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Database: UniProt
Entry: W5JIV1_ANODA
LinkDB: W5JIV1_ANODA
Original site: W5JIV1_ANODA 
ID   W5JIV1_ANODA            Unreviewed;      1097 AA.
AC   W5JIV1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Alanyl aminopeptidase {ECO:0000313|EMBL:ETN62815.1};
GN   ORFNames=AND_005486 {ECO:0000313|EMBL:ETN62815.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN62815.1};
RN   [1] {ECO:0000313|EMBL:ETN62815.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN62815.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN62815.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC005486-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; ADMH02001370; ETN62815.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5JIV1; -.
DR   STRING; 43151.W5JIV1; -.
DR   EnsemblMetazoa; ADAC005486-RA; ADAC005486-PA; ADAC005486.
DR   VEuPathDB; VectorBase:ADAC005486; -.
DR   VEuPathDB; VectorBase:ADAR2_006157; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_2_2_1; -.
DR   OMA; SKIWRRE; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF302; AMINOPEPTIDASE N-LIKE PROTEIN; 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   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:0000313|EMBL:ETN62815.1};
KW   Hydrolase {ECO:0000313|EMBL:ETN62815.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:ETN62815.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..283
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          422..634
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          757..1072
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  123061 MW;  5FF116B88A946F46 CRC64;
     MTEPDSDDDA FLTGGDSSSR PVRDGVAVCS QKRALLVTAI VLGTLLATAL VIAYAGPQTV
     CPCAGKIPPG YVPDGYNSSE PFQPIATNGQ PFPWLLPTLP NNVKPNRYIL TIHPNLTTLD
     VKGQVSIELY VEKETNFVVL HAQDLNITEK ALVGPKGFAL KILRMLEYTP RQQLYIETRE
     KLRKKANYTL SIRWHSKMIL DQFEGDFDMK KTLAATVLKP GSTRKAFPCF DEPHLRAAFK
     ISLFRDRFHI GLSNSIVQDT DDVGFYMGTG LLRDDFAETP PLPPDSVSWV ISDFKRELLE
     PSSKYQRVNA SKATDGTAIT KPNVPAAVPK VASKSEKKPF RNLTAVLLSK NLFKLTNNLP
     TKEPAAEEIN VVTTHPIDSS TASLLGDERE MMWAGETSLI RTAPAYSFYA PETHIAKGTF
     ILHTSRDILE YLQQWLSVAY PLSKLDFVAL PSLLDDLSSS LGLIVCRTSF LNEPNSISAK
     EYHMSVVKIS EGIVKQYFGG LISPKAWKHK WLWEGLIRYL SRFLLSTIQP LWPMKELFLI
     DTLTKALDID ALQGWDSISA GASDTGDNDP FFVDKSASLL SMLQSAIGER NFRQCLGKFL
     RTYQFQTAEP ADLWVLCAKQ VNNSRYIKEM MIQWTNAAAF PLLNVTLNGT SLTVHQTDFR
     PAEYLAIYDE PIEEIEGDDT PGGRSTTTST TTTTTIAPTG DTKAGSRWIF PIHYTTDVLN
     GNGTTPEDME QHEQQPSLSV WLNSSEAVIT LNHSPEWVKL NYGQTGYYRV LYDETNLNKL
     VNQLHTNNEV FSTQDRVGLV SDIFTLCHAN LIPCHAAMEL ISYFPKEKEW GPIALGTNHL
     EKWRKILKYS ECYLVLAEYV RQNLAKSIQT IGWEDAGEEE IKLLRPVLML SATLWEESDT
     IKFAKSLVSN FTANSVPIPP NLRSVAYIGS VLSGEFQYWQ FCWDRYMAVR RERSSVLEER
     MELLRALGVT KDAWLQNRLL SHVITLPVFE IVQVLDAIAG TPTGGAMACR FLQAKWFDFQ
     SKLGRGTVQF ARVISAITQY GSTKFDYDEL KSLVNRFGDG PGLKLLNMTL STVAANVEWV
     SRSQASIYSW IENKYHF
//
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