ADT2_CAEEL
ID ADT2_CAEEL Reviewed; 1020 AA.
AC Q19204; Q8IU50;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 5.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs adt-2 {ECO:0000305};
DE Short=ADAMTS adt-2 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9P2N4};
DE Flags: Precursor;
GN Name=adt-2 {ECO:0000312|WormBase:F08C6.1a};
GN Synonyms=sma-21 {ECO:0000312|WormBase:F08C6.1a};
GN ORFNames=F08C6.1 {ECO:0000312|WormBase:F08C6.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAC41253.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ishikawa Y., Inoue H., Takahashi K.;
RT "ADAMTS-like protease from C. elegans.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-364.
RX PubMed=21256840; DOI=10.1016/j.ydbio.2011.01.016;
RA Fernando T., Flibotte S., Xiong S., Yin J., Yzeiraj E., Moerman D.G.,
RA Melendez A., Savage-Dunn C.;
RT "C. elegans ADAMTS ADT-2 regulates body size by modulating TGFbeta
RT signaling and cuticle collagen organization.";
RL Dev. Biol. 352:92-103(2011).
CC -!- FUNCTION: Regulates body size probably independently of the TGF beta-
CC like dbl-1 pathway. However, may regulate some dbl-1-mediated
CC transcription. Plays a role in cuticle collagen fibril organization.
CC Required for embryonic development. {ECO:0000269|PubMed:21256840}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at the L1 larval stage in glial
CC cells associated with amphid, phasmid, labial and posterior deirid
CC sensory neurons and continues throughout adulthood. Expressed in vulva
CC at the L4 larval stage and in adults. {ECO:0000269|PubMed:21256840}.
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. {ECO:0000250|UniProtKB:P03956}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC adult body length and width and a reduction in adult lifespan. The
CC cuticle displays several defects including disruption of the lateral
CC cuticle overlying the seam cells, abnormal constriction of the annuli,
CC discontinuous alae and mislocalization of collagen col-19 positive
CC fibrils. Prevents the up-regulation of a transcriptional reporter of
CC the TGF beta-like dbl-1 pathway, RAD-SMAD.
CC {ECO:0000269|PubMed:21256840}.
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DR EMBL; AB072347; BAC41253.1; -; mRNA.
DR EMBL; BX284606; CCD67341.2; -; Genomic_DNA.
DR PIR; T15976; T15976.
DR RefSeq; NP_001024532.2; NM_001029361.3.
DR AlphaFoldDB; Q19204; -.
DR IntAct; Q19204; 2.
DR STRING; 6239.F08C6.1a.2; -.
DR MEROPS; M12.A47; -.
DR PaxDb; Q19204; -.
DR PeptideAtlas; Q19204; -.
DR EnsemblMetazoa; F08C6.1a.1; F08C6.1a.1; WBGene00000083.
DR GeneID; 181022; -.
DR KEGG; cel:CELE_F08C6.1; -.
DR UCSC; F08C6.1a.1; c. elegans.
DR CTD; 181022; -.
DR WormBase; F08C6.1a; CE48012; WBGene00000083; adt-2.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_296160_0_0_1; -.
DR InParanoid; Q19204; -.
DR OMA; HYDGICY; -.
DR OrthoDB; 211122at2759; -.
DR PhylomeDB; Q19204; -.
DR PRO; PR:Q19204; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000083; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q19204; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008361; P:regulation of cell size; IMP:WormBase.
DR Gene3D; 2.20.100.10; -; 7.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 6.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 6.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..163
FT /evidence="ECO:0000255"
FT /id="PRO_0000440901"
FT CHAIN 164..1020
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs adt-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5010117116"
FT DOMAIN 211..407
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 431..529
FT /note="Disintegrin"
FT /evidence="ECO:0000250|UniProtKB:G5ECS8"
FT DOMAIN 702..751
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 757..811
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 813..861
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 863..911
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 915..963
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 966..1015
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MOTIF 174..181
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT ACT_SITE 362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 376..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 714..745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 718..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 729..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 769..805
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 773..810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 784..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 825..855
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 829..860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 840..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 875..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 879..910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 890..895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 927..957
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 931..962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 942..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 978..1009
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 982..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 993..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MUTAGEN 364
FT /note="G->S: In wk156; reduced seam cell size, lifespan and
FT reduced adult body length with increased body width."
FT /evidence="ECO:0000269|PubMed:21256840"
SQ SEQUENCE 1020 AA; 113527 MW; 232095EE5B98FAC7 CRC64;
MLLPLLISGL LFRNADAFLP FFNEDDLKYT FGVDTHAEVP NHEEIDPVPY YHQNGSLHKL
EFMAFNKKYN LSLEPTLAKL LSSGVTVVKK NEKKGGSLDF GSTLDSCHYH HYGEKVYAAI
SNCDGRIKGT VIDDGEIIVV HPFPDHHAHR SKRATENGAH VVYKRETLAG EPKDFCGLDN
VVTEESLVED ESAIFEDVFV TGQRLTQQSD LIVELAVFVD ENLWRHFSSK HGGMADRKLQ
DYTLTLLNNI QIMYYQPTAS PPLTFRVIRY EVLTRQPSAL AGYLHNHGNA QMYLDRFCRY
QRNLAVRDWD HAIMLTGYDI HRGAGSRSIS GIARLDGMCD PWNTCTLAEG LDFTSAFIGT
HELGHSVGMR HDEPYCQSKH IMSSSLGPGK VTWSTCSLRD YHQFLQRLDG RGKNCLRVSN
MPNKLEISSN VKPGQIYDAN LQCELMHGNG YQQVTPRQDS YDGICYMMWC GQSSFGRIIT
SHPALEGTFC GPSKWCQLGR CVPWTGTNEI QPTVQHVAPV VTTLPSRIDG SWSGWGATIC
SQCTCNGILG SVGLAIARRT CSAPYPANGG SDCVGSTSRA VLCSRQCGRA SKSVDEYISD
KCMEQKRLKN DRELTGKGSQ LNRFPQRACK VFCDVQQHYG SQRNYRFFGD NLPDGTSCGY
DRYCLDGECL ALNCNNNALI SRDQSCPTDT CPITDQSSSV YRGQWGTWSL WTSCTATCGG
GYRKRNRACS ITGQCEGNED ETEVCSSESC PSVLRVGNEW STWTEWNHCS VSCGRGSQAR
YRKCLSPHRT LAFDCPEKNI EVRSCDNGPC NAIGVWGTWG GWSTCSTSCG PGTLVRQRTC
NREPCDGSAH ERRSCNVATC QNDGIWSLWN EWSDCSRVCG KGLRSRSRSC FGSGCMGASS
EQQFCNEQAC ASSSANDWGT WSGWSQCSVS CGAGVKRRTR TCRTGNCPGN YKESAICNDR
DCENKNAAWG GWGYWSSCSE TCGDGVRKRV RKCYGSGNCD GQQYEKQYCN LRVCDFRRKF
