ID G1NAP4_MELGA Unreviewed; 1595 AA.
AC G1NAP4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Low-density lipoprotein receptor-related protein {ECO:0000256|PIRNR:PIRNR036314};
GN Name=LRP5 {ECO:0000313|Ensembl:ENSMGAP00000009617.1};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009617.1, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000009617.1, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000009617.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ENSMGAT00000010446.2; ENSMGAP00000009617.1; ENSMGAG00000009268.2.
DR GeneTree; ENSGT00940000156574; -.
DR HOGENOM; CLU_002489_0_0_1; -.
DR InParanoid; G1NAP4; -.
DR OMA; HTPCEDN; -.
DR TreeFam; TF315253; -.
DR Proteomes; UP000001645; Chromosome 5.
DR Bgee; ENSMGAG00000009268; Expressed in liver and 16 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0006865; P:amino acid transport; IEA:Ensembl.
DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl.
DR GO; GO:0008078; P:mesodermal cell migration; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0110135; P:Norrin signaling pathway; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
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:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 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; 13.
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; 13.
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, ECO:0000256|PIRNR:PIRNR036314};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036314};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR036314};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR036314};
KW Wnt signaling pathway {ECO:0000256|PIRNR:PIRNR036314}.
FT TRANSMEM 1366..1386
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR036314"
FT REPEAT 98..140
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 141..184
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 185..227
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 276..315
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 363..405
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 406..448
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 449..492
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 493..535
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 582..619
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 665..707
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 708..750
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 751..793
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 794..835
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 883..920
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1059..1103
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1104..1146
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1196..1234
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 984..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1260..1275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1278..1290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1285..1303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1297..1312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1316..1328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1323..1341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1335..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1595 AA; 178857 MW; DD47FF864D1041C7 CRC64;
YVFVFSSVAS PFLLFANRRD VRLVDAGGTK LESTVVVSGL EDAAAVDFQY SQGIVFWTDV
SEEAIKQTYI NQTGNVVQNV IISGLVSPDG LACDWIGKKL YWTDSETNRI EVANLNGTSR
KVLFWQDLDQ PRAIALDPAH GYMYWTDWGE TPRIERAGMD SSTRKIIVDS DIYWPNGLTI
DLDEQKLYWA DAKLSFIHRA NLDGSFRQKV VEGSLTHPFA LTLSGDTLYW TDWQTRSIHA
CNKRTGEKRR EILSALYSPM DIQVLSPDRQ PYFHTPCEEN NGGCSHLCLL SPRDPFYSCA
CPTGVQLEDD GRTCKSGAEE VLLLARRTDL RRISLDMPDF TDIILQIDNI RHAIAIDYDP
VEGYIYWTDD DVRAIRRAYL DGSGAQTLVT TEINHPDGIA VDWVARNLYW TDTGTDRIEV
TRLNGTSRKI LISENLDEPR AIVLNPVMGY MYWTDWGESP KIECAYLDGS ERRVLVNTSL
GWPNGLALDL EEDKLYWGDA KTDKIEVINV DGTMRKTLLE DKLPHIFGFT LLGDYIYWTD
WQRRSIERVH KIRASRDIII DQLPDLMGLK ATSVTKVFGT NPCAENNGGC SHLCFFTPQE
TRCACPIGLE LLSDMKTCII PEAFLVFTSR AAIHRISLET NNNDVAIPLT GVKEASALDF
DVSDNRIYWT DVSLKTISRA FMNGSSVEHV IEFGLDYPEG MAVDWMGKNL YWADTGTNRI
EVARLDGQYR QVLVWKDLDN PRSLALDPTK GYMYWTEWGG KPRIVRAYMD GTNSITLVDK
VGRANDLTID YADQRLYWTD LDTSMIESSN MLGQEREIIA DDLPHPFGLT QYSDYIYWTD
WNLHSIERAD KTSGKNRTLI QGHLDFVMDI LVFHSSRQDG LNDCVQNNGH CGHLCLAIPN
GFRCGCAAHY TLDPNSRNCS SPTSFLLFSQ KSAISRMIPD DQQSPDIILP MHGLRNVKAI
DYDPLDKLIY WVDGRQNIIK RAKDDGTQPF TVMSSPNQSQ NPEKQPHDLS IDIYSHTLYW
TCEATNSVNV HRLNGESIGM VLRGDHDKPR AIVVNAERGY MYFTNMQERA PKIERAALDG
TEREVLFTTG LIRPVALVID NKLGKLFWVD ADLKRIESCD LSGANRVTLE DSNILQPMGL
TVLGNHLYWI DRQQQMIERV EKTNGYKRTR IQGRIAHLTG IHAVEELDME EFSAHPCSRD
NGGCSHICIA KGDGTPRCSC PEHLVLLQNL LTCGEPPTCS PDQFTCATGE IDCIPMAWRC
DGFPECDDQS DEDSCPICSA SQFQCEKGQC IDAHLRCNGE IDCQDKSDEV DCDTICLLNQ
FRCASGQCIL LKQQCDSFPD CIDGSDELMC EKSKPSSDEP QPHSSAIGPV IGIILSLFVM
GGMYFVCQRV VCQRYAGPNS PFPHEYVSGT PHVPLNFIAP GSSQHGTFTG ISCGKSMISS
MSLMGGSSGA PLYDRNHVTG ASSSSSSSTK ATFYPQILNP PPSPATDRSL YNAEMFYSSN
IPSTTRSYRP YLIRGTAPPT TPCSTDVCDS DYTTSRWKAN KYYIDLNSDS DPYPPPPTPR
SQYMSAEESC PPSPATERSY FHLYPPPPSP CTDSS
//
