ADT1_CAEEL
ID ADT1_CAEEL Reviewed; 1461 AA.
AC G5ECS8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs adt-1 {ECO:0000305};
DE Short=ADAMTS adt-1 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9P2N4};
DE Flags: Precursor;
GN Name=adt-1 {ECO:0000303|PubMed:11796737, ECO:0000312|WormBase:C02B4.1};
GN ORFNames=C02B4.1 {ECO:0000312|WormBase:C02B4.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:BAC05514.1};
RN [1] {ECO:0000312|EMBL:BAC05514.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11796737; DOI=10.1074/jbc.m200144200;
RA Kuno K., Baba C., Asaka A., Matsushima C., Matsushima K., Hosono R.;
RT "The Caenorhabditis elegans ADAMTS family gene adt-1 is necessary for
RT morphogenesis of the male copulatory organs.";
RL J. Biol. Chem. 277:12228-12236(2002).
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).
CC -!- FUNCTION: Plays a role in ray morphogenesis in the male tail, probably
CC by remodeling the extracellular matrix (ECM) in the cuticle.
CC {ECO:0000269|PubMed:11796737}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In hermaphrodites, expressed in the vulva, head
CC ganglia, ventral nerve cord and amphid neurons. Expressed in the rays
CC of the male tail. {ECO:0000269|PubMed:11796737}.
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}.
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DR EMBL; AB066246; BAC05514.1; -; mRNA.
DR EMBL; BX284606; CAA90293.2; -; Genomic_DNA.
DR PIR; T18856; T18856.
DR RefSeq; NP_510116.2; NM_077715.4.
DR AlphaFoldDB; G5ECS8; -.
DR SMR; G5ECS8; -.
DR STRING; 6239.C02B4.1; -.
DR MEROPS; M12.302; -.
DR EPD; G5ECS8; -.
DR PaxDb; G5ECS8; -.
DR EnsemblMetazoa; C02B4.1a.1; C02B4.1a.1; WBGene00000082.
DR GeneID; 181412; -.
DR KEGG; cel:CELE_C02B4.1; -.
DR CTD; 181412; -.
DR WormBase; C02B4.1; CE31872; WBGene00000082; adt-1.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_004934_0_0_1; -.
DR InParanoid; G5ECS8; -.
DR OMA; CRNIKRP; -.
DR OrthoDB; 211122at2759; -.
DR PhylomeDB; G5ECS8; -.
DR PRO; PR:G5ECS8; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000082; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; G5ECS8; 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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 12.
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; 12.
DR SMART; SM00209; TSP1; 13.
DR SUPFAM; SSF82895; SSF82895; 12.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 12.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..163
FT /evidence="ECO:0000255"
FT /id="PRO_0000440900"
FT CHAIN 164..1461
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs adt-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440951"
FT DOMAIN 233..435
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 464..546
FT /note="Disintegrin"
FT /evidence="ECO:0000305"
FT DOMAIN 708..759
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 761..802
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 804..852
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 853..898
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 903..952
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 955..1000
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1035..1083
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1087..1133
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1148..1200
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1203..1260
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1265..1321
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1324..1378
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1382..1435
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MOTIF 190..197
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT ACT_SITE 389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 405..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 719..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 723..758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 735..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 816..846
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 820..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 831..836
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 862..892
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 866..897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 877..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1047..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1051..1082
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1062..1067
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1160..1194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1162..1199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1173..1184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1215..1253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1219..1259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1231..1243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1277..1314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1281..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1292..1304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1336..1372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1340..1377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1351..1362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 1461 AA; 162616 MW; 3CFDC1C07C1F493A CRC64;
MPPFYIVITF LLSTVFRISQ SVHHHLNEEE LKQVFGVSNK HDVPEYSLIE ATRHPLKNGN
LKMKFTAWND TYHLNLRKNS RIVSPHIISV VRHGDDDVTT YAGLRDYEQC HYQGEVKSHG
NMKAAISDCG ALMGSIVMED HFLVLQTLPK RVHHLQKERH LVYKRSAGLL TNAESKIREE
ITRLQEEQES FCDTSEQLDD PAMTIPAHLH FNYTIPTSAQ LDSSFIFPNM DPITLEIGLF
LDSKLFEHFE REYIQDAEQH LLEFSLALIN NVHVLYQQDT LTPNLDIVIV RYEMWRTQPS
ALSTGVHKNG QAQSLLDAFC RYQAHMNPGT DLTDMNHYDH GVLLTGYDIY HTTTSVAGVA
PVARMCDPLF ACSLVEGLHL GRSFVLAHEM GHNMGMVHDG VQNQCNKGCC LMSAVNGAGK
TTWSDCSVRE FNAFLLQLDE SGRGNCLRDA SPGLISTNHL SDLRLPGQRF TADQQCSYFW
GRDYKVEIPN GKAMDDICRI LWCGNSGSTI STAHPALEGS WCGANKWCHK GQCTHWTFGL
TPVPIDGEWS EWGGAEKGCP IQQCAVSGSI TVQGQHRDCV NPAPNNGGKT CEGANIRGIV
CGATSSNCLG FTREEFGNKI CSSIKYDPHK PDQQLTGEGF EHSTQPCRVW CHLIGSELIR
NKGQFPDGTP CGFDAYCVGG QCLALSCDNK ALVEQPEDCP RIEGRSVHQW EEWSSWSECS
VSCGLGGREV RERKCSSGRK CQGVSEESRP CEGVLRDCEE FGEWKEWGSC SEKCALGVQK
RFRPCLTDQC SSKHLQEERP CDNEGCWTNW DEWSSCSQSC GGGRRYRIRK CLDDKCDGDD
LEKESCNTQK CISQSWGDWL PCSVSCGIGF QIRERLCDGE LCATANKQAR TCNQQQCPSA
FSLSVWSEWG EWTTCSATCG EGLQSRERSC RRGSCTEDDA SQTRRCVNGP CEHSYLTWSE
WTTCETCSSF DSRKRIAKCD GTTENCQDKI DEETCDIACL REKHSFGPIS PRRPKLITSN
DLRKAFGRPL LPIESIHSEK WSEWGPCSVT CGSGRRVRTR GCQEASCPEQ HIQTEECNLN
SCLELFIWSD WSSCSKSCGQ DGIQTRQKLC LFNNAECSSY AESRRCKDLP SCSSISSGRT
ISENGFDAPR WSEWSSWSAC SCFSLTSTRR RFCQVVDPTV QGFCAGAILE QIPCAPGSCS
PSAGGWSLWS EWSSCSKDCG DTGHQIRNRM CSEPIPSNRG AYCSGYSFDQ RPCVMDNVCS
DEKVDGGWTD WTAWSECTDY CRNGHRSRTR FCANPKPSQG GAQCTGSDFE LNPCFDPARC
HLRDGGWSTW SDWTPCSASC GFGVQTRDRS CSSPEPKGGQ SCSGLAHQTS LCDLPACDHE
SDGEWSAWNE WSGCMGNCGI GTRTRVRACV SPPVSDGGQP CFGRSSEITE CRQSPSTALC
SSFITSSHLA DGYFIDTDQQ Q
