ID A0A8C5UGW3_9PASS Unreviewed; 1849 AA.
AC A0A8C5UGW3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Low-density lipoprotein receptor-related protein 4 {ECO:0000256|ARBA:ARBA00074424};
OS Malurus cyaneus samueli.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Meliphagoidea; Maluridae; Malurus.
OX NCBI_TaxID=2593467 {ECO:0000313|Ensembl:ENSMCSP00000021932.1, ECO:0000313|Proteomes:UP000694560};
RN [1] {ECO:0000313|Ensembl:ENSMCSP00000021932.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMCSP00000021932.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms an
CC AGRIN receptor complex that binds AGRIN resulting in activation of
CC MUSK. Interacts (via the extracellular domain) with SOST; the
CC interaction facilitates the inhibition of Wnt signaling. Interacts with
CC MESD; the interaction promotes glycosylation of LRP4 and its cell-
CC surface expression. {ECO:0000256|ARBA:ARBA00061830}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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}.
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DR Ensembl; ENSMCST00000022492.1; ENSMCSP00000021932.1; ENSMCSG00000015124.1.
DR OrthoDB; 664115at2759; -.
DR Proteomes; UP000694560; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProtKB-ARBA.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR FunFam; 2.120.10.30:FF:000029; LDL receptor related protein 4; 1.
DR FunFam; 4.10.400.10:FF:000017; LDL receptor related protein 4; 2.
DR FunFam; 4.10.400.10:FF:000092; LDL receptor related protein 4; 1.
DR FunFam; 2.10.25.10:FF:000009; Low-density lipoprotein receptor isoform 1; 1.
DR FunFam; 4.10.400.10:FF:000009; Low-density lipoprotein receptor-related protein 1; 1.
DR FunFam; 2.120.10.30:FF:000008; Low-density lipoprotein receptor-related protein 4; 3.
DR FunFam; 4.10.400.10:FF:000085; low-density lipoprotein receptor-related protein 4; 1.
DR FunFam; 4.10.400.10:FF:000098; low-density lipoprotein receptor-related protein 4; 1.
DR FunFam; 4.10.400.10:FF:000113; Low-density lipoprotein receptor-related protein 8; 1.
DR FunFam; 4.10.400.10:FF:000006; Putative low-density lipoprotein receptor; 1.
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; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_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; IPR051221; LDLR-related.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR PANTHER; PTHR22722:SF15; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 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; 15.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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:UP000694560};
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};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1849
FT /note="Low-density lipoprotein receptor-related protein 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034727329"
FT TRANSMEM 1669..1690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 417..432
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 479..521
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 522..564
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 565..608
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 609..651
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 784..826
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 827..869
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 870..913
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 914..956
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1092..1134
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1135..1177
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1178..1221
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1222..1263
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1396..1438
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1439..1481
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1482..1525
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1526..1567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1795..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 70..82
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 77..95
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 89..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 109..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 116..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 147..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 154..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 166..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 197..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 209..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 230..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 237..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 249..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 269..281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 276..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 288..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 311..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 318..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1849 AA; 207553 MW; F36198DC9B1AF624 CRC64;
DRWYLFKTFF FLSSFTGVTS STECSCGRNH FTCAVSAFGE CTCIPAQWQC DGDNDCGDHS
DEDGCMLPTC SPLDFHCDNG KCIRRSWVCD GDNDCEDDSD EQDCPPRECE EDEFSCQNGY
CIRSLWHCDG DNDCGDNSDE QCDMRKCSEK EFRCSDGSCI AEHWFCDGDT DCKDGSDEEN
CPSDVPAATC SLEEFQCAYG RCILDIYHCD GDDDCGDWSD ESDCSSHQPC RSGEFMCNSG
LCINAGWRCD GDFDCDDQSD ERNCTTSMCT ADQFRCKSGR CVRLSWRCDG EDDCSDNSDE
ENCENTGTPQ CAPDQFLCGN GRCIGQRKLC NGANDCGDGS DESPHQNCRP RTGEENCNVN
NGGCAQKCQM VRGMVQCTCH TGYRLLEDGR SCQDVNECAE EGYCSQGCTN SEGGFQCWCE
QGYELRPDKR SCKALGPEPV LLFANRIDIR QVLPHRSEYT LLLNNLENAI ALDFHHSKEL
VFWSDVTLDR IMRANLNGSN VEEVVSTGLE SPGGLAIDWI HDKLYWTDSG TSRIEVANLD
GTHRKVLLWQ NLEKPRAIAL HPMEGTIYWT DWGNTPRIEY SNMDGSNRRI IADTHLFWPN
GLTIDYAGHR MYWVDAKHHV IERADLDGRN RRAVISQGLP HPFAITVFED SLYWTDWHTK
SINSANKFTG KNQEIIRNKL HFPMDIHTLH PQRQPAGRNR CGDNNGGCTH LCLPSSKDYT
CACPTGFRKT SSHACAQSLD KFLLFARRMD IRRISFDTDD LSDDVIPLAD VRSAVALDWD
SKDDYVYWTD VSTDSISRAK WDGSKQEVVV DTSLESPAGL AIDWVTNKLY WTDAGTDRIE
VSNTDGTMRT VLIWENLDRP RDIVVDPVEG YMYWTDWGAN PKIERAGMDA SNRLVIISSN
LTWPNGLAID YESQRLYWAD AGMKTIEYAG LDGSHRKVLI GNNLPHPFGL TLYGERIYWT
DWQAKSIQSA DRRTGQSRET LQDNLENLMD IHVFHRHRPP VRTACKVRNG GCSHLCLLAP
LPKGYSCTCP TGINLQSDGK TCSPGMTSFL IFARRTDIRM VSLDIPYFAD VVVSVNVTMK
NTIAIGVDPR EGKVYWSDST LRKISRASLD GSQFEDIITT GLLTTDGLAV DAIGRKIYWT
DTGTNRIEVG NLDGSMRKVL VWQNLDSPRA IALYHEMGYM YWTDWGENAK LERSGMDGSG
RVVLISNNLG WPNGLAVDKA GSQLLWADAH TERIEAADLN GANRHTLLSP VQHPYGLTLL
DSYIYWTDWQ TRSIHRADKD TGANVILVRA NLPGLMDIQA VDRARPLGFN KCGIRNGGCS
HLCLPHPTGF SCACPTGIQL KRDEQTCDSS PETYLLFSSR ASIRRISLDT SDHTDVHIPV
PELNNVISLD YDSVDGKIYY TDVFLDVIRR ADLNGSNMET VIGQGLKTTD GLAVDWVARN
LYWTDTGRNT IEVARLDGSS RKVLINNSLD EPRAIAVFPK KGYLFWTDWG HIAKIERAHL
DGSERKILIN TDLGWPNGLT LDYDTRRIYW VDAHLDRIES CDLNGKLRQV LVSQVSHPFA
LTQQDRWIYW TDWQTKSIQR VDKYSGRNKE TVLANVEGLM DIIVVSPQRQ TGTNACGVNN
GGCTHLCFAR ASDFVCACPD EPDGRPCSTS EFAECHLDSR QSYPVKYDYI IGGLLSILFI
LLLIAALIIY RHNKSKFTDP GLGNLTYSNP SYRTSTQEVK IESIPKPTMY NQLCYKKETG
PDHSYTKEKI KIVEGICLLS SDDSEWDDLK QIRSSRGGIL RDHVCMKTDT VSIQASSGSL
DDTETEQLLQ EEQSECSSVN TAAATPERRG SLPDTGWKHQ RKPSTESEV
//
