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Database: UniProt
Entry: A0A158NY68_ATTCE
LinkDB: A0A158NY68_ATTCE
Original site: A0A158NY68_ATTCE 
ID   A0A158NY68_ATTCE        Unreviewed;      1660 AA.
AC   A0A158NY68;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   Name=105625766 {ECO:0000313|EnsemblMetazoa:XP_012062476.1};
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_012062476.1, 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_012062476.1}
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; ADTU01003247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01003248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012062476.1; XM_012207086.1.
DR   STRING; 12957.A0A158NY68; -.
DR   EnsemblMetazoa; XM_012207086.1; XP_012062476.1; LOC105625766.
DR   GeneID; 105625766; -.
DR   KEGG; acep:105625766; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   InParanoid; A0A158NY68; -.
DR   OrthoDB; 2877710at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 11.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR   Pfam; PF12662; cEGF; 2.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00057; Ldl_recept_a; 11.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00192; LDLa; 12.
DR   SMART; SM00135; LY; 8.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   SUPFAM; SSF57424; LDL receptor-like module; 11.
DR   SUPFAM; SSF63825; YWTD domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 7.
DR   PROSITE; PS50068; LDLRA_2; 11.
DR   PROSITE; PS51120; LDLRB; 3.
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}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1368..1389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          221..260
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          390..433
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          434..476
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          1002..1036
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          1220..1262
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        23..41
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        62..74
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        69..87
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        109..127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        156..174
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        168..183
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        225..235
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        717..729
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        724..742
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        736..751
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        800..812
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        807..825
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        819..834
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        864..879
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        882..894
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        889..907
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        901..916
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        934..952
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1590..1608
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1660 AA;  187927 MW;  465BE66BFA447C12 CRC64;
     MRLDSNFKTQ KCQNLHGKNS FICNNGQCIL LSYRCDGTDD CTDGSDEEDC DDYSDSNSSI
     KCSKHEYKCK SNNCIPIAKF CDVIQDCPDG SDEYDDCVKD LNCSGRFQCA DEHCVFHDWV
     CDSNKDCPDG SDEWNCNANK TSSASYCKIE NSQYLCENQL CIPLKLVCNG KDDCGDKSDE
     AGCTSSCSVK CDHECKQTPK GSICFCKPGY KLQNDNRTCI DIDECQIYGV CDQECINTPG
     SYSCRCQTDY FLQQDKKTCK AIAGEATIVF SAKTEIVGMY LDSQINFIVA KHLNRVIGVA
     MNGDHTYWSD IEEDREVIVR STPQNKHEVI VMMGLKEISA IAVDWITQNI YFTDTGYNRI
     GVCKDDGTYC TILINDTDKP TGLALLPTHG KMYWCDWSSN PHIAVAGMDG KNIRIFVSTN
     LKAPQSLTID YPTNRLYWAD IKLKKIETIR LDGTDRRVVL HDIIEDPFSL AVFENKLYWS
     DWESKSVESC NKFTGKDWNI LHLGQHSHFS VHIDHSAIKP KVDNPCHFNP CSELCMLNQE
     NGYTCACTLD KKLNADNHTC QEVTKNLLIL HDTIFTNYYH GMLGKLKTRI ASKVLLPQDI
     VSDPTSGQVI CYIMTERFEK AIVLFDPVSD TFKNTILHNV SYFSMAFDHV GNNLYMTNKP
     SSSINVYNVK TLAMTVFYFK EYVPYYITLV PEERCDGNVH CPNGEDETIG CHXKKKCKKD
     EFTCTNGECV SIKSHCNWHY DCTDQSDEEN CIKPKCTNDE FQCRNGVTPC ISKSLLCDGD
     FDCEDGSDER PEACKSNASC LNDKFQCNDG NCISLSLKCN GIDDCLDGSD ERHCLAKSVY
     LTNCTADKYR CLDTYLCLPK KVKCDGKSDC PKNDDEHNCV FCFDNEFTCD NAECIPENWV
     CDQSDDCGDN SDEKNCDGSK KTIMESTKCD EFKCSIGTCL PYSKVCDGNR DCPDGSDENG
     KCQIACMVNN FCKGLCYKTP KGDVCGCPYG YRLAADATSC EDINECENDV CSQFCRNTVG
     SFECSCQEGY YLRNKVSCKA IGPAMEFITV TDNDIRKISS NLHSIDKIYS LSGLSINGLD
     VNAVHDSIYW SNGEFGTIKK LNIKTKKVTT IMIVEHPQSL AVDWITDNVY VNDNGYLNTI
     KVCNLEKEKC ATLIEIEEKA KVVSIVVDSI NRWLFWTQIT WQMDVPFSKI CRTDMMGADM
     KIIGSDVSFV SGIAIDHIKS KLYWSDSFSK TIESSNFDGS QRSMFLRTNM YYPFGISIYE
     QSLYWLMDTS GQLQSCKLYG KKSCETINIG KNNVHKQFAI LHISRQPVDK NPCNEKYCDY
     MCVLKKDNAT CICLDGKSIE SNNICTNMNN GRTSFKNLTR NARYTSGLYS LIIIVLLIIV
     LSLCIYYYYQ KNRLKSKSMN NLSCSSIHFH NPSYDRSNEV EVTLNSIVAG LSPGQHEYVN
     PIDNKFLNLK DAMENSENRQ KSDPYSKERD IEEIEKQDSL IYFSKLRMLN QENGYTCACT
     LDKELNRQSH LSSRDEMYCL VTPDSLVNCS KHEYQYLSTN LCLSKQVRMK CIPKSWECEK
     HDCDDNSDKK SCVDSKKTIM ESTECDGFKC SIGTYLPYLK VCDGIQDCPD DSDENATPRG
     DVYYPDGYHL AADATSCEDE RRINECEKDD EFARNFVEIQ
//
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