ID A0A3P8SER4_AMPPE Unreviewed; 1168 AA.
AC A0A3P8SER4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 3 {ECO:0000313|Ensembl:ENSAPEP00000010595.1};
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:ENSAPEP00000010595.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000010595.1, 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:ENSAPEP00000010595.1}
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; A0A3P8SER4; -.
DR STRING; 161767.ENSAPEP00000010595; -.
DR Ensembl; ENSAPET00000010883.1; ENSAPEP00000010595.1; ENSAPEG00000007558.1.
DR GeneTree; ENSGT00940000156085; -.
DR OMA; GYCDANK; -.
DR Proteomes; UP000265080; Chromosome 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000265080};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1168
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017945171"
FT DOMAIN 255..459
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1007..1050
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1087..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 397
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 401
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 407
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 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 332..381
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 375..454
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 414..440
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..515
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..534
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..539
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 562..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 566..604
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 577..589
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1168 AA; 131739 MW; A2EF73F71D4849E3 CRC64;
MLMTSLHRMF IGVLMGLIYV LKEETAKQLR SRLKEYGLVT PFSTDSHGHY LSHLLSATHK
QRVKRETFSS GDSEQRLFFN ISAFGKEFHL RLRPNNRLVA PGAMVEWHDE IQAFGNFSTA
NVSTVDQAEP GHNATERILR RELLKTDCTF TGDITDVPGA SVAINNCDGL AGMIRTDSDE
YFIEPLEKGA QELEDQGRVH MVYRRSALLQ EQSDISMDYQ LQEPELDVPR TLDSVTRQVN
ETLHRHRRDA GEDDYNIEIL LGVDDSVVRF HGKEHVQNYL LTLMNIVNEI YHDESLGVHI
NVVLVRMIML GYAKSISLIE RGNPSRSLEN VCRWAFVQQK GDPDHAEHHD HAIFLTRQGF
GPTGMQGYAP VTGMCHPVRS CTLNHEDGFS SAFVVAHETG HVLGMEHDGQ GNRCGDETAM
GSVMAPLVQA AFHRYHWSMC SGQELKRYIH TYDCLLDDPF KHDWPQLPEL PGINYSMDEQ
CRFDFGVGYK ICTSFRTFDP CKQLWCSHPD NPYFCKTKKG PPLDGTECAP GKWCYKGHCM
WKNPNQVKQD GSWGSWSKYG SCSRSCGTGV RFRTRQCNNP APSNGGQDCP GVNYEYQLCN
TDDCPKHFED FRAQQCQLRN SHFEFQNAKH HWLPYEHPDT SKRCHLYCQS KETGDVVYMK
LLVHDGTRCS YKDAYSICVR GECVKVGCDR EIGSNKVEDK CGVCGGDNSH CRTVKGTFTR
TPKKAGYLKM FLIPPGARHV IIQEHEASPQ ILAIKNQATG HYILNGKGEE VKSRSFIDLG
VEWHYIMEED VETLHTDGPL HDPVVVLIIP RDNETRSTLM YKYIIHEDSV PVNNNNVIQE
DTYEWALKSW SPCSKPCAGG FQYTKYGCRK KGDSKMVHRG YCDANKKPKP IRRMCNLQDC
TQPQWISDEW EHCTKTCGSL GFQIRTVRCV QFLHDGTNRS VHSKYCSGEK PESRRPCNRV
SCPAQWRTGA WSECSVTCGE GMERRLVTCR IGDQCNGEKP ENVRMCRPGP CHDEPCNGDK
SIFCQMEVLT RYCSIPGYNK LCCDSCSKRT GVLSLFSEAA ETEEHVRFGS ASQLLETLTA
SVAANSTRAG KQSLGKGSNT SGSAAKQTST TAPGKKAPSK ITTAPRRVPR HVDLTGRKLS
TVADLTEDQT SSSSMESRRP TAYSEVER
//
