ATS18_HUMAN
ID ATS18_HUMAN Reviewed; 1221 AA.
AC Q8TE60; Q6P4R5; Q6ZWJ9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18;
DE Short=ADAM-TS 18;
DE Short=ADAM-TS18;
DE Short=ADAMTS-18;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS18; Synonyms=ADAMTS21;
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 2), AND VARIANTS ILE-626 AND SER-946.
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-191;
RP ILE-626 AND ILE-769.
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 761-1221 (ISOFORM 1), AND VARIANT
RP ARG-1080.
RC TISSUE=Cerebellum;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-382 AND THR-455.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [7]
RP VARIANT LEU-179.
RX PubMed=21862674; DOI=10.1136/jmedgenet-2011-100306;
RA Aldahmesh M.A., Khan A.O., Mohamed J.Y., Alkuraya H., Ahmed H., Bobis S.,
RA Al-Mesfer S., Alkuraya F.S.;
RT "Identification of ADAMTS18 as a gene mutated in Knobloch syndrome.";
RL J. Med. Genet. 48:597-601(2011).
RN [8]
RP VARIANTS MMCAT PRO-202 AND TRP-577.
RX PubMed=23818446; DOI=10.1002/humu.22374;
RA Aldahmesh M.A., Alshammari M.J., Khan A.O., Mohamed J.Y., Alhabib F.A.,
RA Alkuraya F.S.;
RT "The syndrome of microcornea, myopic chorioretinal atrophy, and telecanthus
RT (MMCAT) is caused by mutations in ADAMTS18.";
RL Hum. Mutat. 34:1195-1199(2013).
RN [9]
RP VARIANT LEU-179, AND LACK OF INVOLVEMENT IN KNOBLOCH SYNDROME.
RX PubMed=23667181; DOI=10.1136/jmedgenet-2013-101755;
RA Aldahmesh M.A., Khan A.O., Mohamed J.Y., Levin A.V., Wuthisiri W.,
RA Lynch S., McCreery K., Alkuraya F.S.;
RT "No evidence for locus heterogeneity in Knobloch syndrome.";
RL J. Med. Genet. 50:565-566(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {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=1;
CC IsoId=Q8TE60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE60-2; Sequence=VSP_015776, VSP_015777;
CC -!- TISSUE SPECIFICITY: Expressed in fetal lung, liver, and kidney and in
CC adult brain, prostate, submaxillary gland, and endothelium.
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: Microcornea, myopic chorioretinal atrophy, and telecanthus
CC (MMCAT) [MIM:615458]: A ocular syndrome characterized by microcornea
CC and myopic chorioretinal atrophy. Microcornea is defined by a corneal
CC diameter inferior to 10 mm in both meridians in an otherwise normal
CC eye. In addition to ocular findings, some patients have telecanthus and
CC posteriorly rotated ears. {ECO:0000269|PubMed:23818446}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: Variant Leu-179 has been originally reported as disease-
CC causing mutation in a patient with Knobloch syndrome (PubMed:21862674).
CC It has been subsequently shown that Knobloch syndrome in the patient
CC was due to an intronic mutation in COL18A1. Variant Leu-179 is,
CC therefore, not responsible for the disease phenotype (PubMed:23667181).
CC {ECO:0000305|PubMed:21862674, ECO:0000305|PubMed:23667181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC85503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC83612.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
CC Sequence=CAC83612.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AJ311903; CAC83612.1; ALT_SEQ; mRNA.
DR EMBL; AC009139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063283; AAH63283.1; -; mRNA.
DR EMBL; AK122677; BAC85503.1; ALT_INIT; mRNA.
DR CCDS; CCDS10926.1; -. [Q8TE60-1]
DR RefSeq; NP_955387.1; NM_199355.3. [Q8TE60-1]
DR AlphaFoldDB; Q8TE60; -.
DR SMR; Q8TE60; -.
DR BioGRID; 128084; 8.
DR IntAct; Q8TE60; 4.
DR STRING; 9606.ENSP00000282849; -.
DR MEROPS; M12.028; -.
DR GlyGen; Q8TE60; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TE60; -.
DR PhosphoSitePlus; Q8TE60; -.
DR BioMuta; ADAMTS18; -.
DR DMDM; 296439427; -.
DR MassIVE; Q8TE60; -.
DR PaxDb; Q8TE60; -.
DR PeptideAtlas; Q8TE60; -.
DR PRIDE; Q8TE60; -.
DR ProteomicsDB; 74402; -. [Q8TE60-1]
DR ProteomicsDB; 74403; -. [Q8TE60-2]
DR Antibodypedia; 30389; 157 antibodies from 24 providers.
DR DNASU; 170692; -.
DR Ensembl; ENST00000282849.10; ENSP00000282849.5; ENSG00000140873.16. [Q8TE60-1]
DR GeneID; 170692; -.
DR KEGG; hsa:170692; -.
DR MANE-Select; ENST00000282849.10; ENSP00000282849.5; NM_199355.4; NP_955387.1.
DR UCSC; uc002ffc.4; human. [Q8TE60-1]
DR CTD; 170692; -.
DR DisGeNET; 170692; -.
DR GeneCards; ADAMTS18; -.
DR HGNC; HGNC:17110; ADAMTS18.
DR HPA; ENSG00000140873; Group enriched (brain, placenta).
DR MalaCards; ADAMTS18; -.
DR MIM; 607512; gene.
DR MIM; 615458; phenotype.
DR neXtProt; NX_Q8TE60; -.
DR OpenTargets; ENSG00000140873; -.
DR Orphanet; 369970; Microcornea-myopic chorioretinal atrophy-telecanthus syndrome.
DR PharmGKB; PA24544; -.
DR VEuPathDB; HostDB:ENSG00000140873; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000157553; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; Q8TE60; -.
DR OMA; REKRSPI; -.
DR PhylomeDB; Q8TE60; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; Q8TE60; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q8TE60; -.
DR BioGRID-ORCS; 170692; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; ADAMTS18; human.
DR GenomeRNAi; 170692; -.
DR Pharos; Q8TE60; Tbio.
DR PRO; PR:Q8TE60; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8TE60; protein.
DR Bgee; ENSG00000140873; Expressed in cerebellar vermis and 117 other tissues.
DR ExpressionAtlas; Q8TE60; baseline and differential.
DR Genevisible; Q8TE60; HS.
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:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 6.
DR Gene3D; 3.40.390.10; -; 1.
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 Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT PROPEP 48..284
FT /evidence="ECO:0000250"
FT /id="PRO_0000029200"
FT CHAIN 285..1221
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 18"
FT /id="PRO_0000042163"
FT DOMAIN 293..498
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 498..577
FT /note="Disintegrin"
FT DOMAIN 589..644
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 931..990
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 991..1049
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1052..1116
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1123..1178
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1184..1221
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 258..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..876
FT /note="Spacer"
FT MOTIF 252..259
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 254
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 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..420
FT /evidence="ECO:0000250"
FT DISULFID 395..402
FT /evidence="ECO:0000250"
FT DISULFID 414..493
FT /evidence="ECO:0000250"
FT DISULFID 453..477
FT /evidence="ECO:0000250"
FT DISULFID 521..546
FT /evidence="ECO:0000250"
FT DISULFID 532..553
FT /evidence="ECO:0000250"
FT DISULFID 541..572
FT /evidence="ECO:0000250"
FT DISULFID 566..577
FT /evidence="ECO:0000250"
FT DISULFID 601..638
FT /evidence="ECO:0000250"
FT DISULFID 605..643
FT /evidence="ECO:0000250"
FT DISULFID 616..628
FT /evidence="ECO:0000250"
FT VAR_SEQ 1064..1082
FT /note="CSATCGLGVRKREMKCSEK -> VWIRSHCWVRRLRPSWLTQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_015776"
FT VAR_SEQ 1083..1221
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_015777"
FT VARIANT 179
FT /note="S -> L (in dbSNP:rs387906972)"
FT /evidence="ECO:0000269|PubMed:21862674,
FT ECO:0000269|PubMed:23667181"
FT /id="VAR_066554"
FT VARIANT 191
FT /note="Y -> H (in dbSNP:rs11643211)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060231"
FT VARIANT 202
FT /note="L -> P (in MMCAT; dbSNP:rs397515468)"
FT /evidence="ECO:0000269|PubMed:23818446"
FT /id="VAR_070849"
FT VARIANT 382
FT /note="R -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs368783738)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036152"
FT VARIANT 455
FT /note="K -> T (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs776584074)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036153"
FT VARIANT 577
FT /note="C -> W (in MMCAT; dbSNP:rs148319220)"
FT /evidence="ECO:0000269|PubMed:23818446"
FT /id="VAR_070850"
FT VARIANT 626
FT /note="L -> I (in dbSNP:rs11640912)"
FT /evidence="ECO:0000269|PubMed:11867212,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060232"
FT VARIANT 769
FT /note="L -> I (in dbSNP:rs9930984)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057083"
FT VARIANT 946
FT /note="A -> S (in dbSNP:rs12935394)"
FT /evidence="ECO:0000269|PubMed:11867212"
FT /id="VAR_057084"
FT VARIANT 1080
FT /note="S -> R (in dbSNP:rs35478105)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057085"
FT VARIANT 1159
FT /note="S -> T (in dbSNP:rs3743749)"
FT /id="VAR_057086"
FT CONFLICT 410
FT /note="I -> T (in Ref. 1; CAC83612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1221 AA; 135167 MW; 4F662B2D2ABF5CA3 CRC64;
MECALLLACA FPAAGSGPPR GLAGLGRVAK ALQLCCLCCA SVAAALASDS SSGASGLNDD
YVFVTPVEVD SAGSYISHDI LHNGRKKRSA QNARSSLHYR FSAFGQELHL ELKPSAILSS
HFIVQVLGKD GASETQKPEV QQCFYQGFIR NDSSSSVAVS TCAGLSGLIR TRKNEFLISP
LPQLLAQEHN YSSPAGHHPH VLYKRTAEEK IQRYRGYPGS GRNYPGYSPS HIPHASQSRE
TEYHHRRLQK QHFCGRRKKY APKPPTEDTY LRFDEYGSSG RPRRSAGKSQ KGLNVETLVV
ADKKMVEKHG KGNVTTYILT VMNMVSGLFK DGTIGSDINV VVVSLILLEQ EPGGLLINHH
ADQSLNSFCQ WQSALIGKNG KRHDHAILLT GFDICSWKNE PCDTLGFAPI SGMCSKYRSC
TINEDTGLGL AFTIAHESGH NFGMIHDGEG NPCRKAEGNI MSPTLTGNNG VFSWSSCSRQ
YLKKFLSTPQ AGCLVDEPKQ AGQYKYPDKL PGQIYDADTQ CKWQFGAKAK LCSLGFVKDI
CKSLWCHRVG HRCETKFMPA AEGTVCGLSM WCRQGQCVKF GELGPRPIHG QWSAWSKWSE
CSRTCGGGVK FQERHCNNPK PQYGGLFCPG SSRIYQLCNI NPCNENSLDF RAQQCAEYNS
KPFRGWFYQW KPYTKVEEED RCKLYCKAEN FEFFFAMSGK VKDGTPCSPN KNDVCIDGVC
ELVGCDHELG SKAVSDACGV CKGDNSTCKF YKGLYLNQHK ANEYYPVVLI PAGARSIEIQ
ELQVSSSYLA VRSLSQKYYL TGGWSIDWPG EFPFAGTTFE YQRSFNRPER LYAPGPTNET
LVFEILMQGK NPGIAWKYAL PKVMNGTPPA TKRPAYTWSI VQSECSVSCG GGYINVKAIC
LRDQNTQVNS SFCSAKTKPV TEPKICNAFS CPAYWMPGEW STCSKACAGG QQSRKIQCVQ
KKPFQKEEAV LHSLCPVSTP TQVQACNSHA CPPQWSLGPW SQCSKTCGRG VRKRELLCKG
SAAETLPESQ CTSLPRPELQ EGCVLGRCPK NSRLQWVASS WSECSATCGL GVRKREMKCS
EKGFQGKLIT FPERRCRNIK KPNLDLEETC NRRACPAHPV YNMVAGWYSL PWQQCTVTCG
GGVQTRSVHC VQQGRPSSSC LLHQKPPVLR ACNTNFCPAP EKREDPSCVD FFNWCHLVPQ
HGVCNHKFYG KQCCKSCTRK I
