ID   ATS17_HUMAN             Reviewed;        1095 AA.
AC   Q8TE56; Q2I7G4; Q6ZN75;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17;
DE            Short=ADAM-TS 17;
DE            Short=ADAM-TS17;
DE            Short=ADAMTS-17;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAMTS17;
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 1), AND VARIANT SER-1094.
RX   PubMed=11867212; DOI=10.1016/s0378-1119(01)00861-7;
RA   Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.;
RT   "Cloning, expression analysis, and structural characterization of seven
RT   novel human ADAMTSs, a family of metalloproteinases with disintegrin and
RT   thrombospondin-1 domains.";
RL   Gene 283:49-62(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-566.
RA   Tan J., Davila S., Hibberd M.L., Seielstad M.;
RT   "Genetic variation in ADAMTS17 gene.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   VARIANTS LEU-216; THR-482 AND SER-1094, INVOLVEMENT IN WMS4, ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=19836009; DOI=10.1016/j.ajhg.2009.09.011;
RA   Morales J., Al-Sharif L., Khalil D.S., Shinwari J.M., Bavi P.,
RA   Al-Mahrouqi R.A., Al-Rajhi A., Alkuraya F.S., Meyer B.F., Al Tassan N.;
RT   "Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia,
RT   ectopia lentis, glaucoma, spherophakia, and short stature.";
RL   Am. J. Hum. Genet. 85:558-568(2009).
RN   [6]
RP   INVOLVEMENT IN WMS4.
RX   PubMed=22486325; DOI=10.3109/13816810.2012.666708;
RA   Khan A.O., Aldahmesh M.A., Al-Ghadeer H., Mohamed J.Y., Alkuraya F.S.;
RT   "Familial spherophakia with short stature caused by a novel homozygous
RT   ADAMTS17 mutation.";
RL   Ophthalmic Genet. 33:235-239(2012).
RN   [7]
RP   INVOLVEMENT IN WMS4.
RX   PubMed=24940034;
RA   Shah M.H., Bhat V., Shetty J.S., Kumar A.;
RT   "Whole exome sequencing identifies a novel splice-site mutation in ADAMTS17
RT   in an Indian family with Weill-Marchesani syndrome.";
RL   Mol. Vis. 20:790-796(2014).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms may exist.;
CC       Name=1; Synonyms=a;
CC         IsoId=Q8TE56-1; Sequence=Displayed;
CC       Name=2; Synonyms=b;
CC         IsoId=Q8TE56-2; Sequence=VSP_040331, VSP_040332, VSP_040333;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at high
CC       levels in the lung, brain, whole eye and retina. Isoform 1 shows a
CC       weaker expression in the heart, kidney and skeletal muscle. Isoform 2
CC       shows a weaker expression in the kidney, bone marrow and skeletal
CC       muscle. Isoform 1 and isoform 2 are expressed at high levels in the
CC       fetal heart, kidney, and whole eye, whereas a weak expression is seen
CC       in the fetal liver. {ECO:0000269|PubMed:19836009}.
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. {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 4 (WMS4) [MIM:613195]: An autosomal
CC       recessive syndrome characterized by lenticular myopia, ectopia lentis,
CC       glaucoma, spherophakia and short stature. Brachydactyly and decreased
CC       joint flexibility are present in some patients.
CC       {ECO:0000269|PubMed:19836009, ECO:0000269|PubMed:22486325,
CC       ECO:0000269|PubMed:24940034}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; AJ315735; CAC86016.1; -; mRNA.
DR   EMBL; DQ217943; ABB70740.1; -; Genomic_DNA.
DR   EMBL; AK131344; BAD18500.1; -; mRNA.
DR   EMBL; AC015723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS10383.1; -. [Q8TE56-1]
DR   RefSeq; NP_620688.2; NM_139057.3. [Q8TE56-1]
DR   RefSeq; XP_016877473.1; XM_017021984.1. [Q8TE56-2]
DR   AlphaFoldDB; Q8TE56; -.
DR   SMR; Q8TE56; -.
DR   BioGRID; 128083; 32.
DR   IntAct; Q8TE56; 2.
DR   STRING; 9606.ENSP00000268070; -.
DR   MEROPS; M12.027; -.
DR   GlyCosmos; Q8TE56; 7 sites, No reported glycans.
DR   GlyGen; Q8TE56; 8 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TE56; -.
DR   PhosphoSitePlus; Q8TE56; -.
DR   BioMuta; ADAMTS17; -.
DR   DMDM; 296434401; -.
DR   jPOST; Q8TE56; -.
DR   MassIVE; Q8TE56; -.
DR   PaxDb; 9606-ENSP00000268070; -.
DR   PeptideAtlas; Q8TE56; -.
DR   ProteomicsDB; 74396; -. [Q8TE56-1]
DR   ProteomicsDB; 74397; -. [Q8TE56-2]
DR   Antibodypedia; 29223; 97 antibodies from 26 providers.
DR   DNASU; 170691; -.
DR   Ensembl; ENST00000268070.9; ENSP00000268070.4; ENSG00000140470.15. [Q8TE56-1]
DR   GeneID; 170691; -.
DR   KEGG; hsa:170691; -.
DR   MANE-Select; ENST00000268070.9; ENSP00000268070.4; NM_139057.4; NP_620688.2.
DR   UCSC; uc002bvv.2; human. [Q8TE56-1]
DR   AGR; HGNC:17109; -.
DR   CTD; 170691; -.
DR   DisGeNET; 170691; -.
DR   GeneCards; ADAMTS17; -.
DR   GeneReviews; ADAMTS17; -.
DR   HGNC; HGNC:17109; ADAMTS17.
DR   HPA; ENSG00000140470; Tissue enhanced (lymphoid).
DR   MalaCards; ADAMTS17; -.
DR   MIM; 607511; gene.
DR   MIM; 613195; phenotype.
DR   neXtProt; NX_Q8TE56; -.
DR   OpenTargets; ENSG00000140470; -.
DR   Orphanet; 363992; Ichthyosis-short stature-brachydactyly-microspherophakia syndrome.
DR   PharmGKB; PA24543; -.
DR   VEuPathDB; HostDB:ENSG00000140470; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158773; -.
DR   HOGENOM; CLU_000660_8_0_1; -.
DR   InParanoid; Q8TE56; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; Q8TE56; -.
DR   TreeFam; TF313537; -.
DR   PathwayCommons; Q8TE56; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q8TE56; -.
DR   BioGRID-ORCS; 170691; 15 hits in 1146 CRISPR screens.
DR   ChiTaRS; ADAMTS17; human.
DR   GenomeRNAi; 170691; -.
DR   Pharos; Q8TE56; Tbio.
DR   PRO; PR:Q8TE56; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8TE56; Protein.
DR   Bgee; ENSG00000140470; Expressed in thymus and 113 other cell types or tissues.
DR   ExpressionAtlas; Q8TE56; baseline and differential.
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: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; 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; 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   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 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; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00608; ACR; 1.
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; Q8TE56; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues; Deafness;
KW   Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..223
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029198"
FT   CHAIN           224..1095
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 17"
FT                   /id="PRO_0000029199"
FT   DOMAIN          232..452
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          453..542
FT                   /note="Disintegrin"
FT   DOMAIN          543..598
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          800..860
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          861..922
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          925..968
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          972..1029
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1045..1084
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          50..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..779
FT                   /note="Spacer"
FT   MOTIF           199..206
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         201
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         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        832
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        839
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        894
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        308..373
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..355
FT                   /evidence="ECO:0000250"
FT   DISULFID        367..447
FT                   /evidence="ECO:0000250"
FT   DISULFID        406..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        476..500
FT                   /evidence="ECO:0000250"
FT   DISULFID        487..508
FT                   /evidence="ECO:0000250"
FT   DISULFID        495..527
FT                   /evidence="ECO:0000250"
FT   DISULFID        521..532
FT                   /evidence="ECO:0000250"
FT   DISULFID        555..592
FT                   /evidence="ECO:0000250"
FT   DISULFID        559..597
FT                   /evidence="ECO:0000250"
FT   DISULFID        570..582
FT                   /evidence="ECO:0000250"
FT   DISULFID        873..916
FT                   /evidence="ECO:0000250"
FT   DISULFID        877..921
FT                   /evidence="ECO:0000250"
FT   DISULFID        888..905
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..243
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040331"
FT   VAR_SEQ         713..745
FT                   /note="ALKDSGKGSINSDWKIELPGEFQIAGTTVRYVR -> GYIEAAVIPAGARRI
FT                   RVVEDKPAHSFLGKTQMT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040332"
FT   VAR_SEQ         746..1095
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040333"
FT   VARIANT         216
FT                   /note="S -> L (in dbSNP:rs7496668)"
FT                   /evidence="ECO:0000269|PubMed:19836009"
FT                   /id="VAR_057081"
FT   VARIANT         482
FT                   /note="M -> T (in dbSNP:rs28567966)"
FT                   /evidence="ECO:0000269|PubMed:19836009"
FT                   /id="VAR_057082"
FT   VARIANT         566
FT                   /note="R -> T"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_064041"
FT   VARIANT         1094
FT                   /note="N -> S (in dbSNP:rs2573652)"
FT                   /evidence="ECO:0000269|PubMed:11867212,
FT                   ECO:0000269|PubMed:19836009"
FT                   /id="VAR_060317"
FT   CONFLICT        702
FT                   /note="V -> A (in Ref. 3; BAD18500)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1095 AA;  121127 MW;  A5D7A40484754D5D CRC64;
     MCDGALLPPL VLPVLLLLVW GLDPGTAVGD AAADVEVVLP WRVRPDDVHL PPLPAAPGPR
     RRRRPRTPPA APRARPGERA LLLHLPAFGR DLYLQLRRDL RFLSRGFEVE EAGAARRRGR
     PAELCFYSGR VLGHPGSLVS LSACGAAGGL VGLIQLGQEQ VLIQPLNNSQ GPFSGREHLI
     RRKWSLTPSP SAEAQRPEQL CKVLTEKKKP TWGRPSRDWR ERRNAIRLTS EHTVETLVVA
     DADMVQYHGA EAAQRFILTV MNMVYNMFQH QSLGIKINIQ VTKLVLLRQR PAKLSIGHHG
     ERSLESFCHW QNEEYGGARY LGNNQVPGGK DDPPLVDAAV FVTRTDFCVH KDEPCDTVGI
     AYLGGVCSAK RKCVLAEDNG LNLAFTIAHE LGHNLGMNHD DDHSSCAGRS HIMSGEWVKG
     RNPSDLSWSS CSRDDLENFL KSKVSTCLLV TDPRSQHTVR LPHKLPGMHY SANEQCQILF
     GMNATFCRNM EHLMCAGLWC LVEGDTSCKT KLDPPLDGTE CGADKWCRAG ECVSKTPIPE
     HVDGDWSPWG AWSMCSRTCG TGARFRQRKC DNPPPGPGGT HCPGASVEHA VCENLPCPKG
     LPSFRDQQCQ AHDRLSPKKK GLLTAVVVDD KPCELYCSPL GKESPLLVAD RVLDGTPCGP
     YETDLCVHGK CQKIGCDGII GSAAKEDRCG VCSGDGKTCH LVKGDFSHAR GTALKDSGKG
     SINSDWKIEL PGEFQIAGTT VRYVRRGLWE KISAKGPTKL PLHLMVLLFH DQDYGIHYEY
     TVPVNRTAEN QSEPEKPQDS LFIWTHSGWE GCSVQCGGGE RRTIVSCTRI VNKTTTLVND
     SDCPQASRPE PQVRRCNLHP CQSRWVAGPW SPCSATCEKG FQHREVTCVY QLQNGTHVAT
     RPLYCPGPRP AAVQSCEGQD CLSIWEASEW SQCSASCGKG VWKRTVACTN SQGKCDASTR
     PRAEEACEDY SGCYEWKTGD WSTCSSTCGK GLQSRVVQCM HKVTGRHGSE CPALSKPAPY
     RQCYQEVCND RINANTITSP RLAALTYKCT RDQWTVYCRV IREKNLCQDM RWYQRCCQTC
     RDFYANKMRQ PPPNS
//