ID   ATS7_HUMAN              Reviewed;        1686 AA.
AC   Q9UKP4; Q14F51; Q6P7J9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7;
DE            Short=ADAM-TS 7;
DE            Short=ADAM-TS7;
DE            Short=ADAMTS-7;
DE            EC=3.4.24.-;
DE   AltName: Full=COMPase;
DE   Flags: Precursor;
GN   Name=ADAMTS7;
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], FUNCTION, COFACTOR, PH DEPENDENCE, INTERACTION
RP   WITH COMP, INDUCTION, TISSUE SPECIFICITY, AND VARIANTS ALA-1319; SER-1414
RP   AND ALA-1583.
RX   PubMed=16585064; DOI=10.1096/fj.05-3877fje;
RA   Liu C.-J., Kong W., Ilalov K., Yu S., Xu K., Prazak L., Fajardo M.,
RA   Sehgal B., Di Cesare P.E.;
RT   "ADAMTS-7: a metalloproteinase that directly binds to and degrades
RT   cartilage oligomeric matrix protein.";
RL   FASEB J. 20:988-990(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-307.
RC   TISSUE=Ovary;
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   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
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   [4]
RP   PROTEIN SEQUENCE OF 237-243, IDENTIFICATION, GLYCOSYLATION, PROTEOLYTIC
RP   PROCESSING, AND TISSUE SPECIFICITY.
RX   PubMed=15192113; DOI=10.1074/jbc.m402380200;
RA   Somerville R.P.T., Longpre J.-M., Apel E.D., Lewis R.M., Wang L.W.,
RA   Sanes J.R., Leduc R., Apte S.S.;
RT   "ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin
RT   sulfate proteoglycan containing a mucin domain.";
RL   J. Biol. Chem. 279:35159-35175(2004).
CC   -!- FUNCTION: Metalloprotease that may play a role in the degradation of
CC       COMP. {ECO:0000269|PubMed:16585064}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 7.5 and 9.5. {ECO:0000269|PubMed:16585064};
CC   -!- SUBUNIT: Interacts with COMP. {ECO:0000269|PubMed:16585064}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}. Note=Also found associated with the external cell
CC       surface. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC       skeletal muscle, kidney and pancreas. Detected in meniscus, bone,
CC       tendon, cartilage, synovium, fat and ligaments.
CC       {ECO:0000269|PubMed:15192113, ECO:0000269|PubMed:16585064}.
CC   -!- INDUCTION: Up-regulated in articular cartilage and synovium from
CC       arthritis patients. {ECO:0000269|PubMed:16585064}.
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: N-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. N- and C-
CC       glycosylations can also facilitate secretion. O-glycosylated
CC       proteoglycan. Contains chondroitin sulfate.
CC       {ECO:0000269|PubMed:15192113}.
CC   -!- PTM: May be cleaved by a furin endopeptidase (By similarity). The
CC       precursor is sequentially processed. {ECO:0000250,
CC       ECO:0000269|PubMed:15192113}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD56358.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AY327122; AAQ94616.1; -; mRNA.
DR   EMBL; BC061631; AAH61631.1; -; mRNA.
DR   EMBL; AF140675; AAD56358.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS32303.1; -.
DR   RefSeq; NP_055087.2; NM_014272.4.
DR   AlphaFoldDB; Q9UKP4; -.
DR   SMR; Q9UKP4; -.
DR   BioGRID; 116344; 102.
DR   IntAct; Q9UKP4; 4.
DR   STRING; 9606.ENSP00000373472; -.
DR   MEROPS; M12.231; -.
DR   GlyCosmos; Q9UKP4; 17 sites, 2 glycans.
DR   GlyGen; Q9UKP4; 21 sites, 3 O-linked glycans (18 sites).
DR   iPTMnet; Q9UKP4; -.
DR   PhosphoSitePlus; Q9UKP4; -.
DR   BioMuta; ADAMTS7; -.
DR   DMDM; 205371741; -.
DR   EPD; Q9UKP4; -.
DR   MassIVE; Q9UKP4; -.
DR   PaxDb; 9606-ENSP00000373472; -.
DR   PeptideAtlas; Q9UKP4; -.
DR   ProteomicsDB; 84828; -.
DR   Antibodypedia; 27710; 199 antibodies from 21 providers.
DR   DNASU; 11173; -.
DR   Ensembl; ENST00000388820.5; ENSP00000373472.4; ENSG00000136378.15.
DR   GeneID; 11173; -.
DR   KEGG; hsa:11173; -.
DR   MANE-Select; ENST00000388820.5; ENSP00000373472.4; NM_014272.5; NP_055087.2.
DR   UCSC; uc002bej.4; human.
DR   AGR; HGNC:223; -.
DR   CTD; 11173; -.
DR   DisGeNET; 11173; -.
DR   GeneCards; ADAMTS7; -.
DR   HGNC; HGNC:223; ADAMTS7.
DR   HPA; ENSG00000136378; Tissue enriched (heart).
DR   MIM; 605009; gene.
DR   neXtProt; NX_Q9UKP4; -.
DR   OpenTargets; ENSG00000136378; -.
DR   PharmGKB; PA24551; -.
DR   VEuPathDB; HostDB:ENSG00000136378; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000159819; -.
DR   HOGENOM; CLU_000660_2_1_1; -.
DR   InParanoid; Q9UKP4; -.
DR   OMA; YCSERQA; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; Q9UKP4; -.
DR   TreeFam; TF313537; -.
DR   PathwayCommons; Q9UKP4; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q9UKP4; -.
DR   BioGRID-ORCS; 11173; 14 hits in 1148 CRISPR screens.
DR   ChiTaRS; ADAMTS7; human.
DR   GenomeRNAi; 11173; -.
DR   Pharos; Q9UKP4; Tbio.
DR   PRO; PR:Q9UKP4; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9UKP4; Protein.
DR   Bgee; ENSG00000136378; Expressed in right atrium auricular region and 87 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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; IDA:BHF-UCL.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IDA:BHF-UCL.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IMP:BHF-UCL.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR   GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:BHF-UCL.
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; 8.
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; 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; 7.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 8.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 8.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 7.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9UKP4; HS.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Proteoglycan; Reference proteome;
KW   Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..236
FT                   /evidence="ECO:0000269|PubMed:15192113"
FT                   /id="PRO_0000029176"
FT   CHAIN           237..1686
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 7"
FT                   /id="PRO_0000029177"
FT   DOMAIN          242..452
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          462..537
FT                   /note="Disintegrin"
FT   DOMAIN          538..593
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          821..880
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          881..940
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          942..995
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1411..1459
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1462..1522
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1523..1567
FT                   /note="TSP type-1 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1569..1629
FT                   /note="TSP type-1 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1632..1672
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          698..809
FT                   /note="Spacer"
FT   REGION          1024..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1666..1686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           202..209
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1098..1112
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         204
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         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        318..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..354
FT                   /evidence="ECO:0000250"
FT   DISULFID        366..447
FT                   /evidence="ECO:0000250"
FT   DISULFID        405..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        474..497
FT                   /evidence="ECO:0000250"
FT   DISULFID        485..503
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..522
FT                   /evidence="ECO:0000250"
FT   DISULFID        516..527
FT                   /evidence="ECO:0000250"
FT   DISULFID        550..587
FT                   /evidence="ECO:0000250"
FT   DISULFID        554..592
FT                   /evidence="ECO:0000250"
FT   DISULFID        565..577
FT                   /evidence="ECO:0000250"
FT   VARIANT         214
FT                   /note="S -> P (in dbSNP:rs3825807)"
FT                   /id="VAR_046112"
FT   VARIANT         307
FT                   /note="T -> M (in dbSNP:rs2127898)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_046113"
FT   VARIANT         1319
FT                   /note="T -> A (in dbSNP:rs11630236)"
FT                   /evidence="ECO:0000269|PubMed:16585064"
FT                   /id="VAR_046114"
FT   VARIANT         1414
FT                   /note="G -> S (in dbSNP:rs2929155)"
FT                   /evidence="ECO:0000269|PubMed:16585064"
FT                   /id="VAR_046115"
FT   VARIANT         1583
FT                   /note="G -> A (in dbSNP:rs7495616)"
FT                   /evidence="ECO:0000269|PubMed:16585064"
FT                   /id="VAR_046116"
FT   CONFLICT        642
FT                   /note="E -> K (in Ref. 1; AAD56358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1101
FT                   /note="H -> R (in Ref. 2; AAQ94616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1364
FT                   /note="S -> T (in Ref. 2; AAQ94616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1479
FT                   /note="G -> D (in Ref. 2; AAQ94616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1511
FT                   /note="P -> H (in Ref. 2; AAQ94616)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1686 AA;  184095 MW;  AB38264B8E8DB740 CRC64;
     MPGGPSPRSP APLLRPLLLL LCALAPGAPG PAPGRATEGR AALDIVHPVR VDAGGSFLSY
     ELWPRALRKR DVSVRRDAPA FYELQYRGRE LRFNLTANQH LLAPGFVSET RRRGGLGRAH
     IRAHTPACHL LGEVQDPELE GGLAAISACD GLKGVFQLSN EDYFIEPLDS APARPGHAQP
     HVVYKRQAPE RLAQRGDSSA PSTCGVQVYP ELESRRERWE QRQQWRRPRL RRLHQRSVSK
     EKWVETLVVA DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE
     EEDLKITHHA DNTLKSFCKW QKSINMKGDA HPLHHDTAIL LTRKDLCAAM NRPCETLGLS
     HVAGMCQPHR SCSINEDTGL PLAFTVAHEL GHSFGIQHDG SGNDCEPVGK RPFIMSPQLL
     YDAAPLTWSR CSRQYITRFL DRGWGLCLDD PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA
     YSAFCEDMDN VCHTLWCSVG TTCHSKLDAA VDGTRCGENK WCLSGECVPV GFRPEAVDGG
     WSGWSAWSIC SRSCGMGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR
     HVQCSHFDAM LYKGQLHTWV PVVNDVNPCE LHCRPANEYF AEKLRDAVVD GTPCYQVRAS
     RDLCINGICK NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV SGTFEEAEGL GYVDVGLIPA
     GAREIRIQEV AEAANFLALR SEDPEKYFLN GGWTIQWNGD YQVAGTTFTY ARRGNWENLT
     SPGPTKEPVW IQLLFQESNP GVHYEYTIHR EAGGHDEVPP PVFSWHYGPW TKCTVTCGRG
     VQRQNVYCLE RQAGPVDEEH CDPLGRPDDQ QRKCSEQPCP ARWWAGEWQL CSSSCGPGGL
     SRRAVLCIRS VGLDEQSALE PPACEHLPRP PTETPCNRHV PCPATWAVGN WSQCSVTCGE
     GTQRRNVLCT NDTGVPCDEA QQPASEVTCS LPLCRWPLGT LGPEGSGSGS SSHELFNEAD
     FIPHHLAPRP SPASSPKPGT MGNAIEEEAP ELDLPGPVFV DDFYYDYNFI NFHEDLSYGP
     SEEPDLDLAG TGDRTPPPHS HPAAPSTGSP VPATEPPAAK EEGVLGPWSP SPWPSQAGRS
     PPPPSEQTPG NPLINFLPEE DTPIGAPDLG LPSLSWPRVS TDGLQTPATP ESQNDFPVGK
     DSQSQLPPPW RDRTNEVFKD DEEPKGRGAP HLPPRPSSTL PPLSPVGSTH SSPSPDVAEL
     WTGGTVAWEP ALEGGLGPVD SELWPTVGVA SLLPPPIAPL PEMKVRDSSL EPGTPSFPTP
     GPGSWDLQTV AVWGTFLPTT LTGLGHMPEP ALNPGPKGQP ESLSPEVPLS SRLLSTPAWD
     SPANSHRVPE TQPLAPSLAE AGPPADPLVV RNAGWQAGNW SECSTTCGLG AVWRPVRCSS
     GRDEDCAPAG RPQPARRCHL RPCATWHSGN WSKCSRSCGG GSSVRDVQCV DTRDLRPLRP
     FHCQPGPAKP PAHRPCGAQP CLSWYTSSWR ECSEACGGGE QQRLVTCPEP GLCEEALRPN
     TTRPCNTHPC TQWVVGPWGQ CSGPCGGGVQ RRLVKCVNTQ TGLPEEDSDQ CGHEAWPESS
     RPCGTEDCEP VEPPRCERDR LSFGFCETLR LLGRCQLPTI RTQCCRSCSP PSHGAPSRGH
     QRVARR
//