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Database: UniProt
Entry: A0A182MGC2_9DIPT
LinkDB: A0A182MGC2_9DIPT
Original site: A0A182MGC2_9DIPT 
ID   A0A182MGC2_9DIPT        Unreviewed;      1762 AA.
AC   A0A182MGC2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Protein eyes shut {ECO:0008006|Google:ProtNLM};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA017639-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
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 culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA017639-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA017639-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   EMBL; AXCM01000141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 139723.A0A182MGC2; -.
DR   EnsemblMetazoa; ACUA017639-RA; ACUA017639-PA; ACUA017639.
DR   VEuPathDB; VectorBase:ACUA017639; -.
DR   OrthoDB; 101939at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 7.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.200; -; 4.
DR   Gene3D; 2.10.25.10; Laminin; 13.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 6.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 3.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00179; EGF_CA; 12.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 8.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; 13.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 13.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
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}.
FT   DOMAIN          6..42
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          44..80
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          82..118
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          120..158
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          160..196
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          198..234
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          236..275
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          570..606
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          624..832
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          882..919
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          926..1114
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1115..1151
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1153..1191
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1271..1456
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1452..1489
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1490..1523
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1529..1748
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          352..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        10..20
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        32..41
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        70..79
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        108..117
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        148..157
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        186..195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        224..233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        265..274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        596..605
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        909..918
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1141..1150
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1181..1190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1479..1488
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1513..1522
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1762 AA;  192756 MW;  FABE6D526FA0DF35 CRC64;
     MHLTEAGFAC LSNPCVYGVC IDDLNSTYSC YCIDGYTGVH CQTNWDECWS NPCLNGGICI
     DGVASYNCTC PDGFLGLNCE ENFNECQSNP CQNGGLCHDK DNAFYCTCAL GYEGEFCELD
     IAVCDTGDRC HNGAACIEGP GLEFSCRCTE GYEGRLCDAE INECASAPCQ NGAICIDKFA
     SYICACPMGF GGMNCEEEIL VCASSPCANQ ALCLMEEDSP TCYCVPDFHG ERCELQYDEC
     QLGPEPRCVN GATCVDGVDE YFCTCAPNFT GENCECLILD DDGQIEMDCN YTAPIASTSG
     DMTDSSFFTS TMESFPFSTD GIWKATDASL ERTTSYSLFT YTAGPTVVSE FTDPSVERPY
     NGTSVQVSPN YSASDSGSDQ YSTTSLSESV TDGATVSRGT VPPDQEKDTK STVESGDTTP
     PDTMSENVPT VSGVEDKPSS VPDITHDGTL TDVSSTDYTT VKSSSKQPSI DYGSGSSVSE
     FPTTPMDALL TTSDHPSVST LTPELSSFFT ESPTNRSVPT FHGEDQVTDT PSFTTAPTLF
     TSPDATTRSS FGTTSGASIV PPLTTRSPEV IQQCDDTVCA NGGTCAMTPN GIRCHCDFRY
     AGPFCDMPVS IQNAAFSKES FLRHIIYRRN SSSDPSIQSV DTLKQLASMS VRFKAKLTSR
     EGLIVLATAE GDDGNHYVAL FLHKGLLQFQ FSCGLQTMLL SEIEGTVNNG YELNVKVQLN
     FNDRYSHCNA SLHVNETLAM SGEQPTWLGN VLRTRPQKEG SDGVAALASI KQSWLHLGGR
     PIKTMYTLSH NISRYHGFTG CVYDLEINGA PVAIFDNAED AYKIYECTSL ACLSSPCRNG
     AICVEADGYG LAGRYSPSVT QPDTVSAWSC KCAFGYMGKT CERSVCDNNP CRFGGTCVTF
     PESGYLCLCP YGKHGHFCEH DLDILQPSFF GSIKGISSYV AYPIAFPVED RFEFSFKIIP
     TTTAQISLLA FIGQPYDHHD QSDHFSVSFI QGFILVTWNL GSGPRRIFTQ QPIQVQSSRP
     TTIHAGRNGR TAWLSIDGKV NISGNSPGNS RKLNVSPQLF IGGHEGVNFS SLPHDLPLHS
     GFQGCLFDIR LVAGPIHIPL QHIGGMRGRS VGQCGTKECH RHACQNNGAC LQHGSTFTCI
     CQEDWNGILC SQKVNPCDES VSKCASDSTC FPLVSGYECD CPYGKVGKRC ESNLKYLSDV
     SFSGRRSYVA LRWPNVGTGD WIAAYRENEV RYEKIVQHSH IIPHNHSILL KSIRELDKIN
     DVLKVLPEAN DTELYAGHSV IPRSENYRQL RVRQLTIELQ VRPLSEKGLI LFIRTFDSNA
     QEQGFISISL QGGVVEYRIS SARTQTAVVR SNHVLATGEW HFIRIVKYGK RLTLWVEGKS
     TSIIGSVREE YVSLTKKLYL GGLPDLSTLP YDAISGYPVP FRGCIRHVNL NGTRITLNDS
     SIVASRNIND CDGTPCGGDI CAHGGLCWLD EHSQPRCKCP EYSKGANCEI QESCEVVQCR
     NNGQCLKNGR CSCGVGWTGH YCEIATTKYS SLGFNDRSYI LIPSQKIKMK DKRNDDSTSM
     AGKLPFGLQI SFNISTLEDG MLAWTTDETG RYFGIGIRDG FLVVVSNMLK EDPTNVASGA
     TGPWKAFVAD GDWHNVLLET KSHQLRLFVD GYELLAGTLI PNSRSQAYDR PVLSEEITYL
     GGFPDANVYN RTMGNFATSF NGCIQHILLG NQLDELDYVD YDGANINESQ TRIRFVSIVI
     PLNDDPFCST NYKKEEMIFE SF
//
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