ID M3XNZ0_MUSPF Unreviewed; 992 AA.
AC M3XNZ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LVRN {ECO:0000313|Ensembl:ENSMPUP00000000790.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000790.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000790.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AEYP01047974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004759129.1; XM_004759072.2.
DR RefSeq; XP_012915179.1; XM_013059725.1.
DR AlphaFoldDB; M3XNZ0; -.
DR STRING; 9669.ENSMPUP00000000790; -.
DR MEROPS; M01.026; -.
DR Ensembl; ENSMPUT00000000805.1; ENSMPUP00000000790.1; ENSMPUG00000000793.1.
DR GeneID; 101674251; -.
DR KEGG; mpuf:101674251; -.
DR CTD; 206338; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000160535; -.
DR HOGENOM; CLU_003705_2_0_1; -.
DR InParanoid; M3XNZ0; -.
DR OMA; YLEAFSY; -.
DR OrthoDB; 3085317at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 104..308
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 344..572
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 649..971
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 46..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 505
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 992 AA; 112848 MW; BD2B27D6109E4F69 CRC64;
MGPPSSSGFY VSRAVALLLA GLAAAFLLAL AALAALYGRC ARVPPSDLPH RAGPDTAPSP
PGTPEEPLPP GRTRPTREPV VTATTGHGRP PGPWDQLRLP PWLVPLHYEL ELWPRLRPQE
SWAPTLTFTG RVNITVRCTA ATRRLLLHSL FLDCESAEVR GPLASDAGDG TVGRVPVDDV
WFAFDMQYMV LELGGPLQPG GRYELQLSFS GLVYQDLREG LFFSVYTDQG ERRALLASQM
EPTFARSVFP CFDEPALKAT FNVTIIHDPS YVALSNMPKL GQSVRRDTNG SVWTVSTFST
TPHMPTYLVA LAVCDYAYVD RSERGKEIRI WARKDAIENG NADFALNITG PIFSFLEDLF
NISYPLPKTD IIALPTFDNS AMENWGLLIF DESLLLMPLN DQVTDKKAVI SFILSHEIGH
QWFGNLVTMN WWNDVWLKEG FASYFEFGVI NYFNPKFPRN EIFFSNILRN VLSEDHVLVS
RAVSLKAENF TETSEINELF DLFTYNKGAS LARMLSSFLN ENLFINALKS YLKTFSYSNA
EQDDLWRHFQ MVIDDQNKTL LPATVKSIMD SWTHQSGFPV ITLNVSTGTV KQEPFYLGKV
KNETLLPHND TWIVPILWIK NGITQSLVWL DKSSKIFPEM QVSASNHDWV ILNLNMTGYY
RVNYDQLGWK KLNQQLEKDP KAIPVIHRLQ VIDDAFSLSK NNYIEIETAL DLTKYLAEED
EIIVWYAVLV NLVTKDLVFD ANSYDMYPLL KKYLLKRLTS IWNVYSTIIR ENATVLQDDY
LALVALEKLF ETACWLGLED CLQLSRELFK NWTNQPENEI PSPIKSVILC YGIALGSEEE
WDFLLNMYAN KTKEEERIQL AYAMSCSRDP RILNRYLEYA ITASPFAFNE TNVIEVVAAA
EVGRYIAKDF LVNNWQAVSE RYGTQSLVTL MNIIGRTIST DLQITELQQF FGNMLEEHQR
LTVHAKLQTI KNKNLENKRR SARMTAWLRR NA
//
