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Database: UniProt
Entry: A0A182PPW9_9DIPT
LinkDB: A0A182PPW9_9DIPT
Original site: A0A182PPW9_9DIPT 
ID   A0A182PPW9_9DIPT        Unreviewed;       795 AA.
AC   A0A182PPW9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AEPI008999-PA};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI008999-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
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 epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI008999-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI008999-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A182PPW9; -.
DR   STRING; 199890.A0A182PPW9; -.
DR   EnsemblMetazoa; AEPI008999-RA; AEPI008999-PA; AEPI008999.
DR   VEuPathDB; VectorBase:AEPI008999; -.
DR   OrthoDB; 5406290at2759; -.
DR   Proteomes; UP000075885; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF237; MIND-MELD, ISOFORM J; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00023049}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..795
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008131776"
FT   DOMAIN          272..476
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          486..574
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          727..764
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          92..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        546..566
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        754..763
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   795 AA;  88047 MW;  3E5B38C2DD826698 CRC64;
     MKLMSPLRAL LLALVMTLAE SAGEADYTLD DSFWNEESPV GEVERLLKEH QQNQELVDKI
     GSSYYQIIYP VQLRHHEKMG ISTREVNQPK FPQRGYDGSY SGSGGGRGRS RTGKHFHRTS
     LLIKAFNHKF RLDLELNTQL LAPNIVQKHY LPSGFAQDSH REIEHCYYHG TVKDYPGASA
     AFHTCNGVSG VIHVGNETFV IHPFYGGDLS QKHPHVIFEA RTKSNKGCAN SGNLEWRTRS
     IRRGSSHHAG LAELIDRNGA GRYRRDVRET TKYIETALII DKAMFQKRNG STRTEVVHDA
     IQVANIADLY FRTLNTRVSV VYIETWQGQN QAQIDGGKDI SKAISNFNDY TSRNLYKIDK
     DTTQLLTGET FAGGEVGMSV PETVCTPKAV GISVDMNPYE PHLLAGTMAH MIGHNIGMGH
     DDNRDECICR DWHGCIMSQS IVGLENVQPY KFSECSRQDY NDALRIGHGL CLLNKPNEVR
     IMVELRKNCG NGIVEDDEEC DCGSALDCDK TDPCCDGITC KLKKESQCAT GPCCDKCILK
     PPGVICRDAH NECDLPEYCN GESGQCPPDV HKKNGNPCGM NSTGFSTGYC FNGVCPTQAA
     QCERIWGYSG TGADRVCYEQ FNSKGSINGH CGKDSNGNYI KCEPENIQCG SLQCKDGDRT
     PVEDCSEHLY SRAIISIRGT EYECKSITGT STNSNTPPFG LVRDGTPCGD NLICVNQTCV
     SIFPYIDQTK CPTNHNNLEC FGNGDCTNNN KCFCKFGWTG PDCSIQAHIT TTYPAPVTSA
     TSETTIIMEK KTTRY
//
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