ID A0A158NC55_ATTCE Unreviewed; 1204 AA.
AC A0A158NC55;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=105618183 {ECO:0000313|EnsemblMetazoa:XP_012055113.1};
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_012055113.1, 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_012055113.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. {ECO:0000256|RuleBase:RU280815}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}.
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; ADTU01011659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01011660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01011661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01011662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01011663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01011664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012055113.1; XM_012199723.1.
DR AlphaFoldDB; A0A158NC55; -.
DR STRING; 12957.A0A158NC55; -.
DR EnsemblMetazoa; XM_012199723.1; XP_012055113.1; LOC105618183.
DR GeneID; 105618183; -.
DR KEGG; acep:105618183; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; A0A158NC55; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
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; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24044:SF503; DELTA-LIKE PROTEIN; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR02059; JAGGEDFAMILY.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00179; EGF_CA; 13.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 5.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU280815};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280815};
KW Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1204
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629040"
FT TRANSMEM 1035..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..210
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 211..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 278..316
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 318..354
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 356..392
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 394..432
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 434..469
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 471..507
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 509..545
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 596..632
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 634..670
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 672..708
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 711..748
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 750..786
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 788..824
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1067..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 168..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 181..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 201..210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 234..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 306..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 344..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 382..391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 422..431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 438..448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 459..468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 497..506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 535..544
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 622..631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 660..669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 698..707
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 738..747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 776..785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 814..823
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1204 AA; 129992 MW; 015D8F9F0972F8A2 CRC64;
MRAATTYILF LAHLIQATTA SGYFEVQILS LTNNRGTLVD GRCCGGGGGG GKEEFPPCTT
PCSTAFWLCL KEYQSNVTAI GSCSFGNVSS HALGQNTFTL SDPVTLHLHF TFRWTRQFTL
ILRARDEESA GVIEEASYSG IVLPGPTWHT LNHQGKNANL AYRVRVQCAD HYYNATCTKF
CRPRNDIFGH YTCDENGDKV CIQGWKGVDC ETAVCKEGCH PVHGHCNVSG ECQCRHGWRG
ELCDQCMPYP GCKHGYCNGS SWQCICDTNW GGILCDQDLN YCGTHEPCQN GGTCENTAPD
QYRCTCPEGF SGPTCEKIDN PCASNPCLNG ATCREFGETA QCECAPGFSG SFCAIDIDEC
ASQPCQNGGT CVDGKNSFVC NCPFAWKGVL CQFDVDECTL KESPCKNSIT CINLAGDYRC
RCRSGFTGKN CTKNINDCVG QCQHGALCID LVDDYHCSCT PGYSGKDCDV DIDECASKPC
QNGGDCRDLV NAYECVCPVG FTGYQCEIDR DHCSPNPCRN SAPCFNTQTD YYCHCPTQWQ
GRNCSEPALN NPQFGVLDDG QSGCGSEGTP CGGKGRCSGG RCICDPGYTG VHCHENINDC
RGNPCLNGGT CVDLLNSFQC ICREGWSGDL CDQNVDDCLT QPCHNNGTCV DGVADFTCIC
QGDWKGKTCT LRRGHCDEDT CRNGGDCKDH GDSFTCNCPR GWEGTICHIA SPSACTSNPC
ANGATCVNTV DGSYRCVCRE GFEGPDCRSN VDNCQPVPCL NGGKCVDGDN WFRCECAPGF
TGPDCRINVN ECASDPCTGG ATCVDGIASY SCICPPGRTG PRCEIRTAGG PGCTATTWED
ECNVCECRNG KNQCSNVWCG PGNCLNGTSC LAHEVCVPSP GESCLAPPCP AWGECRPIET
GRRVGPPALP APPSCWPGQT TLGPTCSRLT ILLRRDTLAS GTSVELLCRR LRKLLVDPRR
PQSVVLLCDL KPGDNDTIEV TIFSEAAADA ARDLGETLSR PLARPLVLVS VLEVKVETAL
LSEPSLASAA NASSYVTVLG SALAIVLLLV LFGSFWYLKT MRHRSNLTAT TSSETSLHRH
RSDLDEKSNN LQNEENLRRY ANPLKDQDSE PRVSVVRPLS GTSLGTLTGT EESLEMVSEE
GRHRLPPLYK PPSAEARNNT ASFSYEEGPH KPYIKPRLQE PMYPHQQPGT SQTSGPHQVL
TVHV
//
