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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//