ID A0A096MGM6_POEFO Unreviewed; 818 AA.
AC A0A096MGM6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=ADAM metallopeptidase domain 9 {ECO:0000313|Ensembl:ENSPFOP00000030567.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000030567.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000030567.1}
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:PRU00076}.
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DR EMBL; AYCK01021171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01021172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01021173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01021174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096MGM6; -.
DR Ensembl; ENSPFOT00000022623.1; ENSPFOP00000030567.1; ENSPFOG00000010000.2.
DR GeneTree; ENSGT00940000156239; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000028760};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..818
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001927943"
FT TRANSMEM 696..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..402
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 410..498
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 637..671
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 728..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..818
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 361..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 661..670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 818 AA; 88817 MW; D8D1EA5CB75CE3AA CRC64;
MGGRGGAALL ELCGILLLLT GSCHCRDSQQ TEHLASYQLT APRPIGGRLR RDAEGRPPNQ
QVSFIIPVDG NDLLVHLQRN EVLLPPDFTV FTYGPNGSLI TSRPPVQNHC QYQGFVQDME
GSAVAMSVCS GLRGVMHLTN DSYGIEPLGS APEQHLLYRL QDVTSQPRGC GTPHYGHGDA
AEHAQYDPEE IQHRRRSRVK RAVLHKTHYV ELLLVVDNDR FKHMNGNETA VREQMIHLAN
LIDGIYMQLN VRVVLVGLDI WTKQNLINTE GGAGEVLSRF TQWREKELVP RRRHDSAQLI
LMKSFGVTAG MAFVSTVCSR SHGGGINAFL NNNVAAFASI VAHELGHNLG MNHDDGRTCS
CPAAACIMHS GATGSKNFSS CSADDFEKMI LSTGGTCLLN VPRPDEAYSA PYCGNRLVDV
GEECDCGSEK ECEEDPCCEY RTCKLRPGAQ CASGECCSGC QFLPGGTVCR SKKDQECDLP
EYCNGSTSFC QSDVFVQNGH PCRNQQAYCY NGRCQHLDGQ CQALFGPKAT AAPDICFKDV
NSKGDRFGNC GYQHSGYKKC ESRNAQCGKL QCLNVKGGTV FGILPSIITT PIHGATCFGV
DFMLGSDVPD PGMVNEGTKC GDNKVCMNFE CRSADVLSYD CDVETKCHGH GVCNSNRNCH
CDYGWSPPSC KLSGYGGSVD SGPTWNDKDT SLRDGLLVFF FLVLPLLALA AFVFLRRNEL
LRRLGLSRRK RSQGYQADGA TSTKPTNPGR APPPRAQPPP AGRGTANFIV RDGVVETSET
SERAPPFAAR PPPPPLKPKP SAASQPLVPQ RPAPAPPV
//
