ID A0A493TUN0_ANAPP Unreviewed; 983 AA.
AC A0A493TUN0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LVRN {ECO:0000313|Ensembl:ENSAPLP00000029603.1};
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:ENSAPLP00000029603.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000029603.1, 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:ENSAPLP00000029603.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; A0A493TUN0; -.
DR STRING; 8840.ENSAPLP00000029603; -.
DR Ensembl; ENSAPLT00000019786.1; ENSAPLP00000029603.1; ENSAPLG00000013734.2.
DR GeneTree; ENSGT00940000160535; -.
DR Proteomes; UP000016666; Chromosome Z.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF31; AMINOPEPTIDASE Q; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 81..286
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 322..550
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 627..926
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 483
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 983 AA; 111971 MW; AF3EBEE26774FE32 CRC64;
MGARGGSGLY VGRRAAALVA AVLLALLAAL LALAALYGRC RGEEAPPAPP KSPDGAAGGA
GVPGGPPGVP SWRRLPRHLL PLHYDLELWP RVRPGQAGPF SFVGQVNITV RCRQDTRAAV
LHSAGLRIRG AAVRGPLPEP GDAVWGSLPN PGVVVEVPEL QEAAGEVAVL ELRGRLQAGR
RYVLQLGFQG RLEEDLDGLF LTRYTDQGRS SMLIASQLEP TYARTVYPCF DEPAMKATFN
IRIIHDPSYV ALSNMPAIDT SEMKDENGSL WTVTTFKTSL KMSTYITAFV ICDFDYVTRT
ERGNEIRIWA RKEAIKNGYV DYALNITGPI FSFLEDLLNI SYPLPKTDLV ALPDFGAGAM
ENWGLMTFQE SSLMYLPSDK FTSRKAMIAI IVSHELGHQW FGNLVTMKWW NDLWLNEGLA
SYFEYLGATF VEPRLSLDKI FYDHVVQPVL REDNEVGVRS LSQNEDKIKG SFSLISLFDS
ITYNKGASIT WMLSGFLTEK LFIKALNLYL KEFSFSNANQ DDLWTHIQMV VDAQDEVHLP
ASVKKIMDSW TCQNGFPVLT LNITTGTISQ EQFLNKKNEN TSTDSYNNTW IVPISWMRNG
SSQPLIWLDK SSKFFPEMQV SESEYDWILL NVNLSGYYRV NYDQLNLKRL VHLLENDPKA
IPAVSRFQLL DDVFALTQFG YIQIETALEL TKYLAREDEL FIWNVVLLNL VPENLESTLK
NYEVYPLLKK YLLKRMLPIY HYYAGFIRQN VDALEHDYFA KVYLEKLFAT ACWLGLQDCL
DLSYELYTKW MDNPQYKIPF LIRRTVSCYG VALGSDKEWN FAWEMYNHTD STKEDKDILL
SAMSCAKESW LLHRYLQYGL SDTLFSSNCT SIIISYVVTK DIGHRIAWDF VTENWPLLNE
RYGKELLHDV LKVMGRFVNT DVQIQESICL DSFPRYSLFF LKNSIFVLSA CDQHTCVSPE
LQFRKHIFFC NDRFSRIMCF FSH
//
