ID A0A3Q1BJU7_AMPOC Unreviewed; 748 AA.
AC A0A3Q1BJU7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Zinc metalloproteinase-disintegrin-like batroxstatin-1 {ECO:0000313|Ensembl:ENSAOCP00000012959.1};
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:ENSAOCP00000012959.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000012959.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; A0A3Q1BJU7; -.
DR Ensembl; ENSAOCT00000020849.1; ENSAOCP00000012959.1; ENSAOCG00000017511.1.
DR GeneTree; ENSGT00940000156716; -.
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 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; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..373
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 381..467
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 599..631
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 677..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 288..368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 328..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 330..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 439..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 603..613
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 621..630
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 748 AA; 82610 MW; 7A2ACEC94F432F9D CRC64;
MSQTADLWLL KKAKKKQLKF HLAAKVTVYT WTMTRTLLLW VLILNASLKP SESHGPEFEE
GKDYEVVRPV RLHTVRKRQA EHLRPQTINY AMTVGGKGIE MQLEKNKGYF RTSAQRYLIE
PLSGDDEGDH AVTTFNEKNF TPAVCGVTNT TWSDDYEPPT GRSRSRSAGI SIVQQQKYIK
LFLVADNREY VKMKRDQTVL RKRIFEVVNF VNMAYKPLRT FIALVGLEVW SNGDLITVTP
PAGANLDAFR TWRNTELVKR KKHDNAHLIS AIDFEGATVG LAYIGTLCSG HSVGVVQDHN
DRAIAVGATL AHEMGHNLGM DHDDSSTCAC SGDSCIMAAA LSWNVPRTFS SCSSNHYEKY
LTNRNPSCLL DKPDYKGIVA PAVCGNGFME QGEQCDCGTV EECTNPCCNA TTCMLKEGSQ
CGDGECCENC QISPRSRECR RKQDDCDLAE FCDGNSATCP EDVFAVNGLP CAGGLGYCYN
GQCPQRPDQC VKMYGSGAVE ARASCYDQNK RGVYYGFCRR PSKEQYIPCQ QQDVFCGKLF
CHNGNENPNY GRMVRVGDCK AAFFEDYTKD YGQVDTGTRC GDGKVCSQNQ CVTLETAYRN
INCSAKCPGH AVCNHRSECQ CEPGWMPPYC DSKDGSFSSL SMGATVAVTV TVILVLLGAI
AAAVGIIWKK RQSPLLPTTQ TQRKPVVSSC ARHLNKVPNQ PRPVRQARRP KPKGAPPPPP
PAGNRPKPPS QNYIAARQAL RPVPPPKV
//
