ID A0A218V9I0_9PASE Unreviewed; 1911 AA.
AC A0A218V9I0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Low-density lipoprotein receptor-related protein 4 {ECO:0000313|EMBL:OWK62586.1};
GN Name=LRP4_0 {ECO:0000313|EMBL:OWK62586.1};
GN ORFNames=RLOC_00009870 {ECO:0000313|EMBL:OWK62586.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK62586.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK62586.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK62586.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK62586.1}.
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DR EMBL; MUZQ01000024; OWK62586.1; -; Genomic_DNA.
DR STRING; 299123.ENSLSDP00000023585; -.
DR Proteomes; UP000197619; 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; 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; 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; 3.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 14.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 4.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Lipoprotein {ECO:0000313|EMBL:OWK62586.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:OWK62586.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1911
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012804199"
FT TRANSMEM 1731..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..444
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 491..533
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 534..576
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 577..620
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 621..663
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 796..838
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 839..879
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 880..923
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 924..966
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1102..1144
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1145..1187
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1188..1231
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1232..1273
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1406..1448
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1449..1491
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1492..1535
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1536..1577
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1659..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 62..77
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 82..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 89..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 101..116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 121..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 128..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 159..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 166..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 178..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 202..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 209..227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 221..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 242..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 249..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 261..276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 281..293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 288..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 300..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 323..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1911 AA; 213237 MW; D4ABBF81B06A1CB2 CRC64;
MRRRGGGCLL PAPPQLLLVL LGALLRSRGV TSSTECSCGR NHFTCAVSAF GECTCIPAQW
QCDGDNDCGD HSDEDGCMLP TCSPLDFHCD NGKCIRRSWV CDGDNDCEDD SDEQDCPPRE
CEEDEFSCQN GYCIRSLWHC DGDNDCGDNS DEQCDMRKCS EKEFRCSDGS CIAEHWFCDG
DTDCKDGSDE ENCPSDVPAA TCSLEEFQCA YGRCILDIYH CDGDDDCGDW SDESDCSSHQ
PCRSGEFMCN SGLCINAGWR CDGDFDCDDQ SDERNCTTSM CTADQFRCKS GRCVRLSWRC
DGEDDCSDNS DEENCENTGT PQCASDQFLC GNGRCIGQRK LCNGANDCGD GSDESPHQNC
RPRTGEENCN VNNGGCAQKC QMVRGMVQCT CHTGYRLLED GRSCQDVNEC AEEGYCSQGC
TNSEGGFQCW CEQGYELRPD KRSCKALGPE PVLLFANRID IRQVLPHRSE YTLLLNNLEN
AIALDFHHSK ELVFWSDVTL DRIMRANLNG SNVEEVVSTG LESPGGLAID WIHDKLYWTD
SGTSRIEVAN LDGTHRKVLL WQNLEKPRAI ALHPMEGTIY WTDWGNTPRI EYSNMDGSNR
RIIADTHLFW PNGLTIDYAG HRMYWVDAKH HVIERADLDG RNRKAVISQG LPHPFAITVF
EDSLYWTDWH TKSINSANKF TGKNQEIIRN KLHFPMDIHT LHPQRQPAGR NRCGDNNGGC
THLCLPSSKD YTCACPTGFR KTSSHACAQS LDKFLLFARR MDIRRISFDT DDLSDDVIPL
ADVRSAVALD WDSKDDYVYW TDVSTDSISR AKWDGSNQEV VVDTSLESPA GLAIDWVTNK
LYWTDADRIE VSNTDGTMRT VLIWENLDRP RDIVVDPIGG FMYWTDWGAN PKIERAGMDA
SNRLVIISSN LTWPNGLAID YESQRLYWAD AGMKTIEYAS LDGSHRKVLI GSNLPHPFGL
TLYGERIYWT DWQAKSIQSA DRRSGQSRET LQDNLENLMD IHVFHRHRPP VHTACEVNNG
GCSHLCLLAP LPKGYSCTCP TGINLQSDGK TCSPGMTSFL IFARRTDIRM VSLDIPYFAD
VVVSVNVTMK NTIAIGVDPH EGKVYWSDST LRKISRAALD GSQFEDIITT GLLTTDGLAV
DAIGRKIYWT DTGTNRIEVG NLDGSMRKVL VWQNLDSPRA IALYHEMGYM YWTDWGENAK
LERSGMDGSG RVVLISNNLG WPNGLAVDKA GSQLLWADAH TERIEAADLN GAHRHTLLSP
VQHPYGLTLL DSYIYWTDWQ TRSIHRADKD TGANVILVRA NLPGLMDIQA VDRARPLGFN
KCGVRNGGCS HLCLPHPTGF SCACPTGIQL KRDEQTCDSS PETYLLFSSR ASIRRISLDT
SDHTDVHIPV PELNNVISLD YDSVDGKIYY TDVFLDVIRR ADLNGSNMET VIGQGLKTTD
GLAVDWVARN LYWTDTGRNT IEVARLDGSS RKVLINNSLD EPRAIAVFPK KGYLFWTDWG
HIAKIERANL DGSERKILIN TDLGWPNGLT LDYDTRRIYW VDAHLDRIES CDLHGKLRQV
LVSQVSHPFA LTQQDRWIYW TDWQTKSIQR VDKYSGRNKE TVLANVEGLM DIIVVSPQRQ
TGSNACGVNN GGCTHLCFAR ASDFVCACPD EPDGRPCSTI PGVVPPGPEP TSKSERSQTL
PGRLGTSTTK PLTSLETVER NCSDKDARQG LCTRANEAVL ATMGEGLHVS YIIGGLLSIL
FILLLIAALI IYRHNKSKFT DPGLGNLTYS NPSYRTSTQE VKIESIPKPT MYNQLCYKKE
TGPDHSYTKE KIKIVEGICL LSSDDSEWDD LKQIRSSRGG ILRDHVCMKT DTVSIQASSG
SLDDTETEQL LQEEQSECSS VNTAAATPER RGSLPDTGWK HQRKPSTESE V
//
