ATS16_HUMAN
ID ATS16_HUMAN Reviewed; 1224 AA.
AC Q8TE57; C6G490; Q8IVE2;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 16;
DE Short=ADAM-TS 16;
DE Short=ADAM-TS16;
DE Short=ADAMTS-16;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS16; Synonyms=KIAA2029;
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).
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].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-1224 (ISOFORM 1).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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=Q8TE57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE57-2; Sequence=VSP_007664, VSP_007665;
CC -!- TISSUE SPECIFICITY: Expressed in fetal lung and kidney and in adult
CC prostate and ovary.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix. {ECO:0000250}.
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}.
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DR EMBL; AJ315734; CAC86015.1; -; mRNA.
DR EMBL; FJ515844; ACS13738.1; -; Genomic_DNA.
DR EMBL; AC010269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB095949; BAC23125.1; -; mRNA.
DR CCDS; CCDS43299.1; -. [Q8TE57-1]
DR RefSeq; NP_620687.2; NM_139056.3. [Q8TE57-1]
DR AlphaFoldDB; Q8TE57; -.
DR SMR; Q8TE57; -.
DR BioGRID; 128082; 2.
DR IntAct; Q8TE57; 2.
DR STRING; 9606.ENSP00000274181; -.
DR MEROPS; M12.026; -.
DR GlyGen; Q8TE57; 7 sites.
DR iPTMnet; Q8TE57; -.
DR PhosphoSitePlus; Q8TE57; -.
DR BioMuta; ADAMTS16; -.
DR DMDM; 296439429; -.
DR jPOST; Q8TE57; -.
DR MassIVE; Q8TE57; -.
DR PaxDb; Q8TE57; -.
DR PeptideAtlas; Q8TE57; -.
DR PRIDE; Q8TE57; -.
DR ProteomicsDB; 74398; -. [Q8TE57-1]
DR ProteomicsDB; 74399; -. [Q8TE57-2]
DR Antibodypedia; 59056; 46 antibodies from 14 providers.
DR DNASU; 170690; -.
DR Ensembl; ENST00000274181.7; ENSP00000274181.7; ENSG00000145536.15. [Q8TE57-1]
DR GeneID; 170690; -.
DR KEGG; hsa:170690; -.
DR MANE-Select; ENST00000274181.7; ENSP00000274181.7; NM_139056.4; NP_620687.2.
DR UCSC; uc003jdl.4; human. [Q8TE57-1]
DR CTD; 170690; -.
DR DisGeNET; 170690; -.
DR GeneCards; ADAMTS16; -.
DR HGNC; HGNC:17108; ADAMTS16.
DR HPA; ENSG00000145536; Tissue enhanced (brain, ovary).
DR MIM; 607510; gene.
DR neXtProt; NX_Q8TE57; -.
DR OpenTargets; ENSG00000145536; -.
DR PharmGKB; PA24542; -.
DR VEuPathDB; HostDB:ENSG00000145536; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159433; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; Q8TE57; -.
DR OMA; LRCAEKY; -.
DR PhylomeDB; Q8TE57; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; Q8TE57; -.
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; Q8TE57; -.
DR BioGRID-ORCS; 170690; 5 hits in 1068 CRISPR screens.
DR GenomeRNAi; 170690; -.
DR Pharos; Q8TE57; Tbio.
DR PRO; PR:Q8TE57; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TE57; protein.
DR Bgee; ENSG00000145536; Expressed in buccal mucosa cell and 106 other tissues.
DR ExpressionAtlas; Q8TE57; baseline and differential.
DR Genevisible; Q8TE57; 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:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048232; P:male gamete generation; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1902017; P:regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
DR Gene3D; 2.20.100.10; -; 5.
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 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..279
FT /evidence="ECO:0000250"
FT /id="PRO_0000029194"
FT CHAIN 280..1224
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 16"
FT /id="PRO_0000029195"
FT DOMAIN 290..495
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 496..585
FT /note="Disintegrin"
FT DOMAIN 586..641
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 874..922
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 927..987
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 988..1048
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1051..1115
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1127..1181
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1186..1223
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..873
FT /note="Spacer"
FT MOTIF 247..254
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 38..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 249
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 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 366..417
FT /evidence="ECO:0000250"
FT DISULFID 392..399
FT /evidence="ECO:0000250"
FT DISULFID 411..490
FT /evidence="ECO:0000250"
FT DISULFID 450..474
FT /evidence="ECO:0000250"
FT DISULFID 518..543
FT /evidence="ECO:0000250"
FT DISULFID 529..550
FT /evidence="ECO:0000250"
FT DISULFID 538..569
FT /evidence="ECO:0000250"
FT DISULFID 563..574
FT /evidence="ECO:0000250"
FT DISULFID 598..635
FT /evidence="ECO:0000250"
FT DISULFID 602..640
FT /evidence="ECO:0000250"
FT DISULFID 613..625
FT /evidence="ECO:0000250"
FT DISULFID 939..981
FT /evidence="ECO:0000250"
FT DISULFID 943..986
FT /evidence="ECO:0000250"
FT DISULFID 954..970
FT /evidence="ECO:0000250"
FT VAR_SEQ 1063..1072
FT /note="CSVTCERGTQ -> VGALVSRERG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_007664"
FT VAR_SEQ 1073..1224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_007665"
FT VARIANT 110
FT /note="M -> V (in dbSNP:rs1863968)"
FT /id="VAR_057076"
FT VARIANT 486
FT /note="A -> T (in dbSNP:rs16875054)"
FT /id="VAR_057077"
FT VARIANT 789
FT /note="R -> C (in dbSNP:rs9313105)"
FT /id="VAR_057078"
FT VARIANT 859
FT /note="R -> L (in dbSNP:rs16875122)"
FT /id="VAR_057079"
FT VARIANT 863
FT /note="E -> K (in dbSNP:rs35394775)"
FT /id="VAR_057080"
FT CONFLICT 90
FT /note="P -> A (in Ref. 1; CAC86015)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> P (in Ref. 1; CAC86015)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> Y (in Ref. 4; BAC23125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1224 AA; 136203 MW; FB6115E6C97A9683 CRC64;
MKPRARGWRG LAALWMLLAQ VAEQAPACAM GPAAAAPGSP SVPRPPPPAE RPGWMEKGEY
DLVSAYEVDH RGDYVSHEIM HHQRRRRAVP VSEVESLHLR LKGSRHDFHM DLRTSSSLVA
PGFIVQTLGK TGTKSVQTLP PEDFCFYQGS LRSHRNSSVA LSTCQGLSGM IRTEEADYFL
RPLPSHLSWK LGRAAQGSSP SHVLYKRSTE PHAPGASEVL VTSRTWELAH QPLHSSDLRL
GLPQKQHFCG RRKKYMPQPP KEDLFILPDE YKSCLRHKRS LLRSHRNEEL NVETLVVVDK
KMMQNHGHEN ITTYVLTILN MVSALFKDGT IGGNINIAIV GLILLEDEQP GLVISHHADH
TLSSFCQWQS GLMGKDGTRH DHAILLTGLD ICSWKNEPCD TLGFAPISGM CSKYRSCTIN
EDTGLGLAFT IAHESGHNFG MIHDGEGNMC KKSEGNIMSP TLAGRNGVFS WSPCSRQYLH
KFLSTAQAIC LADQPKPVKE YKYPEKLPGE LYDANTQCKW QFGEKAKLCM LDFKKDICKA
LWCHRIGRKC ETKFMPAAEG TICGHDMWCR GGQCVKYGDE GPKPTHGHWS DWSSWSPCSR
TCGGGVSHRS RLCTNPKPSH GGKFCEGSTR TLKLCNSQKC PRDSVDFRAA QCAEHNSRRF
RGRHYKWKPY TQVEDQDLCK LYCIAEGFDF FFSLSNKVKD GTPCSEDSRN VCIDGICERV
GCDNVLGSDA VEDVCGVCNG NNSACTIHRG LYTKHHHTNQ YYHMVTIPSG ARSIRIYEMN
VSTSYISVRN ALRRYYLNGH WTVDWPGRYK FSGTTFDYRR SYNEPENLIA TGPTNETLIV
ELLFQGRNPG VAWEYSMPRL GTEKQPPAQP SYTWAIVRSE CSVSCGGGQM TVREGCYRDL
KFQVNMSFCN PKTRPVTGLV PCKVSACPPS WSVGNWSACS RTCGGGAQSR PVQCTRRVHY
DSEPVPASLC PQPAPSSRQA CNSQSCPPAW SAGPWAECSH TCGKGWRKRA VACKSTNPSA
RAQLLPDAVC TSEPKPRMHE ACLLQRCHKP KKLQWLVSAW SQCSVTCERG TQKRFLKCAE
KYVSGKYREL ASKKCSHLPK PSLELERACA PLPCPRHPPF AAAGPSRGSW FASPWSQCTA
SCGGGVQTRS VQCLAGGRPA SGCLLHQKPS ASLACNTHFC PIAEKKDAFC KDYFHWCYLV
PQHGMCSHKF YGKQCCKTCS KSNL
