ID A0A3P8S1A9_AMPPE Unreviewed; 942 AA.
AC A0A3P8S1A9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 15b {ECO:0000313|Ensembl:ENSAPEP00000006668.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000006668.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000006668.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000006668.1}
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; A0A3P8S1A9; -.
DR STRING; 161767.ENSAPEP00000006668; -.
DR Ensembl; ENSAPET00000006841.1; ENSAPEP00000006668.1; ENSAPEG00000004759.1.
DR GeneTree; ENSGT00940000155801; -.
DR OMA; WKEEKSH; -.
DR Proteomes; UP000265080; Chromosome 9.
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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 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; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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 Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 215..424
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 358
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 362
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 368
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 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 290..342
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 319..324
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 336..419
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..403
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..467
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 456..477
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 462..496
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..501
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..558
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 525..563
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 536..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 942 AA; 104088 MW; D7D03847B8940D5C CRC64;
SSPLPCSLSS LCWGATCCFE VDFCIPVRVD HHKHEKHVHR RTEQMNERQV VFRLSAFKQE
FYLRLMPDSS FLAAGSMLPE SDSTASDASA AADLRECFYS GDVNADPDSF AALSLCKGLQ
GGFSYNGMEY FISQSRNEDA PGYGNSFDRT HVIRRRRRAA HSGGNFTSRC GVTPDTNFTI
SLEKYKFMSE LEIDGLTETV LKSLGRSKRF ASIPRFVEVL VVADESMAKF HGDDLKHYLL
TLMSVAARLY KHPSILNSIN IVVVGFMVIN EADKGPKVSS NAALTLRNFC SWQKKLNKHS
DKHPEYWDTA ILFTKQDLCG ATTCDTLGMA DVGTMCDPKR SCSVIEDDGL PSAFTTAHEL
GHVFNMPHDN VKACEEVFGK LKENHMMSPT LIQIDRSRPW SVCSAAIITE FLDRGHGDCL
LDQPQKQLSL PDNLPGSSYS LHRQCELAFG SGSKPCPYMQ PCSKLWCTGK ARGQLVCQTR
HFPWADGTSC GNSKVCYRGA CVDKNSTVDG RWGKWGAFGD CSRSCGGGVQ LAKRECNNPI
PENGGKYCYG LRIKYRSCNL NPCSETGKSF REEQCEAFNG LNLNTNRLGS SVVWVPKYSG
ISPKDKCKLI CRANGTGYFY VLAPKVVDGT PCSPDTSAVC VQGKCIKAGC DGKLDSNKKF
DKCGMCGGDN QGCKKVSGMF TKPIHGYNFV VMLPVGASNI DIRQRGYRGM VSDENYLAVK
NRHGMYLLNG NYVVSAVERD LLVKGSLLRY SGTSTSVEIL QATRPLQEPL TVEVLSVGKM
TPPRVRYSFY ISKESKEEKT LRKEEKSHKA QNSVLADSNK IEAKKQAMGK RPVSHWVTGG
WDSCTVTCGN GLQKRLVQCQ SMEGRPAADC NSADRPVAVR ACGDPCPMWD VGTWSHCSKS
CGRGFKRRPV RCMAENGLTL PRDHCSGRRK PQELDLCNLK PC
//
