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Database: UniProt
Entry: A0A493U2N7_ANAPP
LinkDB: A0A493U2N7_ANAPP
Original site: A0A493U2N7_ANAPP 
ID   A0A493U2N7_ANAPP        Unreviewed;       273 AA.
AC   A0A493U2N7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000032309.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000032309.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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DR   AlphaFoldDB; A0A493U2N7; -.
DR   STRING; 8840.ENSAPLP00000032309; -.
DR   Ensembl; ENSAPLT00000047553.1; ENSAPLP00000032309.1; ENSAPLG00000029058.1.
DR   GeneTree; ENSGT00940000157176; -.
DR   Proteomes; UP000016666; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127:SF863; BONE MORPHOGENETIC PROTEIN 1; 1.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          108..273
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   REGION          84..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        170..192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        172..173
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   273 AA;  30037 MW;  4086B1F647429EBF CRC64;
     PEGVPGGVRA RRPLLLPRPR RVLLLAAGAA GLARGSEGEA RGAFLTYLTA PPTAFLGDIA
     LDEEDLRLFQ VERVVDLAHR TITRLPTNSS GSPQARSRGR QRARSRRAAT SRPERVWPDG
     VIPYVISGNF SGSQRAIFRQ AMRHWEKHTC VTFLERNDED SYIVFTYRPC GCCSYVGRRG
     GGPQAISIGK NCDKFGIVVH ELGHVIGFWH EHTRPDRDDH VSIVRENIQP GREQPSSSSS
     SSFSSPGGLL IPPPPLPALS PQGHFPRHHP AQI
//
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