ID A0A3Q0S9P6_AMPCI Unreviewed; 424 AA.
AC A0A3Q0S9P6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ADAM metallopeptidase domain 19b {ECO:0000313|Ensembl:ENSACIP00000021509.1};
GN Name=ADAM19 {ECO:0000313|Ensembl:ENSACIP00000021509.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000021509.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000021509.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3Q0S9P6; -.
DR Ensembl; ENSACIT00000022066.1; ENSACIP00000021509.1; ENSACIG00000016009.1.
DR GeneTree; ENSGT00940000159624; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; 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:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 28..183
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 196..282
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 254..274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 424 AA; 46421 MW; 1EF978B829F4BD1A CRC64;
MFCVHCGLCW LQYENHGADL EKTKQKLYYK ALNIRVALIG LEVWTSRDMI SVSENPHSTL
AAFLSWRQKQ LRSLPNDNAQ LITSVSLIHS HISHLSCHLS HVWTPVTLVD FVVIVQGNTQ
HWLYPIGVAA TVAHEMGHNF GMSHDIPGYC HASAEDGGCI MAAATGYKIQ LANIKETAFR
GKCLFNLPNT RTMYGGHRCG NGYLEDGEEC DCGDEEECTS PCCNANNCTL KTGAECAHGV
CCHNCKLKSP GVLCRGPSGS CDLPEYCDGK TESCPADFYL VDGTSCAGGR AYCYTGMCLT
LEQQCRSLWG QGGVSFFLNS LHDRDAKCGK IQCSSAASKP IENNAVSIET TVKEGNSKIT
CRGTHVYKLG KEDEEPQGDT LDPGLVMTGT KCGEDSVRLV KMYQTEFPVV VRSAHCCHLK
SLWM
//
