ID A0A8C6V6F9_9GOBI Unreviewed; 1616 AA.
AC A0A8C6V6F9;
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 {ECO:0000256|PIRNR:PIRNR036314};
OS Neogobius melanostomus (round goby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Benthophilinae; Neogobiini;
OC Neogobius.
OX NCBI_TaxID=47308 {ECO:0000313|Ensembl:ENSNMLP00000043036.1, ECO:0000313|Proteomes:UP000694523};
RN [1] {ECO:0000313|Ensembl:ENSNMLP00000043036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSNMLP00000043036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
CC beta-catenin signaling through inducing aggregation of receptor-ligand
CC complexes into ribosome-sized signalosomes.
CC {ECO:0000256|PIRNR:PIRNR036314}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated oligomer
CC aggregates on Wnt-signaling. {ECO:0000256|PIRNR:PIRNR036314}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000256|ARBA:ARBA00009939,
CC ECO:0000256|PIRNR:PIRNR036314}.
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; ENSNMLT00000047789.1; ENSNMLP00000043036.1; ENSNMLG00000025485.1.
DR Proteomes; UP000694523; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:InterPro.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:TreeGrafter.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR GO; GO:0009888; P:tissue development; IEA:UniProtKB-ARBA.
DR CDD; cd00112; LDLa; 2.
DR FunFam; 2.120.10.30:FF:000001; Low-density lipoprotein receptor-related protein 6; 2.
DR FunFam; 2.120.10.30:FF:000017; Low-density lipoprotein receptor-related protein 6; 1.
DR FunFam; 2.120.10.30:FF:000241; Low-density lipoprotein receptor-related protein 6; 1.
DR FunFam; 4.10.400.10:FF:000016; Low-density lipoprotein receptor-related protein 6; 1.
DR FunFam; 4.10.400.10:FF:000074; low-density lipoprotein receptor-related protein 6; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR050778; Cueball_EGF_LRP_Nidogen.
DR InterPro; IPR000742; EGF.
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 InterPro; IPR017049; LRP5/6.
DR PANTHER; PTHR46513:SF40; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 6; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 12.
DR PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 15.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|PIRNR:PIRNR036314};
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036314};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036314};
KW Reference proteome {ECO:0000313|Proteomes:UP000694523};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR036314};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687,
KW ECO:0000256|PIRNR:PIRNR036314}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT CHAIN 20..1616
FT /note="Low-density lipoprotein receptor-related protein"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT /id="PRO_5034398405"
FT TRANSMEM 1375..1395
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT REPEAT 108..150
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 151..194
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 195..237
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 286..325
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 373..415
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 416..458
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 459..502
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 503..545
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 592..629
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 675..717
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 718..760
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 761..803
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 844..886
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 893..931
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 978..1021
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1027..1069
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1070..1114
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1115..1157
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1207..1251
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1458..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1271..1286
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1289..1301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1296..1314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1308..1323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1327..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1334..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1346..1361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1616 AA; 180779 MW; 388D3ACB2BBB3A3F CRC64;
MDVVLRSLLL CSFCFLVRAV PLLLYANRRD LRLVDVAHEK ANATVVVGGL EDAAAVDYVF
SQGFIYWSDV SEEAIKRTVY NQSGASVVQT VIAGLASPDG LACDWLGNKL YWTDSETNRI
EVAELNGSLR KVLFWQELDQ PRAIALDPAR GYMYWTDWGE IPKIERAGMD GTNRSIIIDK
EIYWPNGLTL DYSQQKLYWA DAKHNAIYRS NLDGSSREVV VKGDLPHPFA LTLYEDTLFW
TDWNTHSIHS CRKQTGGDQR IVHSNIFSPM DIHVFSPKRQ PALASPCTAN NGGCSHLCLL
SPSTPFYQCA CPTGVQLLQD DKTCRDGATQ MLLLARRTDL RHMSLDTPDF TDIILQVDDI
RHAIAIDYDP VEGYIYWTDD DIKAIRRSLV DGSDAQFVVT SQVSHPDGIA VDWIARNLYW
TDTGTDRIEV TRLNGTMRKI LIAEDLDEPR AIVLDPVAGF MYWTDWGEVP KIERADLDGM
ERVVMVNTSL GWPNGLALDY ADRKIYWGDA KTDKIEVMNM DGTNRQILVE DKLPHIFGFT
LLGDYIYWTD WQRRSIERVH KRSGEREFII DQLPDLMGLK ATYVHESFGT NPCAENNGGC
SHLCLYKPQG VQCGCPIGLE LISDMQTCIV PEAFLLFSRH TDIRRISLET NNNNVAIPLT
GVKEASALDF DVTDNRIYWT DITLKTISRA FMNGSSLEHV VEFGLDYPEG MAVDWLGKNL
YWADTGTNRI EVAKLDGQHR QVLVWKDLDS PRALALDPVE GYMYWTEWGG KPKIDRAAMD
GTGRNTLVAD VGRANGLTID YAERRLYWTD LDTTLIESSN MLGQDREVIA DDLPHPFGLT
QYQDYIYWTD WSQRSIERAN KTSGQNRTLI QGHLDYVMDI LVFHSSRQGG WNACASTNGH
CSHLCLAVPV SSYVCGCPAH FSLNYDNKTC SAPTSFLLFS QKTAINRMVI DEQQSPDIIL
PIHSLRNVRA IDYDPLDKQL YWIDSKQNVV RRAQEDGNQS MTVVSTSMAG PTQGLQLYDL
SIDIYSRFIY WTSEVTNVIN VTRTDGSRVG VVLRGEHDKP RAIVVNPERG YMYFTNLLER
SPKIERAALD GTEREVLFFS GLGKPVALAI DNEIGKLFWV DSDLRRIESS DLSGANRIVI
ADSNILQPVG LTVFGSHLYW IDKQQQMIER IDKTTREGRT KIQARIAYLS DIHAVHELDM
REYSKHPCTW DNGGCSHICI VKGDGTTRCS CPIHLVLLQD ELSCGEPPTC SPEQFSCTSG
EVDCIPQAWR CDGVAECDDS SDEDDCPVCS ESEFQCDSRQ CIDMSLRCNG EVNCQDSSDE
NKCEVRCPPD QFSCSNGQCI GKHKKCDHNM DCTDNSDELG CYPTEEPPPP PNNTISSIVG
VVLALFVVGA IYFVCQRVLC PQMKDDSETV TNDFVVHGPS SVPLGYVPHP SSLSSSLPGM
SRGKSVIGSL SIMGGSSGPP YDRAHVTGAS SSSSSSTKGT YFPPILNPPP SPATVRSQYT
MEFGYSSNSP STHRSYSYRP YTYRHFAPPT TPCSTDVCDS DYTPGRRVPL KSGTTAKGYT
SDLNYDSEPF PPPPTPRSQY LSAEENCESC PPSPYTERSY SHHLYPPPPS PCTDSS
//
