ID A0A158NDG6_ATTCE Unreviewed; 1057 AA.
AC A0A158NDG6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein eyes shut {ECO:0008006|Google:ProtNLM};
GN Name=105618657 {ECO:0000313|EnsemblMetazoa:XP_012055574.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055574.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012055574.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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; ADTU01012512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01012513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012055574.1; XM_012200184.1.
DR AlphaFoldDB; A0A158NDG6; -.
DR STRING; 12957.A0A158NDG6; -.
DR EnsemblMetazoa; XM_012200184.1; XP_012055574.1; LOC105618657.
DR GeneID; 105618657; -.
DR KEGG; acep:105618657; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR InParanoid; A0A158NDG6; -.
DR OrthoDB; 101939at2759; -.
DR Proteomes; UP000005205; 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:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 7.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 8.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..19
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 21..57
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 59..94
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 96..133
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 135..171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 173..209
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 211..249
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 575..762
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 758..791
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 794..831
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 841..1038
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1034..1057
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 9..18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 47..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 84..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 123..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 161..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 199..208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 239..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 821..830
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1057 AA; 115456 MW; 63CA7498C36A916B CRC64;
MGSTYSCYCI DGYTGINCEI NWDECWSDPC LNGGTCNDGV AAYNCTCPDG FVGINCEQRY
SECSNHPCLN NGTCVDYDGI TCQCLDGYSG EYCEIDASVC NETMCKNSGE CIEGPGFSFY
CRCREGWTGI LCEVDVDECL ASPCRNGGLC INIPSSYTCA CLFGFTGKDC DKAIVPCKEN
PCQNGAVCLL EDDRSVCYCV PDYHGVFCEL RYDDCESKFA QCDNGGTCID GINSFICACP
SNYGGPMCEY SFPSTTTLEM EDTSEQETNL IGTTTAIISP EESTSLMDTS LSLSSPSTVS
FTTYSTSPRT SSSPYTKKYT IMEKTTTSKY EDSSVSSDSS IFLTEVPSTS STRDDFITLE
PVTISSITVT EGYFYETETK STEVYLSTGK SIHDGEITKE PGDYDQTTKI RLPVSSRIDD
VTEYATSSSY QPTIDEGQKD NRTSVTSAIM DHATDVTLPI DTTFRYTTDS IQNRTFEFGT
TIIDTPRTVI PLTTSSTLPS VLSSTIKLDT STVPSSLTST SISSLSQTTV TSIEVNTTEI
DACRGTQCST STTMITPRNI TEYADGCKTD STITQAAFNG KSFVRQRVEV IMTENKSATL
RIYVKLKTAF KNGIILHVYF DNERYSLVYL ELGSLKFQFS CGLETMLLGE IDAIIDNGYE
VGIDMSFQYV ANDENEKCFA KLLVNGTMAV TGEQILPQRG MIPKYANLYI GGIPLTFSHY
FPHVAMGFIG CIDSLKINGI MRHFIHDSIE TFQIEECTSF LCLSNPCQNF GACEESDGRI
RCKCIAGYTG PLCEHSACND NPCSMGATCV SSPGTGFICV CPLGSRGLFC EEDVILVRPA
FSVLVPGFAS YIAYGVSTSI KDTMELKLRL IPRTFDQISL IAYFGQRSPR RDISDHLSIT
FVRGYIMLTW DLGSGVRRIF TSDSLTSLSV TGSVGKSKTY TLRIGRRGKK AWLAVEGLKN
VTGQAVGSMT QLDVSPVLYI GGYKSKNFET LPHDLPLHTG FSGCIFDVEL RTDTTILPLT
GSSPATGRGV GECNRNECIR HSCKNGAVCL HHGASYR
//
