ID A0A3Q1BC17_AMPOC Unreviewed; 734 AA.
AC A0A3Q1BC17;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19-like {ECO:0000313|Ensembl:ENSAOCP00000011595.1};
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:ENSAOCP00000011595.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000011595.1}
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; A0A3Q1BC17; -.
DR Ensembl; ENSAOCT00000019046.1; ENSAOCP00000011595.1; ENSAOCG00000015919.1.
DR GeneTree; ENSGT00940000158971; -.
DR OMA; MGAQCAH; -.
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:SF38; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 33; 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; 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..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..734
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018638054"
FT TRANSMEM 659..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..366
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 374..460
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 608..640
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 DISULFID 432..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 612..622
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 630..639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 734 AA; 80481 MW; 505095C632A2B74B CRC64;
MYSKHRQKNG QISPAKCGRL LVFLSFLLLN GTLGRARGDT GEQELHRGRT VTAQWLSQGR
TKRDAETATQ EECPVRGDIG LSSSDLQLVL QVERNQGLIS LNSSDTYYLE PISGVDPAHH
SLLSAEELPV EGGNCGHSHR STQFNHISNL LRPFHSRVKR NTWGTTKYME LYIVADNTLF
KRQNKDYEKT KARIMEIANY VDKFYRALNI RVPLIGLEVW TDRDQCIITE EPNATLWSFL
QWRQKLKSRK KHDNAQLLTG VIFKGTTIGM APLEGMCSLE NSGGINVDHS ELSIGAAATM
AHEIGHNFGM SHDHDGCCVE ATAEQGGCVM AAATGHPFPR VFSRCSKRDL DSYFQKGGGM
CLYNMPNMKD LVGGKKCGNG FVEDGEECDC GEPDECTNDC CNANNCTLKE EAQCAHGVCC
EGCKLKQAGT MCRGPAGACD LPEYCTGASP YCPANVYLLD GSSCQYGLAY CYNGMCLTHE
QQCLQLWGYG ARPAHDACFE DVNAAGNAFG NCGKDEHGNY MKCEKSDAKC GKIQCHSAAK
KPKGTNAVSI DTTIKTGGIE VKCRGTYVYS TQDGQGDLPD PGLVMTGTKC GEGKVCRDRR
CQNASFTELE TCIARCHSNG VCNSNGNCHC NRGYAPPFCE KPGLGGSVDS GPVQYDSQVG
LVVGLLFAFL VVLPTVLLLF YCYRVKTSYY HKWLSQREKN KSNKYCVLSV CLSVCLSVCL
SDNNTIHSFL GLLY
//