D., Fraser F.W., Hanciu M.,
RA   Aramaki-Hattori N., Martin S., Coles C., Collier F., Ward A.C., Apte S.S.,
RA   McCulloch D.R.;
RT   "Versican processing by a disintegrin-like and metalloproteinase domain
RT   with thrombospondin-1 repeats proteinases-5 and -15 facilitates myoblast
RT   fusion.";
RL   J. Biol. Chem. 288:1907-1917(2013).
CC   -!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-
CC       Glu-|-Leu-1692' site (within the chondroitin sulfate attachment
CC       domain), and may be involved in its turnover. Has angiogenic inhibitor
CC       activity (By similarity). Active metalloprotease, which may be
CC       associated with various inflammatory processes as well as development
CC       of cancer cachexia. May play a critical role in follicular rupture (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:10781075,
CC       ECO:0000269|PubMed:10930576}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- DEVELOPMENTAL STAGE: In embryonic skeletal muscle, significantly
CC       increased levels between 13.5 dpc and 15.5 dpc with maximal expression
CC       observed at 15.5 dpc (PubMed:23233679). Decreased levels in postnatal
CC       skeletal muscle (PubMed:23233679). In myoblasts, up-regulated soon
CC       after induction of myoblast differentiation (PubMed:23233679).
CC       {ECO:0000269|PubMed:23233679}.
CC   -!- INDUCTION: Induced in vitro in colon adenocarcinoma cells by
CC       interleukin-1, or in vivo in kidney and heart by lipopolysaccharide.
CC       Also induced by LH stimulation in granulosa cells of preovulatory
CC       follicles. {ECO:0000269|PubMed:10781075}.
CC   -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC       a tight interaction with the extracellular matrix.
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.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11088.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA24501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB001735; BAA24501.1; ALT_INIT; Genomic_DNA.
DR   EMBL; D67076; BAA11088.1; ALT_FRAME; mRNA.
DR   EMBL; AC126936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040382; AAH40382.1; -; mRNA.
DR   EMBL; BC050834; AAH50834.1; -; mRNA.
DR   CCDS; CCDS28287.1; -.
DR   PIR; T00017; T00017.
DR   RefSeq; NP_033751.3; NM_009621.5.
DR   AlphaFoldDB; P97857; -.
DR   SMR; P97857; -.
DR   BioGRID; 197974; 4.
DR   STRING; 10090.ENSMUSP00000023610; -.
DR   MEROPS; M12.222; -.
DR   GlyCosmos; P97857; 5 sites, No reported glycans.
DR   GlyGen; P97857; 8 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P97857; -.
DR   PhosphoSitePlus; P97857; -.
DR   CPTAC; non-CPTAC-3962; -.
DR   MaxQB; P97857; -.
DR   PaxDb; 10090-ENSMUSP00000023610; -.
DR   PeptideAtlas; P97857; -.
DR   ProteomicsDB; 277135; -.
DR   Pumba; P97857; -.
DR   Antibodypedia; 4291; 460 antibodies from 33 providers.
DR   DNASU; 11504; -.
DR   Ensembl; ENSMUST00000023610.15; ENSMUSP00000023610.9; ENSMUSG00000022893.15.
DR   GeneID; 11504; -.
DR   KEGG; mmu:11504; -.
DR   UCSC; uc012aho.1; mouse.
DR   AGR; MGI:109249; -.
DR   CTD; 9510; -.
DR   MGI; MGI:109249; Adamts1.
DR   VEuPathDB; HostDB:ENSMUSG00000022893; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000156815; -.
DR   HOGENOM; CLU_000660_3_0_1; -.
DR   InParanoid; P97857; -.
DR   OMA; VNRDSHM; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; P97857; -.
DR   TreeFam; TF331949; -.
DR   BRENDA; 3.4.24.B11; 3474.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   BioGRID-ORCS; 11504; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Adamts1; mouse.
DR   PRO; PR:P97857; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P97857; Protein.
DR   Bgee; ENSMUSG00000022893; Expressed in iris and 265 other cell types or tissues.
DR   ExpressionAtlas; P97857; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
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; 3.
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; IPR013274; Pept_M12B_ADAM-TS1.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 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; 2.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01858; ADAMTS1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00209; TSP1; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; P97857; MM.
PE   1: Evidence at protein level;
KW   Calcium; Cleavage on pair of basic residues; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Heparin-binding; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000255"
FT   PROPEP          49..253
FT                   /id="PRO_0000029152"
FT   CHAIN           254..968
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 1"
FT                   /id="PRO_0000029153"
FT   DOMAIN          259..468
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          477..559
FT                   /note="Disintegrin"
FT   DOMAIN          560..615
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          855..911
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          912..968
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..850
FT                   /note="Spacer"
FT   MOTIF           204..211
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        218..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000269|PubMed:10373500"
FT   BINDING         206
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         262
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         262
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         406
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         463
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         466
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   BINDING         466
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        765
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        783
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        946
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        334..386
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        363..368
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        380..463
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        418..447
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        489..512
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        500..522
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        507..541
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        535..546
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT   DISULFID        572..609
FT                   /evidence="ECO:0000250"
FT   DISULFID        576..614
FT                   /evidence="ECO:0000250"
FT   DISULFID        587..599
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         403
FT                   /note="E->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10373500"
FT   CONFLICT        335
FT                   /note="S -> N (in Ref. 1; BAA24501 and 4;
FT                   AAH40382/AAH50834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="S -> T (in Ref. 1; BAA24501 and 4;
FT                   AAH40382/AAH50834)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   968 AA;  105801 MW;  90A44F7D5262B6C5 CRC64;
     MQPKVPLGSR KQKPCSDMGD VQRAARSRGS LSAHMLLLLL ASITMLLCAR GAHGRPTEED
     EELVLPSLER APGHDSTTTR LRLDAFGQQL HLKLQPDSGF LAPGFTLQTV GRSPGSEAQH
     LDPTGDLAHC FYSGTVNGDP GSAAALSLCE GVRGAFYLQG EEFFIQPAPG VATERLAPAV
     PEEESSARPQ FHILRRRRRG SGGAKCGVMD DETLPTSDSR PESQNTRNQW PVRDPTPQDA
     GKPSGPGSIR KKRFVSSPRY VETMLVADQS MADFHGSGLK HYLLTLFSVA ARFYKHPSIR
     NSISLVVVKI LVIYEEQKGP EVTSNAALTL RNFCSWQKQH NSPSDRDPEH YDTAILFTRQ
     DLCGSHTCDT LGMADVGTVC DPSRSCSVIE DDGLQAAFTT AHELGHVFNM PHDDAKHCAS
     LNGVSGDSHL MASMLSSLDH SQPWSPCSAY MVTSFLDNGH GECLMDKPQN PIKLPSDLPG
     TLYDANRQCQ FTFGEESKHC PDAASTCTTL WCTGTSGGLL VCQTKHFPWA DGTSCGEGKW
     CVSGKCVNKT DMKHFATPVH GSWGPWGPWG DCSRTCGGGV QYTMRECDNP VPKNGGKYCE
     GKRVRYRSCN IEDCPDNNGK TFREEQCEAH NEFSKASFGN EPTVEWTPKY AGVSPKDRCK
     LTCEAKGIGY FFVLQPKVVD GTPCSPDSTS VCVQGQCVKA GCDRIIDSKK KFDKCGVCGG
     NGSTCKKMSG IVTSTRPGYH DIVTIPAGAT NIEVKHRNQR GSRNNGSFLA IRAADGTYIL
     NGNFTLSTLE QDLTYKGTVL RYSGSSAALE RIRSFSPLKE PLTIQVLMVG HALRPKIKFT
     YFMKKKTESF NAIPTFSEWV IEEWGECSKT CGSGWQRRVV QCRDINGHPA SECAKEVKPA
     STRPCADLPC PHWQVGDWSP CSKTCGKGYK KRTLKCVSHD GGVLSNESCD PLKKPKHYID
     FCTLTQCS
//