ATS16_MOUSE
ID ATS16_MOUSE Reviewed; 1222 AA.
AC Q69Z28; Q8K206;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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).
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=Q69Z28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69Z28-2; Sequence=VSP_014991, VSP_014992;
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; AK173338; BAD32616.1; -; mRNA.
DR EMBL; BC034739; AAH34739.1; -; mRNA.
DR CCDS; CCDS36723.1; -. [Q69Z28-1]
DR RefSeq; NP_742050.2; NM_172053.3. [Q69Z28-1]
DR AlphaFoldDB; Q69Z28; -.
DR SMR; Q69Z28; -.
DR BioGRID; 234828; 1.
DR STRING; 10090.ENSMUSP00000079041; -.
DR MEROPS; M12.026; -.
DR GlyGen; Q69Z28; 9 sites.
DR iPTMnet; Q69Z28; -.
DR PhosphoSitePlus; Q69Z28; -.
DR PaxDb; Q69Z28; -.
DR PRIDE; Q69Z28; -.
DR Antibodypedia; 59056; 46 antibodies from 14 providers.
DR DNASU; 271127; -.
DR Ensembl; ENSMUST00000080145; ENSMUSP00000079041; ENSMUSG00000049538. [Q69Z28-1]
DR Ensembl; ENSMUST00000109694; ENSMUSP00000105316; ENSMUSG00000049538. [Q69Z28-2]
DR GeneID; 271127; -.
DR KEGG; mmu:271127; -.
DR UCSC; uc007rcz.1; mouse. [Q69Z28-1]
DR CTD; 170690; -.
DR MGI; MGI:2429637; Adamts16.
DR VEuPathDB; HostDB:ENSMUSG00000049538; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159433; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; Q69Z28; -.
DR OMA; LRCAEKY; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q69Z28; -.
DR TreeFam; TF313537; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 271127; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q69Z28; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q69Z28; protein.
DR Bgee; ENSMUSG00000049538; Expressed in efferent duct and 95 other tissues.
DR ExpressionAtlas; Q69Z28; baseline and differential.
DR Genevisible; Q69Z28; MM.
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; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048232; P:male gamete generation; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1902017; P:regulation of cilium assembly; ISO:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
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; 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; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..277
FT /evidence="ECO:0000250"
FT /id="PRO_0000029196"
FT CHAIN 278..1222
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 16"
FT /id="PRO_0000029197"
FT DOMAIN 288..493
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 494..583
FT /note="Disintegrin"
FT DOMAIN 584..639
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 872..920
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 925..985
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 986..1046
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1049..1113
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1125..1179
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1184..1221
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 745..871
FT /note="Spacer"
FT MOTIF 245..253
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 247
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 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 154
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 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 364..415
FT /evidence="ECO:0000250"
FT DISULFID 390..397
FT /evidence="ECO:0000250"
FT DISULFID 409..488
FT /evidence="ECO:0000250"
FT DISULFID 448..472
FT /evidence="ECO:0000250"
FT DISULFID 516..541
FT /evidence="ECO:0000250"
FT DISULFID 527..548
FT /evidence="ECO:0000250"
FT DISULFID 536..567
FT /evidence="ECO:0000250"
FT DISULFID 561..572
FT /evidence="ECO:0000250"
FT DISULFID 596..633
FT /evidence="ECO:0000250"
FT DISULFID 600..638
FT /evidence="ECO:0000250"
FT DISULFID 611..623
FT /evidence="ECO:0000250"
FT VAR_SEQ 886..900
FT /note="GKMNSKAGCYRDLKV -> DRQCQTGRGHLEISS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014991"
FT VAR_SEQ 901..1222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014992"
SQ SEQUENCE 1222 AA; 136282 MW; 3A95FB40A8F15083 CRC64;
MESRGCAALW VLLLAQVSEQ QTPACALGLA AAASGSPEDP QPPPFSGSSW LETGEYDLVS
AYEVDHRGDY VSHDIMHYQR RRRRRAVTQP GGDALHLRLK GPRHDLHLDL KAASNLMAPG
FMVQTLGKGG TKSVQMFPPE ENCFYQGSLR SQGNSSVALS TCQGLLGMIR TKDTDYFLKP
LPPHLTSKLN RSAQGDSPSH VLYKRSTERQ APRENEVLMI TRKRDLARPH LHHDNFHLGP
SQKQHFCGRR KKYMPQPPND DLYILPDEYK PSSRHKRSLL KSHRNEELNV ETLVVVDRKM
MQSHGHENIT TYVLTILNMV SALFKDGTIG GNINIVIVGL ILLEDEQPGL AISHHADHTL
TSFCQWQSGL MGKDGTRHDH AILLTGLDIC SWKNEPCDTL GFAPISGMCS KYRSCTVNED
SGLGLAFTIA HESGHNFGMV HDGEGNMCKK SEGNIMSPTL AGRNGVFSWS SCSRQYLHKF
LSTAQAICLA DQPKPVKEYK YPEKLPGQLY DANTQCKWQF GEKAKLCMLD FRKDICKALW
CHRIGRKCET KFMPAAEGTL CGQDMWCRGG QCVKYGDEGP KPTHGHWSDW SPWSPCSRTC
GGGISHRDRL CTNPRPSHGG KFCQGSTRTL KLCNSQRCPL DSVDFRAAQC AEYNSKRFRG
WLYKWKPYTQ LEDQDLCKLY CIAEGFDFFF SLSNKVKDGT PCSEDSRNVC IDGMCERVGC
DNVLGSDATE DSCGVCKGNN SDCVTHRGLY SKHHSTNQYY HMVTIPSGAR SIHIYETNIS
TSYISVRNSL KRYYLNGHWS VDWPGRYKFS GATFNYKRSY KEPENLTSPG PTNETLIVEL
LFQGRNPGVA WEFSLPRSGA KKTPAAQPSY SWAIVRSECS VSCGGGKMNS KAGCYRDLKV
PVNASFCNPK TRPVTGLVPC KVSPCPSSWS VGNWSVCSRT CGGGTQSRPV RCTRRAHYRD
ESIPASLCPQ PEPPIHQACN SQSCPPAWST GPWAECSRTC GKGWRKRTVA CKSTNPSARA
QLLHDTACTS EPKPRTHEIC LLKRCHKHKK LQWLVSAWSQ CSVTCQGGTQ QRVLRCAEKY
ISGKYRELAS KKCLHLPKPD LELERACGLI PCPKHPPFDA SGSPRGSWFA SPWSQCTASC
GGGVQRRTVQ CLLRGQPASD CFLHEKPETS SACNTHFCPI AEKRGTFCKD LFHWCYLVPQ
HGMCGHRFYS KQCCNTCSKS NL
