ID A0A158Q478_DRAME Unreviewed; 4654 AA.
AC A0A158Q478;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=EGF-like domain-containing protein {ECO:0000313|WBParaSite:DME_0000419201-mRNA-1};
GN ORFNames=DME_LOCUS8075 {ECO:0000313|EMBL:VDN58102.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000419201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000419201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN58102.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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:PRU00124}.
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DR EMBL; UYYG01001165; VDN58102.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q478; -.
DR WBParaSite; DME_0000419201-mRNA-1; DME_0000419201-mRNA-1; DME_0000419201.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 30.
DR Gene3D; 2.40.128.620; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 34.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 8.
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; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 30.
DR Pfam; PF00058; Ldl_recept_b; 6.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00192; LDLa; 35.
DR SMART; SM00135; LY; 33.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57424; LDL receptor-like module; 34.
DR SUPFAM; SSF63825; YWTD domain; 8.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01209; LDLRA_1; 15.
DR PROSITE; PS50068; LDLRA_2; 34.
DR PROSITE; PS51120; LDLRB; 13.
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 Reference proteome {ECO:0000313|Proteomes:UP000274756};
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 4529..4554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 472..514
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 556..600
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1452..1467
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 1516..1558
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1559..1602
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1603..1646
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1647..1691
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1914..1960
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1961..2003
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2180..2224
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2225..2268
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2545..2595
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 3251..3266
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 4302..4345
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 4347..4388
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 4621..4654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4621..4643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 40..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 47..65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 59..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 103..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 212..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 219..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 231..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 271..286
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1055..1073
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1138..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1145..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1179..1191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1186..1204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1240..1255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1304..1316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1311..1329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2760..2778
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2794..2806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2801..2819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2813..2828
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2834..2846
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2841..2859
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2921..2933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2928..2946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2975..2993
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3061..3073
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3068..3086
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3101..3113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3108..3126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3120..3135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3148..3160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3155..3173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3634..3646
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3641..3659
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3653..3668
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3716..3728
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3723..3741
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3842..3854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3849..3867
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3861..3876
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3881..3893
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3888..3906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3900..3915
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3924..3936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3931..3949
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 4014..4026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 4021..4039
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 4033..4048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 4654 AA; 518783 MW; F4BA695EFA736E03 CRC64;
MYFFNLYKNY ERVDFILVDS PVARPVFPVG ISNSGNVGGC TKNDFRCNDG KCIRMEWKCD
GSGDCSDGED EKDCPHPGCK PDQWQCDRYE WHSVSCIAEY QRCDNITDCA DGSDEVDCPA
NSVSCNVDDG SVFQCADGRQ CFDILKKCDG KYDCRDLSDE KDSCPHNHTA CFQYQFRCAD
HSQCIQKSWV CDGSNDCADN SDEPPTCEFK QCNGGEFQCK NKRCQPRKFR CDYYDDCGDN
SDEEGCGHYL CPPQKWNCPG SGHCIDELKL CDGKSDCIDG ADEKNCSSNL CSSLGCQAGC
HPSPSGGTCT CPVGYKLDER FHRTCSDINE CNEWGYCDQG CQNHRPGFTC SCPGECYTLE
MMHGPGTDNL TMRGYCISRE PEKLRLYVAR REGLYRLNPN DKNEEVKKLV NGEFIYGIDF
DYEDKQMFWT DRLSHSVFSA NIDDNGDIQH IKKLDLKNLI YPRNLAVDWI TNHLYIIESG
SRRIDVSTYD GSRRTVLIAD GLTLPLDIAL DPLRGEMFFT NQFKLEKAAM DGTRRKTLIN
IHTHQVSGIV VDIAAKRVYW VDPKVDRVES IDYDGNDRRI VSQGMNNVPH PFGLALFDQY
LYWTDWTRLG IVRIEKFGSP STVIWSNKEN NVFPMGIAAY HPMAQLGHQE SICLGLKIDN
PCLQSGCQGM CILSKDSREF GVGYRCACPI GQKLVDEKRC VDSEDYLLFS SNKVVRGIFP
EMQQNALSEA ILPISPISQR RIGMYFEVEC DIHGGSFFYA DIMDNTVTRV KPDGEGSAPV
LVTHNDGIVS MSFDWIAKQL YYVDNIRNSL EVVKVLEQGL VHPDQLIHRQ LLSGLRDPVA
IAVHPWKGAL FFAEAQRPAR IFRCMIDASD CKVIRNTTLG RPSSFAIDFE ENRLCYGDTL
LKTISCMNFD GSRHFVLPID NPIPVAIALL GEELYYVHQR PYSIRRVSKR NGGIGKIVRE
FTGEERSVFS LKSCSRSNQP IPDPSIDHPC RASDCSQLCF ALPNSSSSSE AQPLIKKCGC
RQGYKINTEN MRNCQRDPRE SVEPLCPNNS SQFLCRNGRC IPNEWKCDGE NDCLDGSDER
NTEGKPCFIP KECPSNTIMC NNTKKCIPQQ YACDGDNDCG DYSDEDIKYC KNGEPPVCAA
KKFQCDNHRC IPEQWKCDSD NDCGDGSDEK FEMCANSTCS SNQFTCGNGR CIPVYWLCDG
DNDCYDNTDE DKERCPPIHC RADYFRCANG RQCISLRNHC DGQQDCEDGS DEDSCVQQAG
KCKHNEFTCV STGLCIPLAW KCDGQKDCDD GSDEPAGICS ESQCASDHFK CDNGRCIFNA
WLCDGENDCG DNSDEDIKHG CQKSQQLSPK CPFEQISCAG SSDICIPLHN LCDGKDHCPG
GTDEGGRCAR DLCAAGRAGC SYKCHMSPDG PICSCPFGEQ LVNKTRCEPE NECLDARTCS
QRCKDEKHGF TCSCDEGYTL GVDKRTCKVT KDLEDARIYI SNRNRIYWSD HKIENWHTFE
AQIENAVALA WDSVDDRIYW SDIREKKIFS ATRNGTNMTA FIAEGLDVTE GISIDWVARN
LYWVDSSLNT IEVASLDRPS ARVVLLYKNI DQPRGIAVDP RKGLLFWTDW GQKPRIERAN
MDGTERIILV DTKVYWPNTI AIDFTTDRVY FADSKLDYID FVNYDGTGRT QVLASPKFIQ
HPHALAIFED TIYYSDRRLQ RLQLYTKYPN GTSGNYAAHT FSRALGVIAV HPVLQPKVAN
NPCSGNQCSH LCLIGKSFTC KCPMGKILDS SGKNCVNDMQ PFLMLVQKNS IFGVKMDESV
NGTPAMSGMV PIAGLNNAFD AAYDPETSEA FCLEHSTTSR VIGPNVSTSR IPDDPYCMAV
DWIGRNLYVG NKISQTIDVI RTHGTQYRAT ILNNDQSPTA VAQPVAIAID SGRGILFWLD
RGAGAVSSKV ARADLDGKNA LVIVSNDLSE LDQIALDLSN QRVYFSESKA GRISSVNYDG
QDRQYILNDA GKQPRSLAFF NNRLFYADSA FDSIEVSTIP NNGEAMEFKH FRREIDRLNN
IRVVAPMSST FSHPCRINNG NCEHLCIARP YSQHQCICAS GYILEGATRC KLYDQSFLLI
ATKTRLMGES KSIALEPIGG TSITAVDIEY ESKSIFVAES TGPNRGIHRL TLGSNEMKPV
VKDVFGSFLI RSIAVDWINY NLYFINVDFE RTHLEVCQLD GKHRKVLLST KTETPTSIAV
DPISRYLYWV DQGQQPSIQR SFLDGSNRQV IIHKGIAEPT DLVVDPNSHM IYWTDAKLDG
IFRVRSDGGT PELVRSDIAA GAGIALLGQN MYWTDSRLEK VFSATSKPNQ TLFSPVTLAA
NLAELGNVVV FDESVQPRAS SPCQITDNLR KSPCPQLCFA TPLSQNPTCA CARGVLRGRS
CEEPNSYLMF IDGDRIVDAP IEPDVKASTP LKESFSSIDN LQSFDVDINL RRIYIVTESP
LGVNISWFAM NQPNQHLIFG QTKPKLSENA VRHISDMKLD WLTQKIYFTT GRGGKIYVMD
VQGEHVATVA NGDWTYAIAL DPCAGLMFWS DSGYKISGGV YEPRIERANL AGGDRKVIIK
EGVSLPAAIT VDYREQRIYW ADVNRLDIES CDYNGNNRRT IGNGYRAKSL EIWSQWLYFS
DPLANGVFRI NKDTGGEFEA VAVDRRIPSV IHIFASGSDI RERSQFCSSL TSNLCKKDNG
GCEQLCAVVP TDIGVAASKI QCSCNDTYEL VQLPGKDIAT QCVLKNDFRG ICQPPYNFEC
GDGTCISLSD TCNGVTDCSD GSDEHPTYCN TRVCPEKYFL CTNRRCIETG RHCNGIDDCG
DNSDELNCAS GTACPAGHFA CSNGHCISES KVCDGHNDCH DEKVSDESKS TCPNLPIDCR
GVRIRCPNTN ICIQPADLCD GYDDCGDKSD ENKLFCMNQS CATHYVRCPS GRCIPETWQC
DGDNDCGEGA WDETHKDCAD ENGRRICHGE YLFQCNNGKC ISRAFICDGE DDCGDSSDES
SIHNCGNRTC SDQEFHCRSN ALLAQPKYEC IPKSWLCDGD VTCAGGEDES KELCGIEKKD
CNKGEFRCMN SHCIHASWEC DGDNDCLDGS DEHANCTYSQ CQPEFWQCSN HKCIPNSWKC
DGNDDCDDGS DEKDCRGVNN SSGSRNSCPP GQFYCTSGEC IDNSKVCDRI YDCADRSDES
STCFVNECTT SQFPLCEQKC VDLPKDYKCE CYEGFALDKD DKKSCHDIDE CEDGSSSCSQ
RCENKIGTYK CSCVDGYSMT SDDHTCKRVD PEPEPWLLFA NKHYIRKLSF DGENYELIAR
GFENVISVDI DMTERKAYII DSGKLRLYRV GLEELDKPVT SYEIVLRHNI FGTEGIAVDW
IGRKFYMLNR QDRALRVCEL DGRFCRTLIR DRIVQPKAIV VHPGRGYVYF TEWSLQPYIG
RISMDGSPEL ADPVVKLAEN DLGWPNALTI DFFSDKLYWA DAHLNEIGFM NLDGGARHHI
PAKRTSHVAS MAVFDDYLFW TDWNLLEVIR ADKWRAANET VLKITTQLPN DIRVIHPFRQ
PKYVNPCGTN NGGCSHLCLI SANENSTSYT CSCPDQFILL ADNKTCEPHC TDRQFACGGE
DAKCIPKLWY CDGEADCRDG SDEPGEGICG LRICAVGEFQ CSNHNCTRPF QLCDGNDDCG
DGSDEVDCDK PCDPWMFKCA ATGKCIPKRF ACDGDDDCGD RSDESDTICK NHLRNCTAEE
FRCTNHKCIP KAWKCDNDDD CGDGSDEPSE CVNVECRKGW TRCATSYRCI PNWAFCNGQD
DCRDNSDEII ERCPSCDDIG EFRCATSGKC IPRLRWMCDS ENDCGDDSDE TDPSCGGTSR
PCSESEFRCN DGRCIPGSKV CDGTVQCNDG LDESQCKIRQ CATGFHQCID GTCIPEHRWC
DRRKDCPDAS DEVHCDEHPN RRSCSPFEFE CANSVCVPRK FICDGDNDCG DNSDETTEIC
KGAVCEPPLR FRCAHSRLCL NILQLCNGFN DCGIHDFSDE HLSMCSSFSE YGDCSTDEFK
CTNGKCINAT LACDHNDDCG DATDEIGCAK KNGITCNTNN DNGGCKHLCT DVSDGYYCHC
REGFQTNPED PFDCIDIDEC SGNNTCTQSC LNTKGSYLCR CLDDFENNVV VGAMTGKDCR
AKGEPALIMI ASNDEVVQLN LAHTNGTVRH PAAKSVGNGD LMAVEFDPRR ELMFWIDNEQ
KAIYRSALPK GNQSHIGQQL DIDFRKLGMT PMAMAVDYLT GNLYITTTSD YLSLRNKRMS
EPRIEGNAGA IYVAKSDGRY LRKIIEGRLQ SPLAIVCLPQ LGRICYTDVG TQAKIECADM
DGNHREIIVN ELIFTPTALA VDEAKDNRLY WADPKFHKVE TILPDGSKRT TIISDNRRPT
AIDVFENNIY WASEETSNIY VQDKFGRGRV HILASNVPNV RSIRVQQRFA RDVVRAESSC
ARASCTHLCV ELPGNGFSCL CPDLSTSLND GSCSGPEVEE LRMPIQCACQ NGGVCQLDGT
CDCGEFEGET CQRPSTVSRQ LIGRFGSNMI LAIALLLMLT ACLVLVAFIA VGIYKKRLLL
FKKTEAAESG VSFHGNVISF SNPVLDHKPD EAVPVEYSMI QIRNENAGAS TTFENPVYEM
EENDTTNASK ASTSRSHSIS SADMRPEPSF AVIG
//