ID A0A3B0KB18_DROGU Unreviewed; 2052 AA.
AC A0A3B0KB18;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Blast:Protein crumbs {ECO:0000313|EMBL:SPP83299.1};
GN ORFNames=DGUA_6G018136 {ECO:0000313|EMBL:SPP83299.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP83299.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUW01000007; SPP83299.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0KB18; -.
DR OMA; NCELNLN; -.
DR Proteomes; UP000268350; 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: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; 15.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 22.
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:SF30; DELTA-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 16.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00181; EGF; 24.
DR SMART; SM00179; EGF_CA; 18.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 15.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 12.
DR PROSITE; PS00022; EGF_1; 20.
DR PROSITE; PS01186; EGF_2; 13.
DR PROSITE; PS50026; EGF_3; 23.
DR PROSITE; PS01187; EGF_CA; 8.
DR PROSITE; PS50025; LAM_G_DOMAIN; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1989..2013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..306
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 309..346
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 351..389
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 391..428
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 430..466
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 467..503
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 629..665
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 695..730
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 732..769
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 771..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 811..847
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 849..885
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 887..928
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 930..1114
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1116..1152
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1159..1387
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1383..1419
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1447..1663
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1664..1698
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1700..1736
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1738..1774
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1777..1815
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1818..1854
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1856..1893
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1895..1933
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1934..1974
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 15..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 296..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 336..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 360..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 379..388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 456..465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 493..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 655..664
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 720..729
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 759..768
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 780..797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 799..808
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 837..846
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 875..884
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 918..927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1142..1151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1409..1418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1688..1697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1726..1735
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1764..1773
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1844..1853
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1923..1932
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1964..1973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2052 AA; 224184 MW; 190FCCC9552FE1D6 CRC64;
MAQIVNASAS ATAATAHVTR QQQQQQQRLQ HQQQRSRSAA RRMQSRARTK SAAQITTSTA
QHLLKRAISA PQWIFLFILI YLATDVASVE VQTQEAYFNG STYLRLTTPM PIWDHSAISF
RSCRGGEILA QQYNKNSIVI SVLNDFLQIS LAGPAVHGPN NRLDVKLPYQ LLDNRWHTLQ
FKYEYGNLYL HVDRAASIFA NSTYNSQFLT NQDIGYKDAI LILGNSFSGC LLDGPGLQFV
NNSTVQNVVF GVCPLTPGPC SDHDLFTRLP DNFCLNDPCM GHGTCSSNSE GYECRCTARY
SGKNCQKDNG SPCGKNPCVN GGTCLENSRG DYQCFCDAQH SGQHCETEVN IHPLCQSNPC
LNNGACVVLG STGSIACECP KGYAGPRCEI DTDECASQPC QNNGSCIDRI NGFSCDCSGT
GYTGAFCQTN VDECDKSPCL NGGRCFDTYG WYTCQCLDGW GGEVCERPMT CQTQQCLNGG
SCVDKAIGFQ CLCPPEYSGE LCQLGPSCAQ QCPIDSECIG GKCVCKPGTT GYSWALHGHN
MFGFSFNFFG FKWFFNGLNL TTTKASDLEP PIPAPIEVEM FDPSQCASEK KKRYISPEWL
KRKRCELKLS YNCQQSTGDG GTAAAMALTP INCNATNGKC LNGGTCSMNG THCYCAVGYT
GDRCEKADNC SPLNCQEPMV CVQNQCICPE NKVCNQCATK PCQNGGECLD LPNGDYECKC
ARGWTGRNCA NDVDECTLHP KICGNGICKN EKGSYKCYCT PGFTGIHCDS DVDECLSFPC
LNGATCHNKI NAYDYECVCV PGIIGKNCEI NINECESNPC SKHGTCNDGI GAYTCECEPG
FEGPHCEVNI DECERFNPCQ SGTCIDQIDD YDCDCDANFG GKNCSVPLIG CLTNPCLNSG
TCRPYLVNET IHLYNCTCEN GFQGDTCEKT TTLSMVATSL ISVTTEREEG YDINLQFRTT
LPNGVLAFGT SGEKNEPVSY ILELINGRLN LHSSLLNKWE GVFIGSKLND SNWHKVFVAI
NTSHLVLSAN DEQAIFPVGS YETANNSQPS FPRTYLGGTI PNLKSYLRHL THQPSAFVGC
MQDIVVNGKW IFPDEQSANF TYGDTKLENV QSGCPRTEQC KPNPCHSNGE CTDLWHTFAC
HCPRPFFGHT CQHNMTAATF GHENTTHSAV IVETTDVGRR AIRSILDISM FIRTREPTGQ
VFYLGSDPRK TPTKNIGDSY VSAKLHGGEL LVKMQFSGTP EAYTVGGQKL DNGYNHLIEV
VRNQTLVQVK LNGTEYFRKT LSTTGLLDAQ VLYLGGPAPT RESLLPASTE PGMDESATVL
SKEAADDSKD YFKGIIQDVK VSNGSLNLIV EMYPLNVTDV QVNAKPLGAV SIDRASVLPG
EVSDDLCRKN PCRHNAECRN TWNDYSCKCP NGYKGKDCQE IEFCQLVTCP GESVCQNLDD
GYECLTNTTF TGRERSPLAF FYFQEPPPAE ETGGETGPKQ TLKPSIEIAY RTRAGGTLLF
IDNADSFFEI GVNGGRVTIT WKLTQLHIGE STRFEKENAD GEWSRIFLRA HNGKLEGGWK
GWESMVDPAP SFSVDIDQAA IQYLLSSSTQ VYLGGMPESR QSRGSTLSAQ QGSQFKGCVG
EARVGDLLLP YFSNTELYPR TENVSVQLKA QFRLNTTRPA EGCILCFQTD CRNDGYCRAP
SDEYECTCQA GYEGDDCGTD IDECLNTECQ NNGTCINQVA DFFCQCQDGF QGRHCELNIN
ECAELPCHNG GNCTDLIAAY YCECPEEYTG PQCDILKQMT CENEPCRNGS SCENGFNALT
GNNFTCTCAS GFEGSLCDVP FCERTPCDNG GLCLTTGLSP MCKCSLGYTG RLCEQDINEC
DSNPCQNAGK CMDLVGGYEC NCLGTGFEGI HCENDIDECS VEGEYCGGLG RCFNKPGSFQ
CICEKPHCGA YCNFTDPCNA TDICGNGGRC MEDCGAKPDY YCICTEGFAG KNCTSPIVAK
EDGPSTTDIA IIVIPVVVVL LLIAGALLGT FLVMARNKRA TRGTYSPSAQ EYCNPRLEMD
NVLKPPPEER LI
//
