ID A0A3B4UEA8_SERDU Unreviewed; 1617 AA.
AC A0A3B4UEA8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Low-density lipoprotein receptor-related protein {ECO:0000256|PIRNR:PIRNR036314};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000017006.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000017006.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 -!- SIMILARITY: Belongs to the LDLR family.
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; ENSSDUT00000017313.1; ENSSDUP00000017006.1; ENSSDUG00000012323.1.
DR GeneTree; ENSGT00940000158990; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProt.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 3.
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; IPR000742; EGF-like_dom.
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|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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036314};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Wnt signaling pathway {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 1461..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1477
FT /note="Polar 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 1617 AA; 181014 MW; 2F7E2EB19101BDF8 CRC64;
MGVVLRSLLL CSFCFLIRGV PLLLYANRRD LRLVDAAHEK ANATVVVGGL EDAAAVDYVY
SQGLIYWSDV SEEAIKRTVF NQSGASTVQT VVPGLASPDG LACDWLGRKL YWTDSETNRI
EVAELDGALR KVLFWQELDQ PRAIALDPER GYMYWTDWGE VPKIERAGMD GTNRSMIIDK
DIYWPNGLTL DYSQQKLYWA DAKHNFIHRS NLDGSSREVV VKGELPHPFA LTLYEDTLFW
TDWNTHSIHS CRKQTGGEQR VVHSDIFSPM DIHVFSSKRQ PNLNSPCSVR NGGCSHLCLL
SPVKPFYQCA CPTGVQLLED GKTCRDGATQ MLLLARRTDL RRISLDTPDF TDIILQVDDI
RHAIAIDYDP VEGYIYWTDD EVKAIRRSLP DGSDAQFVVT SQVNHPDGIA VDWIARNLYW
TDTGTDRIEV TRLNGTMRKI LISEDLDEPR AIVLDPVAGY MYWTDWGEVP KIERADLDGM
ERVVMVNTSL GWPNGLALDY DERKIYWGDA KTDMIEVMNM DGSGRRVLVE DKLPHIFGFT
LLGDYIYWTD WQRRSIERVH KRTAEREFII DQLPDLMGLK ATYVHQSFGT NPCADSNGGC
SHLCLYKPQG VQCGCPIGLE LIADMRTCIV PEAFLLFSRH TDIRRISLET NNNNVAIPLT
GVKEASALDF DVTDNRIYWT DITLKTISRA FMNGSALEHV VEFGLDYPEG MAVDWLGKNL
YWADTGTNRI EVAKLDGQHR QVLVWKDLDS PRALALDPAE GYMYWTEWGG KPKIDRAAMD
GTGRITLVAD VGRANGLTID YAERRLYWTD LDTTLIESSN MLGQEREVIA DDLPHPFGLT
QYQDYIYWTD WSQRSIERAN KTSGQNRTVI QGHLDYVMDI LVFHSSRQGG WNACASTNGH
CSHLCLAVPV SSFVCGCPAH FSLNFDNKTC SAPTSFLLFS QKTAINRMVI DEQQSPDIIL
PIHSLRNVRA IDYDPLDKQL YWIDSKQNVI RRAQEDGNQS MTVVSSSVGG ASQGLQLYDL
SIDIYSRFIY WTSEVTNVIN VTRTDGSRVG VVLRGEHDKP RAIVVNPERG YMYFTNLLER
SPKIERAALD GTEREVLFFS GLGKPVALAI DNEVGKLFWV DSDLRRIESS DLSGANRIVI
ADSNILQPVG LTVFGNHLYW IDKQQQMIER IDKTTREGRT KIQARIAYLS DIHAVHELDM
REYSKHPCTW DNGGCSHICI VKGDGTTRCS CPVHLVLLQD ELSCGEPPTC SPEQFSCTSG
EVDCIPQAWR CDGYAECDDK SDEEDCPVCS ESEFQCDSRQ CIDLSLRCNG EFNCQDRSDE
NKCEVRCPLD QFTCSNGQCI GKHKKCDNNV DCTDSSDENG CYATEEPPPP PNNTISSIVG
VVMALFVVGA VYFVCQRVLC PQMKDDGETV TNDFVVHGPS SVPLGYTHET NAPRMSRGKS
VIGSLSIMGG SSGPPYDRAH VTGASSSSSS STKGTYFPPI LNPPPSPATV RSQYTMEFGY
SSNSPSTHRS YSYRPYTYRH FAPPTTPCST DVCDSDYTPG RRAPLKSSTA ASAAAAAKGY
TSDLNYDSEP FPPPPTPRSQ YLSAEENCES CPPSPYTERS YSHHLYPPPP SPCTDSS
//
