ID A0A1B8Y8K2_XENTR Unreviewed; 1198 AA.
AC A0A1B8Y8K2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=XENTR_v90029255mg {ECO:0000313|EMBL:OCA19341.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:OCA19341.1};
RN [1] {ECO:0000313|EMBL:OCA19341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA19341.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA van de Peer Y., Weigel D., Grigoriev I.V.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCA19341.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA19341.1};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3] {ECO:0000313|EMBL:OCA19341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nigerian {ECO:0000313|EMBL:OCA19341.1};
RA Sessions A., Jenkins J., Mitros T., Lyons J.T., Dichmann D.S., Robert J.,
RA Harland R.M., Rokhsar D.S.;
RT "WGS assembly of Xenopus tropicalis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KV460381; OCA19341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8Y8K2; -.
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; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 4.
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:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 254..458
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1009..1052
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1144..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 331..380
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..453
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 413..439
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 480..505
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 491..514
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 527..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 561..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..603
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..588
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1198 AA; 135379 MW; 0AE9A56885BB693B CRC64;
MAYPVVRVMV PSLALLWSHY FKNFETNKYI FDDLLQKKLG EYEVITPVST DAEGRLMSTI
VSVNHKKRFT RDTSQVQHTL YFNVTAFGRE FHLKLRPNTK LIAPGAVIEW HEDQVNLTNG
FHSGNQNPDN DTAHQIWRKE SLWTNCAYVG EITDSPGALV ALSNCDGLAG MIRTKEDEYF
IEPLERGKQK DEENGRLHVV YKRSTAKQIP TGDSHNFSEA DFAGLDNVDS IFSNIEKQVN
ETLRRRRHAG ENDYNIEVLL GVDDSVVRFH GKEHVQNYLL TLMNIVNEIY HDDSIGVHIN
IVLVRMIMLG YAKSISLIER GSPSRSLDNV CRWASQQQKA DPNHSEHHDH AIFLTRQDFG
PAGMQGYAPV TGMCHPMRSC TLNHEDGFSS AFVVAHETGH VLGMEHDGQG NRCGDETAMG
SVMAPLVQAA FHRYHWSRCS GQELKRYIHS YDCLLDDPFE HDWPKLPDLP GINYSMDEQC
RFDFGVGYKM CTAFRTFEPC KQLWCNHPDN PYFCKTKKGP PLDGTECAPG KWCYKGHCMW
KTTNQVKQDG NWGSWTKFGS CSRTCGIGVR FRTRQCNNPM PVNGGQDCSG LNYEYQLCNT
EECPKHFEDF RAQQCQQRNS NFEYQNAKHH WLPYEHPDAN KRCQLYCQSK ETGSIASMKQ
LVHDGTRCSY KDPHSICVRG ECIKVGCDKE IGSNKVDDKC GVCGGDNAHC RTVKGTFTRT
PKKSGYLKMF DIPPGARHVF IQEDEASPHV LAIKNQATGH YILNGKGEEA KSRSFIDLGV
EWEYIIEDDI ETVHTDGPLH DAIVVLVIPQ ENDTKSSLTY KYIIHEDSVP TISHNNVLQE
ESDTYEWALK SWSQCSKPCG GGFQYTKYGC RRKSDNKMVH RSFCEANKKP KPIRRMCNLQ
ECTQPIWITD AWEHCTKSCG SSGYQIRSVR CIQPLHDGTN RSVHSKYCNG DRPESRRPCN
RVPCLAQWKT GAWSECSVTC GEGIEVRQVL CRAGDQCDGE KPESMRDCKL TPCSDEPCLG
DKSIFCQMEV LARYCSIPGY NKLCCESCSK RGTQQPPYFT EAAETEDELF FDPSDLSKAG
MTPTALAPLD AEATSERKKA LAALSFAESD ADLGILSVPE SRPKFSDQAQ RRSHVAAGKN
LARIVGIPPP TPNSNIHLHR PSMPDMDTGH LSSPGRTSRR NDKSFEKRRS LQSSTTER
//
