ID A0A3B3R1I8_9TELE Unreviewed; 1071 AA.
AC A0A3B3R1I8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 3 {ECO:0000313|Ensembl:ENSPKIP00000011561.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000011561.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000011561.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3R1I8; -.
DR Ensembl; ENSPKIT00000023507.1; ENSPKIP00000011561.1; ENSPKIG00000018591.1.
DR GeneTree; ENSGT00940000156085; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261540; Unplaced.
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, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1071
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017300863"
FT DOMAIN 253..457
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 1052..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
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 399
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 405
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 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 330..379
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 373..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 412..438
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 479..504
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 499..532
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 526..537
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 560..597
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 564..602
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..587
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1071 AA; 121504 MW; 78A3E357F9745272 CRC64;
MNLLSQCLFV VVGFTVTLTS ANKASGVEKK EYLKNRLKEY GLITPISTDS EGRYLSCLLS
ANHKQRIRRD VSQGFQARNY NLFFNITAFG RALHLRLRPN ERLVAPGAKV EWRDEVANSE
NDTNTEIQNQ SSIRIERILK RELLKTDCTF VGDITDVPGA SVAINNCDGL AGIIRTDSDE
YFIEPLERGT QEQEKEGRVH VVYRRSDVLH SSSGTSIDYQ VVDSVDTPGT LNNIVQYVNK
TRRKRRHAGD NDYNIEVLLA VDDSVVRFHG KEHVQNYLLT LMNIVNEIYH DVSLGCHINV
VLVRMIMLGY PKSVSLIERE NPSRSLENVC RWAFIQQKAD PEHCEHHDHA IFLTRQSFGP
TGMQGYAPVT GMCHPVRSCT LNHEDGFSSA FVVAHETGHV LGMEHDGQGN RCGDETAMGS
VMAPLVQAAF HRYHWSICSG QELKKYIHSY DCLLDDPFMH DWPQIPELPG MNYSMDDQCR
FDFGVGYKIC TSFRTFDPCK QLWCSHSDNP YFCKTKKGPP LDGTECAPGK WCYKGHCMWR
TSNHAKQDGA WSSWTKFGSC TRSCGTGVRF RTRQCNNPVP SNGGQDCPGV NFEYQLCNMD
DCPKKSEDFR AQQCQKRNLY FKFQNSKHHW LPYEHPDTNK RCHLHCQSRQ TSDVAYMKQL
VHDGTRCSYR DPHSICVRGE CVKVGCDKEI GSNKVEDNCG VCGGDNSHCR TVKGTFTRTP
KKSDKYKGHF KMLLIPPAAR HVMVQEHEGL PQILAIKNQA TGQYILNGKG VEAKSKTFID
LGVQWNYIIE NNVETLYTDG PLNDEVVVLI IPQDNKTTST LMYKYIIHED SIPVHHNNVI
QEDIYEWALK NWSQCSRPCA GGFQYTKYGC RKKGDSKMAH QSYCDVSKKP KPVRRICNME
ECITPQWIAE EWEHCTKTCG NLGYQIRTVQ CMQLLHEGAN RSVHSKHCSG KKPESRRPCN
RQLCPAQWRT GTWLKCSVTC GEGVEHRLVT CPTGGQCNGD KPEAIRPCKR GLCHDEQCTG
DKSIFCQMEV LARYCSIPGY NKLCCESCSK NGSSPTPFFS EAAEDEEEFL S
//
