ID A0A1B0A1T3_GLOPL Unreviewed; 2048 AA.
AC A0A1B0A1T3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI031859-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI031859-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI031859-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:PRU00124}.
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DR STRING; 7398.A0A1B0A1T3; -.
DR EnsemblMetazoa; GPAI031859-RA; GPAI031859-PA; GPAI031859.
DR VEuPathDB; VectorBase:GPAI031859; -.
DR Proteomes; UP000092445; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PTHR46513:SF13; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 4-LIKE PROTEIN; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 10.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 15.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW 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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..2048
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008403434"
FT TRANSMEM 1936..1954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 643..658
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 705..747
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 748..790
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 791..834
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 835..877
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1019..1061
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1062..1104
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1105..1148
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1149..1190
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1323..1365
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1366..1408
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1409..1452
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1453..1494
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1628..1671
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1672..1714
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1715..1758
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 68..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 249..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 300..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 321..333
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 328..346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 340..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 360..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 367..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 379..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 429..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 451..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 458..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 470..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 503..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 515..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 560..575
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2048 AA; 231707 MW; 0268C094ECBE8064 CRC64;
MYYLFVLVLF ARLVHGDYGY PTTTWHGLTD LESKAEYGSA SKQLLIPNHV RDYVGFYHQR
QERLKPQLRS AGGITKGFHT SSPKSGDSDK YHESQDHANY DDYVIHPSDT PSHDISDDDY
FVPELSHYPH EIFTTEPLQQ QTSHEVGQGF NPGESARHRD VGARSGSRTD LYGVRESGDR
REMTRGREGY MNMLHTKQKV FRPHVSLVHD ETRLASPNDG YRRDCPNICG EMQWQCATKC
NCIHANERCD KEPQCEDGSD EYDCDVVGDM MSKLQRECEQ TGMHVMCPKT YRCINKEWLC
DGDDDCGDYS DETHCGERIN CTEDQFECAN GFCIPKQWLC DGENDCKDFS DEGHCNRTSC
SNEHFTCNDG YCVSIAFRCD GERDCNDNSD EYKCPAVINS CPEGEFKCRG GLGGAGGPSG
QCVLNRFLCD GDNDCGDWSD EENCPQKPSQ CTSGELKCAD GTCIPKRWKC DKEQDCDGGE
DEHDCGNMNS SLHSSCGTDE FTCNNGRCIL RTWLCDGYPD CSSAEDEVEC HLQCESGQFL
CPAKKNITNL KICVHQKHVC DGQNDCPFGE DEVNCPHYRD CESDAKCEQL CITTAKGRKE
CACRLGFLMH KNKQNCTDID ECQYLSSPVC SQKCENTYGS FVCSCERGYV LRPDLRTCKA
LGGAMTLIVA NRWDIRRVTL SNNRYAALVK GLHNAIALDY HFKKGILFWS DVSTDVIKTV
YMNGTRVRDV IKWGLEAPGG VAVDWIHDLL FWTDSGTRRV EVSNFQGNLR SVIVSNDLDK
PRAIVVHPGE AMVFWTDWGP NPKIERAYMD GSQRQIIINK GVTWPNGLAI DYPSNKLYWA
DAKQHAIECS NFDGSERIKI LSTHLPHPFA ITIFEDTMYW TDWNTKTVSA ANKITGKGFR
SVHENFHFPM DIHAYHPARQ PEYPDRCQKD RRGLRGGCSH FCLPNKNSRR CGCPIGLSLK
DDGKTCKSAP EKLVLVARRK DIRLRQIHAK SSTYNDVDMI IPLDNLKHAV ALDWTSDSDT
IYWTDVEKSS INKAYLNGSH QQKVIHSNLV SPAGLALDWL TDKLYWTDPS TNRIEVATSN
GKIRTLLIWD LLDKPRDIVV NPIEGLMFWS DWGDRPMIEC AHMDGKKRRV VTSDNLKWPN
GLAIDYEQQR LYFVDGGTKS LEYMNFDGSE RKTLLGGLGH PFGLDVSESR VYWTDWDLKA
ALSADKQTGK NMTTVIANSS DLMDISVFHR YRKRISHACA NDNGGCSHLC LLNPTSYSCA
CPVGITIQPD NRTCSSGPSK YIIFAHRVDI RQISMDFDHL IDVVLPLPPI SNAVALDVDR
KTGQIYWSDI VDSLIMSSSP DGLNVNRIIY ESLDSPDGLV IDSVGRTLYW ADAGRHTVEV
ATLDGRYRHL IAWKDLESPR GLALDYEAGF LFWTDWGHYR KIERAYMDGE NRQRIVTSNL
LWPNGLSLDL KAKRIYWVDA KLKVIDSCDY EGNQRKLIMS ALHHPYALAL TDEFIYWTDW
KSKALHMADR NNVSDKRDVM TNIDGLMDIK VISTNEKLPS NACGENNGGC SQLCLRNPSG
YTCKCGIGLK LINGNSTECE YLPEDYLLIA LRSGIGLISL TTPDLMDVVL PIPGVHGVVV
LDYHYRRNWL YIADVNLDII RRVNLKNLTE SKVIINTKLA TPNGISVDWI ADNIYWSDSD
HRIIEVARLD GSCRKSILSD DMGDPRSLIV HPKRGYLFWS DWDTPSRIER CLLDGSNRTI
LVGNNLGFPT GLTIDFENRR LLWADALEDN IGQVDFNGKH RTVIIPYASH PFGLTMFENS
IFWTDWYNKS VYRAYRKGRS FSQPVEIRDS LSGALDIRAV SLKRQLQEWN QCAQDNGGCS
HLCLFRGLDY VCACPDQIDH SRECSTSPKF YVPPQQRLDE NLADYTDEVT ESDNPMLTED
DFGDDYRIKK SSRRETLILI AIGIVIILLV INLVHNSKRT KSKRHKRGGS SRSVLTFSNP
NYNVDGTPIE PKTTIWKRFK SDRIHERVYE ERSLTTETAS SSLFVPTPSP ATSPSVKKIQ
LSTLSTIA
//
