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   24-JAN-2024, entry version 177.
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; 3.
DR   IntAct; Q8TE57; 2.
DR   STRING; 9606.ENSP00000274181; -.
DR   MEROPS; M12.026; -.
DR   GlyCosmos; Q8TE57; 7 sites, No reported glycans.
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; 9606-ENSP00000274181; -.
DR   PeptideAtlas; Q8TE57; -.
DR   ProteomicsDB; 74398; -. [Q8TE57-1]
DR   ProteomicsDB; 74399; -. [Q8TE57-2]
DR   Antibodypedia; 59056; 56 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   AGR; HGNC:17108; -.
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   OrthoDB; 2910701at2759; -.
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; 6 hits in 1146 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 107 other cell types or tissues.
DR   ExpressionAtlas; Q8TE57; 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: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   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; 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:SF140; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 16; 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; PF08686; PLAC; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 6.
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   Genevisible; Q8TE57; HS.
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
//