ID A0A3Q1CH67_AMPOC Unreviewed; 943 AA.
AC A0A3Q1CH67;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ADAM metallopeptidase domain 19 {ECO:0000313|Ensembl:ENSAOCP00000027072.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027072.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027072.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q1CH67; -.
DR Ensembl; ENSAOCT00000018856.1; ENSAOCP00000027072.1; ENSAOCG00000015615.1.
DR GeneTree; ENSGT00940000159624; -.
DR OMA; HGMMSPR; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..943
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018784298"
FT TRANSMEM 734..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..437
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 445..531
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 683..715
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 787..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 503..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 687..697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 705..714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 943 AA; 102022 MW; 395DDE2A1565AC20 CRC64;
MRPGARPPPP APPRLLLLLD AVRFSLCFVL FLHCVEAAAA SEGAVYNAGE NTQDSQRSIL
QHVQSYEITY PIWLHPLRHK RSANKEHPAE EQVLISAEGQ ELRLQLEKNE QLLATGYQEI
WYTPDGVRKS SSRAKTGQCF YHGKVLGMEG SSVAVSTCSG LRGLISLNTS VSYLIEPLPA
SADPQRHAVF RAESLHLPRG SCLHHHGNNE HEDELNDFIH GMMSPRSTRE KRELSQNMKY
VELLIVADKA EFEKHGSDLE KTKLKLLEAA NLVDKYYKAL SIRVALIGLE VWTSQDMISV
SDNPHGTLAA FLSWRRRQLH ALPNDNAQLI TGRPFQGTTI GLAPLKAMCS DYQSGGVNTD
HSESAVGVAA TMAHEMGHNF GMSHDSAGCC QARAEDGGCI MAAATGHPFP RVFNACNMKE
LKSYLSSGGG KCLFNLPNTR AMYGGQRCGN GYLEDGEECD CGEEEECTSP CCNANNCTLK
AGAECAHGVC CQNCKLKSPG VLCRAPSGPC DLPEYCDGKA ESCPANFYLV DGTSCAGGQA
YCYTGMCLTL EQQCRSLWGR DGRPAPDLCF KKVNEAGDMY GNCGKDLQGK YRSCKERDAK
CGKIQCSASA SKPIENNAVR IETTVSVGSR KVQCLGTHVY KLGQGDEEPQ SDTLDPGLVM
TGTKCGEDLI CFNGECRNAS FLRADECNTK CHGHGLCNNN HNCHCDSGWA PPRCDQKGSG
GSLDSGPVIS HSSLLPVLLV LPLALFVVLA AVGLWCCYKH KLRPLKSSAP PPVPDCSVPI
EGKPLYTDDN VNGHTNPTFL LKKQDSDQLG KPSPRPSPSC PARPRHAIVR PAVKPPPIPA
YAHIQPAAPP QRKYSPQDYT PPPLKSAQAS PPLSGPSMDP KNQPSAIPKH RPEPPNRPPP
PCPVNRPSGG QQHVKDLQVT TNALPRGKAA LAPSAGQKKP NRA
//
