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Database: UniProt
Entry: A0A182VAQ1_ANOME
LinkDB: A0A182VAQ1_ANOME
Original site: A0A182VAQ1_ANOME 
ID   A0A182VAQ1_ANOME        Unreviewed;      1087 AA.
AC   A0A182VAQ1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EnsemblMetazoa:AMEM011746-PA};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM011746-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM011746-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM011746-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A182VAQ1; -.
DR   STRING; 30066.A0A182VAQ1; -.
DR   EnsemblMetazoa; AMEM011746-RA; AMEM011746-PA; AMEM011746.
DR   VEuPathDB; VectorBase:AMEM011746; -.
DR   VEuPathDB; VectorBase:AMEM21_010385; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF294; AMINOPEPTIDASE; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          165..383
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          413..654
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          743..1065
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   REGION          76..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        486
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         485
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         508
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            571
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1087 AA;  123993 MW;  A780B87F78DFB002 CRC64;
     MNNNSNKMQI RESLAMDVDG TTVESSRGYL ITRMTLLATV AIFGCLLLGS GLLIYHFASC
     DEHHASTLHH TTLCEHQHST SHHHQQHAPA PSSDGSASST TQKTLIEAST SRENPGETIP
     AGDNVPGDTG ATGADGMDQG GQRAEDGTVA SSVREDLRLP RSIEPVAYDI RLIPWLVEDN
     FTFLGTVEVL VNVLEDCSNV TLHVAALNIH SASVERSTGR GEKQHSEEAT ADESSEGAPL
     VREMVEIDHN LTVASKQFYV LMLKTPLRRG EQYVVRLRYD GVLNDYLQGF YRSSYTANNE
     TRWIATTQFQ PTDARRAFPC FDEPALKARF NISIARTRDM ISLSNMPRLR SYEARTIDTF
     SEPELQGYVW DVYQQSVPMS TYLVAFVVCD YLNLTSGNFA VWARADAIGS ARYALSVGPK
     LLKFLEDFFH IKYPLPKVDM IALPDFSAGA MENWGLITYR ETAMLYEENV SAISNKQHVI
     TVVAHELAHQ WFGNLVTPSW WTDLWLNEGF ASYMEYLGVD AVEPAWKSME QFVVNELHNV
     FSLDALSSSH QISVEVHNPE EIHEIFDKIS YGKGATIIRM MDHFLTTEVF KRGLTNYLND
     KQVSGGSLCM ACSMLNVKYQ SASQDDLWDY LTNEARRGGI FDEHTSVKEI MDTWTLQTGF
     PVVFVQRDYE SDSIEFRQER FSFANALNGT DAAARQSERF LWWIPITYTT LGDSNFQQTK
     PSIWMKAEEA LVINNHDIPS HDWMIVNVQQ TGYYRVNYDE RNWQMIVRHL QDRNKYKTIA
     ASNRAQLIDD ALNLARAGYL DYGVALNVTR YLVHETDYVP WKAAIAALNY IDSMFIRTRN
     YGLFKKYSMD LLENIYREVG FEDHRDSPLL TVYKRISVLK AVCHLGNKDC VNHCLRKYYE
     WMHQPNPDIN NPISPNLKST VYCTAIKYGD ETEWDFAWER FQKATVASEK EILLSAMGCS
     RVPWILARYL ENAMSDEYGI RKQDAFRVFI SVADNVIGQP IAFDYMRNNW AKMKSYFGAS
     MSNLNIILKY CTKRFNTESE LLELKEFAEI HLKDSGRTIQ QAIEWTESNI AWLNRNAQPI
     VNWLNEV
//
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