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Database: UniProt
Entry: A0A182I0G1_ANOAR
LinkDB: A0A182I0G1_ANOAR
Original site: A0A182I0G1_ANOAR 
ID   A0A182I0G1_ANOAR        Unreviewed;      1243 AA.
AC   A0A182I0G1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AARA007043-PA.2};
OS   Anopheles arabiensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7173 {ECO:0000313|EnsemblMetazoa:AARA007043-PA.2, ECO:0000313|Proteomes:UP000075840};
RN   [1] {ECO:0000313|Proteomes:UP000075840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dongola {ECO:0000313|Proteomes:UP000075840};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   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 arabiensis DONG5_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AARA007043-PA.2}
RP   IDENTIFICATION.
RC   STRAIN=Dongola {ECO:0000313|EnsemblMetazoa:AARA007043-PA.2};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) 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   EMBL; APCN01002074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; APCN01002075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182I0G1; -.
DR   EnsemblMetazoa; AARA007043-RA; AARA007043-PA; AARA007043.
DR   VEuPathDB; VectorBase:AARA007043; -.
DR   VEuPathDB; VectorBase:AARA21_002678; -.
DR   VEuPathDB; VectorBase:AARA21_004509; -.
DR   Proteomes; UP000075840; 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; 2.
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:SF290; 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; 2.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
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};
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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          64..257
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          358..553
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          584..812
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          892..1197
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        658
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         657
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         661
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         680
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            743
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1243 AA;  139142 MW;  6128A1987D0FA208 CRC64;
     MVLHLGKNIV LLLLVVSSST LAVFGQRSAA HPEWNNREFA PAPDTSSPRD DSIDQSYRLP
     TDTVPTHYTI RLHTDLHTGS RAFSGIVDIE FDVIVPTDAI VVHNRDLLIA SAALYAKDQD
     GLLVEFGFPH HEFDQRTEQL TFHPGQVLPI GSYVLTVEYS GLLQTSSNSG FFLKSYVNDD
     GERRYVGTTQ FESTNARMAF PCYDEPLLKA GFTLWITHIA EYNAVSNMPV EEVVPSEEHE
     GYVTTKFGPT PKMSSYLLAF GVSDFVSIED GTQQCLTHHR PRQGSRMVAR TVLITALLCL
     LASPTTFATR PAWQWLSEPS DFTLSFEREL SDLAGSLPVP NRRQAVDESY RLPNNTSPIH
     YHLALRTAIH ENSRQFSGTV KVLFEVLEPT TTVTLHNRRL TVQRAFLHEE AVGGGAGAQI
     EQVAHSTDPD TEHLTLAVSQ LLPAGSRYYL RVEFEGALQN NNNMGFFASS YLDNNGNRRY
     LASSKFEPTH ARSAFPCYDE PLLKASFELE LTHYKEYNAV ANMPLAGAPT PDPDNADYVT
     SRFEVTPLMS TYLLAFAVTD FTIRTADRQT VYARPNVFEE TAFPLEAGNR ILDALSDYMD
     ISYYDYMPKM TQIAIPDRGT GAMENWGLVA YGEPVLLFNP AINTYRNRKS VTTIIAHEYA
     HQWFGNLVSP HWWEYIWLNE GFATLYEYYA AQLAYPEGEY WELFTVEVIH SAFGADASET
     VRPMNWNAAS PSEIAALFDT VAYDKSGSVL NMFRAVLGDP VWRYGLKTYM TARQLDGATA
     DHLYGGLQEA LVSLAPTLLP ATVTVRQLMD SWTSEPGFPV LTVYRTYGEQ QEAILSQERF
     LSSKRLPSGH VYYVPYDFTG GHAPDFEPTP AGYGWLAAKA DKIATGVPND QWIIFNRQQN
     GYYRVNYDAH NWELLIEALH NDPAQIHHRN RAQLVNDAYN LARAEWLDFA VPLRLMSYLR
     RETQYAPWTA AGSALTYLYN KLRGTAHYAH FQVYANHLLL DIYPTLAIDS VAAQETLLQL
     YLKQFINTWA CRVGHGDCLA KTKQALAAAY QARTPVHPDI ATAVYCNGLV DASDEIFVWV
     YEQFKSSRNQ AHRTVLIDAL ACSRQPAQLE SFLTTALGSG AEFDALLATE RTRIVSAVYG
     ASREGVDAVL DFLMVPSRVT EFVQRLGQSA LNSAVSNIAS RTNNQPELDR LNALLVSLGS
     QIPESVATSA RSTVQNNFNW FNTLEGLVVV EFLEQMATTP QEL
//
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