ID A0A2C9H8B1_ANOQN Unreviewed; 2064 AA.
AC A0A2C9H8B1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA016727-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA016727-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA016727-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; 34691.A0A2C9H8B1; -.
DR EnsemblMetazoa; AQUA016727-RA; AQUA016727-PA; AQUA016727.
DR VEuPathDB; VectorBase:AQUA016727; -.
DR Proteomes; UP000076407; 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; 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; 13.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1947..1971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 670..685
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 732..774
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 775..817
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 818..861
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 862..903
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1041..1083
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1084..1126
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1127..1170
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1171..1213
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1346..1388
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1389..1431
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1432..1475
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1476..1517
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1652..1695
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1696..1738
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1739..1782
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1783..1824
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 275..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 327..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 348..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 355..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 367..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 386..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 393..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 405..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 455..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 477..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 484..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 521..533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 528..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 540..555
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 587..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2064 AA; 229134 MW; 1772ADAD63EFAEF2 CRC64;
MVVAAAAEPR RNRGSGRSHR CLAALAGFGV RLGLIVPLLT VPLFLGIAHG EEQTTEITSE
GVGHYGGKSE QSGPPGPNQL GAAWQIFGSN SMRQPGGEGR VVKTKPRKPK PYQKDIRPQL
PPGKIMMAPP RRRTFHQATQ YPKNASVAID RSAGLSHHPI GSHAAGGNVY GSMSHYDTVY
GIRGVERRDN DGFRPFERYG PSAHLGHYHI HPDDDIFRPD EELLMESGGG GGGGGAGAAG
KADGLAGIES CDIKCEPREF TCDKSCACIH MDLHCDGQAD CVLTEDEQNC EIVHQRLAQQ
IKDNCETSGT HVICATTHTC ISRDWLCDGD DDCGDYTDET HCGNRHDCTE EKFECQNGMC
IPRDWVCDGD NDCNDLSDEK NCTKQCTRDE FRCKDGSCIS ASFQCDGETD CIDESDEANC
DRPMQSCPEG EFKCKGALGG MGGPGGRCVL MRFRCDGDND CGDWSDEENC AKKQVDCMIN
EFKCDDGDCI PLQWRCDDKQ DCNNGEDEKN CPVDRIAGRT CSPDEYTCKD GRCILRSWVC
DGSADCRRGE DEQDCDIKCE LNQFLCPSGS RNSTRDSSVC INQKHVCDGH TDCANGEDEM
RCPIVHPCGA HSRCEQLCIT AYSGREECMC RPGYLLHGNG YNCTDIDECS ITSNPVCSQE
CLNVAGSFRC SCQPGYVLRP DQRTCKAVGG SVKLLMANRA DIRQVSLSNN QYTSIAKGLP
NAIALDYHYR QDLLFWTDVS IDVIKRSHLN GSGVRDVIKW GLESPGGLAV DWIHDLLFWT
DSGTRRVEVS TLDGQMRAVI AASDLDKPRA IAVHPGRALV FWTDWGTAPK IERAFMDGSD
RQTIIAEAIF WPNGLTIDYT SSRIYWADAK HVIESANFDG RARRKILSNN LPHPFALALF
EDSMYWTDWH TKTISTASKV NGRGFRVVHE GLHFPMGIQS YHPSRQPDFT NRCAADKSGR
KGGCSHLCLP ARTHRRCACP IGLTLRPDQK TCSTVPDKLL LIARKKDVRV RQLDAANPVD
MVLPLDGIKS TVAVDWCSRT NVIYWTDVGK SMISRAFING SQQEAIVKAN LISPAGLALD
WVTDKIYWTD PGTNRIEAAT TDGRQRALLI WERLDKPRDI VVHPGEGYMF WSDWGSNPLI
ERAGMDGTGR FTLVSENLQW PNGLALDVDK QRLYFLDGGT KSLEYVNYDG TGRNRLITEG
LKHPFGLDVY EKRVYWTDWD THSIQVANMY NGHDRRTILA NNTDLMDIRV FHRNRRDSRN
PCAHKNGGCS YICLLNPTSY SCACPIGIQL KDNGKTCKSG PSNYLVFAHR TEVRQVSLDS
DYQIDVVLPL PPISNVVTLD VDRRTGEIYW ADTIEDVIMR STPDGMRIKQ IYSESMTSVD
GLVIDSIGRK LYWTDAGRKV LEVSDLEEGI RSALVWKDLE QPRGIALDYE SGFLFWSDWG
ANPRIERADM DGENRVDLIT EGLGWPNGLA VDRAAKRIYW ADAQMKTIES CTLSGGARTK
VVENLPHPYA LAVTGRTIYW TDWITKALHS VPKGNPAHIR NVTHGLEGLM DVKVVQEDEE
RHLENVCGAG NGGCSHLCLR NPTGYSCKCP TGLTMREGST TDCKTLPDEY LLIALRSGIG
RISLDTPDLF DVVLPIEGVH GAVVLDYHFD SMYVFYADVN VDAIRRVNMH NYSDTQVIVS
SGLNTPNGIA VDWLADNLYW TDTALKKIEV ARLDGSCRKA ILTDGLDDPR SIILYPKRGF
VFWADWGQTP KIERAYMDGS ERRSIVDFEL GFPTGLAIDF DAKKLYWADA LQDRIELCDF
DGRRRQQVVS HATHPFGFTL TATHLYWTDW YNKSVLRAPK HSVSSVEVAR FSLRGALEIR
AVSGQRQPHD WNPCRSDNGG CSHLCLYAET RYVCGCPDIP DAHHCDPEPA ILVAMKPNDE
MLSASEEKPP HSNGSIVLSS SRMHAQLVII ATAILAGLLI IVIIAILVLI VNSKRKQSKK
SSRSASDVLT FTNPNYNGIE GLCQTGDSGS SRNTIWKRLK YDRAQERVFE EKYLGVQHHG
TSNGSYLAST PTSQITPVSA VLPV
//
