ATL1_HUMAN
ID ATL1_HUMAN Reviewed; 1762 AA.
AC Q8N6G6; A6PVN1; A8K7E1; Q496M6; Q496M8; Q5T708; Q5VZT8; Q8NAI9; Q96RW4;
AC Q9BXY3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=ADAMTS-like protein 1;
DE Short=ADAMTSL-1;
DE AltName: Full=Punctin-1;
DE Flags: Precursor;
GN Name=ADAMTSL1; Synonyms=ADAMTSR1, C9orf94; ORFNames=UNQ528/PRO1071;
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), PARTIAL PROTEIN SEQUENCE, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, MASS SPECTROMETRY,
RP AND DISULFIDE BONDS.
RX PubMed=11805097; DOI=10.1074/jbc.m109665200;
RA Hirohata S., Wang L.W., Miyagi M., Yan L., Seldin M.F., Keene D.R.,
RA Crabb J.W., Apte S.S.;
RT "Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular
RT matrix.";
RL J. Biol. Chem. 277:12182-12189(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Prostate;
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 214-1762 (ISOFORM 4).
RA Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA Tang R., Chen X., Wu C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GLYCOSYLATION AT ASN-251; THR-312; SER-391 AND THR-451, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17395588; DOI=10.1074/jbc.m701065200;
RA Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S.,
RA Apte S.S.;
RT "O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1
RT regulates secretion: implications for the ADAMTS superfamily.";
RL J. Biol. Chem. 282:17024-17031(2007).
RN [9]
RP GLYCOSYLATION AT TRP-39; TRP-42 AND THR-48, LACK OF GLYCOSYLATION AT
RP TRP-36, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-36; TRP-39; TRP-42;
RP TRP-385 AND TRP-445, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19671700; DOI=10.1074/jbc.m109.038059;
RA Wang L.W., Leonhard-Melief C., Haltiwanger R.S., Apte S.S.;
RT "Post-translational modification of thrombospondin type-1 repeats in
RT ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.";
RL J. Biol. Chem. 284:30004-30015(2009).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11805097}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:11805097, ECO:0000269|PubMed:17395588,
CC ECO:0000269|PubMed:19671700}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3;
CC IsoId=Q8N6G6-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8N6G6-1; Sequence=VSP_039326;
CC Name=2;
CC IsoId=Q8N6G6-2; Sequence=VSP_039323, VSP_039324, VSP_039325;
CC Name=4;
CC IsoId=Q8N6G6-4; Sequence=VSP_039327, VSP_039328;
CC Name=5;
CC IsoId=Q8N6G6-5; Sequence=VSP_039322, VSP_039329, VSP_039330,
CC VSP_039331;
CC Name=6;
CC IsoId=Q8N6G6-6; Sequence=VSP_039322, VSP_039329;
CC -!- TISSUE SPECIFICITY: Expressed primarily in adult skeletal muscle.
CC {ECO:0000269|PubMed:11805097}.
CC -!- PTM: C-, N- and O-glycosylated. O-fucosylated by POFUT2 on a serine or
CC a threonine residue found within the consensus sequence C1-X(2)-(S/T)-
CC C2-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 ADAMTSL1. Can also be C-
CC 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.
CC {ECO:0000269|PubMed:11805097, ECO:0000269|PubMed:17395588,
CC ECO:0000269|PubMed:19671700}.
CC -!- PTM: Disulfide bonds are present.
CC -!- MASS SPECTROMETRY: [Isoform 1]: Mass=61935; Mass_error=595;
CC Method=MALDI; Note=The measured range is 28-525.;
CC Evidence={ECO:0000269|PubMed:11805097};
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- CAUTION: Although strongly similar to members of the ADAMTS family it
CC lacks the metalloprotease and disintegrin-like domains which are
CC typical of that family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00789.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI00791.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK34948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF176313; AAK84170.1; -; mRNA.
DR EMBL; AY358327; AAQ88693.1; -; mRNA.
DR EMBL; AK092602; BAC03925.1; -; mRNA.
DR EMBL; AK291956; BAF84645.1; -; mRNA.
DR EMBL; AL158150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58656.1; -; Genomic_DNA.
DR EMBL; BC030262; AAH30262.1; -; mRNA.
DR EMBL; BC100788; AAI00789.1; ALT_FRAME; mRNA.
DR EMBL; BC100790; AAI00791.1; ALT_FRAME; mRNA.
DR EMBL; AF251058; AAK34948.1; ALT_INIT; mRNA.
DR CCDS; CCDS47954.1; -. [Q8N6G6-3]
DR CCDS; CCDS6485.1; -. [Q8N6G6-1]
DR RefSeq; NP_001035362.3; NM_001040272.5. [Q8N6G6-3]
DR RefSeq; NP_443098.3; NM_052866.4. [Q8N6G6-1]
DR AlphaFoldDB; Q8N6G6; -.
DR BioGRID; 124989; 34.
DR IntAct; Q8N6G6; 7.
DR STRING; 9606.ENSP00000369921; -.
DR GlyGen; Q8N6G6; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N6G6; -.
DR PhosphoSitePlus; Q8N6G6; -.
DR BioMuta; ADAMTSL1; -.
DR DMDM; 298286924; -.
DR jPOST; Q8N6G6; -.
DR MassIVE; Q8N6G6; -.
DR PaxDb; Q8N6G6; -.
DR PeptideAtlas; Q8N6G6; -.
DR PRIDE; Q8N6G6; -.
DR ProteomicsDB; 72170; -. [Q8N6G6-3]
DR ProteomicsDB; 72171; -. [Q8N6G6-1]
DR ProteomicsDB; 72172; -. [Q8N6G6-2]
DR ProteomicsDB; 72173; -. [Q8N6G6-4]
DR ProteomicsDB; 72174; -. [Q8N6G6-5]
DR ProteomicsDB; 72175; -. [Q8N6G6-6]
DR Antibodypedia; 24655; 167 antibodies from 24 providers.
DR DNASU; 92949; -.
DR Ensembl; ENST00000276935.6; ENSP00000276935.5; ENSG00000178031.18. [Q8N6G6-4]
DR Ensembl; ENST00000327883.11; ENSP00000327887.7; ENSG00000178031.18. [Q8N6G6-1]
DR Ensembl; ENST00000380545.9; ENSP00000369918.5; ENSG00000178031.18. [Q8N6G6-6]
DR Ensembl; ENST00000380548.9; ENSP00000369921.4; ENSG00000178031.18. [Q8N6G6-3]
DR Ensembl; ENST00000380566.8; ENSP00000369940.4; ENSG00000178031.18. [Q8N6G6-2]
DR Ensembl; ENST00000542621.5; ENSP00000440472.1; ENSG00000178031.18. [Q8N6G6-5]
DR GeneID; 92949; -.
DR KEGG; hsa:92949; -.
DR MANE-Select; ENST00000380548.9; ENSP00000369921.4; NM_001040272.6; NP_001035362.3.
DR UCSC; uc003znb.4; human. [Q8N6G6-3]
DR CTD; 92949; -.
DR DisGeNET; 92949; -.
DR GeneCards; ADAMTSL1; -.
DR HGNC; HGNC:14632; ADAMTSL1.
DR HPA; ENSG00000178031; Tissue enhanced (endometrium).
DR MalaCards; ADAMTSL1; -.
DR MIM; 609198; gene.
DR neXtProt; NX_Q8N6G6; -.
DR OpenTargets; ENSG00000178031; -.
DR Orphanet; 521445; Microcephaly-facial dysmorphism-ocular anomalies-multiple congenital anomalies syndrome.
DR PharmGKB; PA24554; -.
DR VEuPathDB; HostDB:ENSG00000178031; -.
DR eggNOG; KOG3538; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156243; -.
DR HOGENOM; CLU_001717_1_0_1; -.
DR InParanoid; Q8N6G6; -.
DR OMA; WLLSEWT; -.
DR OrthoDB; 38261at2759; -.
DR PhylomeDB; Q8N6G6; -.
DR TreeFam; TF351125; -.
DR PathwayCommons; Q8N6G6; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q8N6G6; -.
DR BioGRID-ORCS; 92949; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; ADAMTSL1; human.
DR GeneWiki; ADAMTSL1; -.
DR GenomeRNAi; 92949; -.
DR Pharos; Q8N6G6; Tbio.
DR PRO; PR:Q8N6G6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N6G6; protein.
DR Bgee; ENSG00000178031; Expressed in lower esophagus muscularis layer and 123 other tissues.
DR ExpressionAtlas; Q8N6G6; baseline and differential.
DR Genevisible; Q8N6G6; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR Gene3D; 2.20.100.10; -; 11.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00209; TSP1; 13.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF82895; SSF82895; 11.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT CHAIN 29..1762
FT /note="ADAMTS-like protein 1"
FT /id="PRO_0000035860"
FT DOMAIN 33..82
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 376..424
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 436..493
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 522..584
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 607..665
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 666..729
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 788..850
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 861..963
FT /note="Ig-like C2-type 1"
FT DOMAIN 1164..1266
FT /note="Ig-like C2-type 2"
FT DOMAIN 1286..1369
FT /note="Ig-like C2-type 3"
FT DOMAIN 1395..1485
FT /note="Ig-like C2-type 4"
FT DOMAIN 1545..1608
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1666..1726
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1726..1762
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 1120..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 36
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 39
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 42
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 48
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17395588"
FT CARBOHYD 312
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:17395588"
FT CARBOHYD 391
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395588"
FT CARBOHYD 451
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:17395588"
FT DISULFID 45..76
FT /evidence="ECO:0000250"
FT DISULFID 49..81
FT /evidence="ECO:0000250"
FT DISULFID 60..66
FT /evidence="ECO:0000250"
FT DISULFID 534..578
FT /evidence="ECO:0000250"
FT DISULFID 538..583
FT /evidence="ECO:0000250"
FT DISULFID 549..567
FT /evidence="ECO:0000250"
FT DISULFID 678..723
FT /evidence="ECO:0000250"
FT DISULFID 682..728
FT /evidence="ECO:0000250"
FT DISULFID 693..712
FT /evidence="ECO:0000250"
FT DISULFID 800..844
FT /evidence="ECO:0000250"
FT DISULFID 804..849
FT /evidence="ECO:0000250"
FT DISULFID 815..832
FT /evidence="ECO:0000250"
FT DISULFID 899..947
FT /evidence="ECO:0000250"
FT DISULFID 1202..1250
FT /evidence="ECO:0000250"
FT DISULFID 1308..1353
FT /evidence="ECO:0000250"
FT DISULFID 1418..1469
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1299
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039322"
FT VAR_SEQ 362..378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039323"
FT VAR_SEQ 448..456
FT /note="CTVTCGQGL -> VTVPSFFVH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039324"
FT VAR_SEQ 457..1762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039325"
FT VAR_SEQ 526..1762
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11805097,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:14702039"
FT /id="VSP_039326"
FT VAR_SEQ 670..683
FT /note="WEIGKWSPCSLTCG -> SSIDSAWNACNVLC (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_039327"
FT VAR_SEQ 684..1762
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_039328"
FT VAR_SEQ 1300..1311
FT /note="QGVNVTINCQVA -> MSGVFCFFFFFL (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039329"
FT VAR_SEQ 1549..1557
FT /note="WMVTSWSAC -> AMGLASGLT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_039330"
FT VAR_SEQ 1558..1762
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_039331"
FT VARIANT 242
FT /note="S -> N (in dbSNP:rs776755)"
FT /id="VAR_017174"
FT MUTAGEN 36
FT /note="W->A: Small reduction in secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 39
FT /note="W->A: Significant reduction in secretion of
FT ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 39
FT /note="W->F: Abolishes secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 42
FT /note="W->A: Modest reduction in secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 42
FT /note="W->F: Abolishes secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 251
FT /note="N->Q: Abolishes N-glycosylation. Reduces secretion
FT of ADAMTSL1."
FT MUTAGEN 312
FT /note="T->A: Small increase in secretion of ADAMTSL1. About
FT 40% increase in secretion of ADAMTSL1; when associated with
FT A-391. Dramatic increase in secretion of ADAMTSL1; when
FT associated with A-391 and A-451."
FT MUTAGEN 385
FT /note="W->A: Significant reduction in secretion of
FT ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 385
FT /note="W->F: No effect on secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 391
FT /note="S->A: Small increase in secretion of ADAMTSL1. About
FT 40% increase in secretion of ADAMTSL1; when associated with
FT A-312. Dramatic increase in secretion of ADAMTSL1; when
FT associated with A-312 and A-451."
FT MUTAGEN 445
FT /note="W->A: Modest reduction in secretion of ADAMTSL1."
FT /evidence="ECO:0000269|PubMed:19671700"
FT MUTAGEN 451
FT /note="T->A: Small increase in secretion of ADAMTSL1.
FT Dramatic increase in secretion of ADAMTSL1; when associated
FT with A-312 and A-391."
FT CONFLICT 54..55
FT /note="SY -> AN (in Ref. 1; AAK84170)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="I -> L (in Ref. 2; AAQ88693)"
FT /evidence="ECO:0000305"
FT CONFLICT 1409
FT /note="D -> G (in Ref. 3; BAC03925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1762 AA; 193409 MW; 2822C0A367C2EF4E CRC64;
MECCRRATPG TLLLFLAFLL LSSRTARSEE DRDGLWDAWG PWSECSRTCG GGASYSLRRC
LSSKSCEGRN IRYRTCSNVD CPPEAGDFRA QQCSAHNDVK HHGQFYEWLP VSNDPDNPCS
LKCQAKGTTL VVELAPKVLD GTRCYTESLD MCISGLCQIV GCDHQLGSTV KEDNCGVCNG
DGSTCRLVRG QYKSQLSATK SDDTVVAIPY GSRHIRLVLK GPDHLYLETK TLQGTKGENS
LSSTGTFLVD NSSVDFQKFP DKEILRMAGP LTADFIVKIR NSGSADSTVQ FIFYQPIIHR
WRETDFFPCS ATCGGGYQLT SAECYDLRSN RVVADQYCHY YPENIKPKPK LQECNLDPCP
ASDGYKQIMP YDLYHPLPRW EATPWTACSS SCGGGIQSRA VSCVEEDIQG HVTSVEEWKC
MYTPKMPIAQ PCNIFDCPKW LAQEWSPCTV TCGQGLRYRV VLCIDHRGMH TGGCSPKTKP
HIKEECIVPT PCYKPKEKLP VEAKLPWFKQ AQELEEGAAV SEEPSFIPEA WSACTVTCGV
GTQVRIVRCQ VLLSFSQSVA DLPIDECEGP KPASQRACYA GPCSGEIPEF NPDETDGLFG
GLQDFDELYD WEYEGFTKCS ESCGGGVQEA VVSCLNKQTR EPAEENLCVT SRRPPQLLKS
CNLDPCPARW EIGKWSPCSL TCGVGLQTRD VFCSHLLSRE MNETVILADE LCRQPKPSTV
QACNRFNCPP AWYPAQWQPC SRTCGGGVQK REVLCKQRMA DGSFLELPET FCSASKPACQ
QACKKDDCPS EWLLSDWTEC STSCGEGTQT RSAICRKMLK TGLSTVVNST LCPPLPFSSS
IRPCMLATCA RPGRPSTKHS PHIAAARKVY IQTRRQRKLH FVVGGFAYLL PKTAVVLRCP
ARRVRKPLIT WEKDGQHLIS STHVTVAPFG YLKIHRLKPS DAGVYTCSAG PAREHFVIKL
IGGNRKLVAR PLSPRSEEEV LAGRKGGPKE ALQTHKHQNG IFSNGSKAEK RGLAANPGSR
YDDLVSRLLE QGGWPGELLA SWEAQDSAER NTTSEEDPGA EQVLLHLPFT MVTEQRRLDD
ILGNLSQQPE ELRDLYSKHL VAQLAQEIFR SHLEHQDTLL KPSERRTSPV TLSPHKHVSG
FSSSLRTSST GDAGGGSRRP HRKPTILRKI SAAQQLSASE VVTHLGQTVA LASGTLSVLL
HCEAIGHPRP TISWARNGEE VQFSDRILLQ PDDSLQILAP VEADVGFYTC NATNALGYDS
VSIAVTLAGK PLVKTSRMTV INTEKPAVTV DIGSTIKTVQ GVNVTINCQV AGVPEAEVTW
FRNKSKLGSP HHLHEGSLLL TNVSSSDQGL YSCRAANLHG ELTESTQLLI LDPPQVPTQL
EDIRALLAAT GPNLPSVLTS PLGTQLVLDP GNSALLGCPI KGHPVPNITW FHGGQPIVTA
TGLTHHILAA GQILQVANLS GGSQGEFSCL AQNEAGVLMQ KASLVIQDYW WSVDRLATCS
ASCGNRGVQQ PRLRCLLNST EVNPAHCAGK VRPAVQPIAC NRRDCPSRWM VTSWSACTRS
CGGGVQTRRV TCQKLKASGI STPVSNDMCT QVAKRPVDTQ ACNQQLCVEW AFSSWGQCNG
PCIGPHLAVQ HRQVFCQTRD GITLPSEQCS ALPRPVSTQN CWSEACSVHW RVSLWTLCTA
TCGNYGFQSR RVECVHARTN KAVPEHLCSW GPRPANWQRC NITPCENMEC RDTTRYCEKV
KQLKLCQLSQ FKSRCCGTCG KA
