ID A0A3Q1BFP3_AMPOC Unreviewed; 678 AA.
AC A0A3Q1BFP3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12-like {ECO:0000313|Ensembl:ENSAOCP00000012343.1};
GN Name=ADAM12 {ECO:0000313|Ensembl:ENSAOCP00000012343.1};
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:ENSAOCP00000012343.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000012343.1}
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; A0A3Q1BFP3; -.
DR Ensembl; ENSAOCT00000020020.1; ENSAOCP00000012343.1; ENSAOCG00000001941.1.
DR GeneTree; ENSGT00940000155495; -.
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; 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:SF112; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 12; 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; PS50214; DISINTEGRIN_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 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 TRANSMEM 541..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..254
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 262..348
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 494..526
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 320..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 498..508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 516..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 678 AA; 73429 MW; E3E25FECAF0BC21D CRC64;
IALENKTFII EPMSGRDTGA HSIYRVEELR LTPGACGHGF NMSSVAPENH IKSPFQSFHT
RVRRFQKQGK DLEKVKQRLA EIANYVDKFY RALNIRVALV GLEVWSDSDK CPVTQDPFTT
LHEFLDWRKV KLLPQKPHDN AQLISGVYFQ GTTIGMAPIM SMCTVEQSGG IVMDHSENPL
GAAVTLAHEL GHNFGMNHDT PERGCGCRMT VDRGGCIMTP STGYPFPTVF STCSKKDLAA
SLEKGVGMCL YNMPEVKVLY GGQKCGNGYV EEGEECDCGE PEECMNPCCN ATTCTLKGDA
VCAHGQCCED CRRKPAGTLC RESSNSCDLP EFCTGASPHC PANVYLHDGH ACHNVEGYCY
NGICQTHEQQ CITLWGPGAK PAPGICFERV NSAGDPYGNC GKDSKGSFAK CDARDAKCGK
IQCQGGSNRP VIGTNAVSIE TNIPLQEGGR ILCRGTHVYL GDDMPDPGLV LAGTKCGDSM
VCLNRQCQNV SVFGVHECSG KCNGRGVCNN KKNCHCEAHW APPFCEKSGF GGSIDSGPMR
LAGILVTLVS LLVASIVIFL KRKTLLRLFF TNRKSTLEKL SACFEVLNGL APSYLSKEGS
DEGRKEVMKE GFILICPSSH NSADFLSGVN IPKMSNGQRA PSGLSPCTDQ HQDANLHPNP
LEPACTRLVT PQCVCCCI
//
