ID A0A182R204_ANOFN Unreviewed; 2053 AA.
AC A0A182R204;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN000193-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN000193-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN000193-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; 62324.A0A182R204; -.
DR EnsemblMetazoa; AFUN000193-RA; AFUN000193-PA; AFUN000193.
DR VEuPathDB; VectorBase:AFUN000193; -.
DR VEuPathDB; VectorBase:AFUN2_013186; -.
DR OrthoDB; 3107655at2759; -.
DR Proteomes; UP000075900; 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; 2.
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; 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; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 12.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 16.
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};
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 1936..1960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 659..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 721..763
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 764..806
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 807..850
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 851..892
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1030..1072
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1073..1115
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1116..1159
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1160..1202
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1335..1377
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1378..1420
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1421..1464
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1465..1506
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1641..1684
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1685..1727
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1728..1771
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1772..1813
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 88..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 264..279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 316..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 337..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 344..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 356..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 375..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 382..400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 394..409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 444..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 466..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 473..491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 485..500
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 510..522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 517..535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 529..544
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 576..591
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2053 AA; 229256 MW; AC40DCEFB46818B4 CRC64;
MAEQHRNRGC GRSYHCRVAL TGFRVRFGLI VPLLTVPLFL GLVHGEEQTT EITSEGVGHY
TGKSDQTQAG PNQLGAAWQI FGSNSMRQSG EGRVVKTKPR KPKPYQKDIR PQLPPGKIMM
APPRRRTFHQ ATQYPKNASI AIDRSAGLSH HPIGSHAAGG NVYGSMSHYD TVYGIRGVER
RDNDGFRPFE RYGPSAHLGH YHIQPDDDIF RPDDELLMES GGGGGGAAGK VDGLAGIESC
DIKCEPREFT CDKSCACIHM DLHCDGQADC VLTEDEQNCE IVHQRLAQQI KDNCETSGTH
VICATTHTCI SRDWLCDGDD DCGDYTDETH CGSRLECTEE KFECQNGMCI PRDWVCDGDN
DCNDLSDEKN CTKQCTRDEF RCKDGSCISA SFQCDGETDC IDESDEANCD RPMQSCPEGE
FKCKGALGGM GGPGGRCVLM RFRCDGDNDC GDWSDEENCP KKQVDCMINE FKCDDGDCIP
LQWRCDDKQD CNNGEDEKNC PVDRIAGRTC SPDEYTCKDG RCILRSWVCD GTADCRRGED
EQDCDIKCEL NQFLCPSGSR NSTRDSSVCI NQKHVCDGHS DCANGEDEMR CPIVHPCGAH
SRCEQLCVTA YSGREECMCR PGYLLHGNGY NCTDIDECTI TSNPVCSQEC MNVAGSFRCS
CQAGYVLRPD QRTCKAVGGS VKLLMANRAD IRQVSLSNNQ YTSIAKGLPN AIALDYHYRQ
DLLFWTDVSI DVIKRSHLNG SGVRDVIKWG LESPGGLAVD WIHDLLFWTD SGTRRVEVST
LDGQMRAVIA ASDLDKPRAI AIHPGRALVF WTDWGTAPKI ERAYMDGSDR QTIIAEAIFW
PNGLTIDYTS SRIYWADAKH VIESANFDGR ARRKILSNNL PHPFALALFE DSMYWTDWHT
KTISTASKVN GRGFRVVHEG LHFPMGIQSY HPSRQPDFTN RCAMDKSGRK GGCSHLCLPA
RTHRRCACPI GLTLRPDQKT CSTVPDKLLL IARKKDVRVR QLDAANPVDM VLPLDGIKST
VAVDWCSRTN VIYWTDVGKS MISRAFINGS QQEAIVKSNL ISPAGLALDW VTDKIYWTDP
GTNRIEAATT DGRQRALLIW ERLDKPRDIV VHPGEGYMFW SDWGSNPLIE RAGMDGSGRF
TLVSENLQWP NGLALDVDKQ RLYFLDGGTK SLEYVNYDGT GRNRLITEGL KHPFGLDVYE
KRVYWTDWDT HSIQVANMYN GHDRRTILAN NTDLMDIRVF HRNRRDSRNP CAHKNGGCSY
ICLLNPTSYS CACPIGIQLK DNGKTCKSGP SNYLVFAHRT EVRQVSLDSD YQIDVVLPLP
PISNVVTLDV DRRTGEIYWA DTIEDVIMRS TPDGMRIKQI YSESMTSVDG LVIDSIGRKL
YWTDAERKVL EVSDLEEGIR SALVWKELEQ PRGIALDYES GYLFWSDWGA NPRIERSDMD
GENRIDLITE GLGWPNGLAV DRSAKRIYWA DAQMKTIESC TFSGGLRTKV VENLPHPYAL
AVTARTIYWT DWITKALHSV PKSNPAHIRN VTHGLEGLMD VKVVQEDEER HLENVCGASN
GGCSHLCLRN PTGYSCKCPT GLTMREGSTT ECKTLPDEYL LIALRSGIGR ISLDTPDLFD
VVLPIEGVHG AVVLDYHFDS MYVFYADVNV DAIRRVNMHN YSDTQVIVSS GLNTPNGIAV
DWLADNLYWT DTALKKIEVA RLDGSCRKAI LTDGLDDPRS IILYPKRGFV FWADWGQTPK
IERSYMDGSE RRSIVDFELG FPTGLAIDFD AKKLYWADAL QDRIELCDFD GRRRQQVVSH
ATHPFGFTLT ATHLYWTDWY NKSVLRAPKY SVSNVEVARF SLRGALEIRA VSGQRQPHDW
NPCRRDNGGC SHLCLYAETR YVCGCPDIPD AHHCDLEPTF LVPMKANDEM LSASEEKPGR
SNGGIVLTTS RMHAQLVIIA TAILAGLLII VIIAILVLIV NSKRKQSKKS SRSASDVLTF
TNPNYNGIEG LCQAGDAGSS RNTIWKRLKY DRAQERVFEE KYLGVQHHGT SNGSYLASTP
TSQITPVSAV LPV
//
