ID A0A2K6GZR5_PROCO Unreviewed; 1922 AA.
AC A0A2K6GZR5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=LDL receptor related protein 4 {ECO:0000313|Ensembl:ENSPCOP00000031675.1};
GN Name=LRP4 {ECO:0000313|Ensembl:ENSPCOP00000031675.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000031675.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000031675.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 379532.ENSPCOP00000031675; -.
DR Ensembl; ENSPCOT00000042634.1; ENSPCOP00000031675.1; ENSPCOG00000028608.1.
DR GeneTree; ENSGT00940000158287; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IEA:Ensembl.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IEA:Ensembl.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IEA:Ensembl.
DR GO; GO:0097105; P:presynaptic membrane assembly; IEA:Ensembl.
DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
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; 2.
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; 4.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1922
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014318674"
FT TRANSMEM 1741..1764
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..1467
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1500..1543
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1544..1585
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1678..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1922
FT /note="Basic and acidic residues"
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 1922 AA; 214262 MW; F759FEB32A1C445F CRC64;
TKSGTWALNG SFCLCPGLAS SPECACGRSH FTCAVSALGE CTCIPAQWQC DGDNDCGDHS
DEDGCMLPTC SPLDFHCDNG KCIRRSWVCD GDNDCEDDSD EQDCPPRECE EDEFPCQNGY
CIRSLWHCDG DNDCGDNSDE QCDMRKCSDK EFRCSDGSCI AEHWYCDGDT DCKDGSDEES
CPSAVPAPPC NLEEFQCAYG RCILDIYHCD GDDDCGDWSD ESDCSSHQPC RSGEFMCDSG
LCINAGWRCD GDADCDDQSD ERNCTTSMCT AEQFRCRSGR CVRLSWRCDG EDDCADNSDE
ENCENTGSPQ CASDQFLCWN GRCIGQRKLC NGVNDCGDNS DESPQQNCRP RTGEENCNVN
NGGCAQKCQM VRGAVQCTCH TGYRLTEDGR TCQDVNECAE EGYCSQGCTN SEGAFQCWCE
TGYELRPDRR SCKALGPEPV LLFANRIDIR QVLPHRSEYT LLLNNLENAI ALDFHHRREL
VFWSDVTLDR ILRANLNGSN VEEVVSTGLE SPGGLAVDWV HDKLYWTDSG TSRIEVANLD
GAHRKVLLWQ NLEKPRAIAL HPMEGTIYWT DWGNTPRIEA SSMDGSGRRI IADTHLFWPN
GLTIDYAGRR MYWVDAKHHV IERANLDGSH RKAVISQGLP HPFAITVFED SLYWTDWHTK
SINSANKFTG KNQEIIRNKL HFPMDIHTLH PQRQPAGKNR CGDNNGGCTH LCLPSGQNYT
CACPTGFRKI NSHACAQSLD KFLLFARRMD IRRISFDTED LSDDVIPLAD VRSAVALDWD
SRDDHVYWTD VSTDTISRAK WDGTGQEVVV DTSLESPAGL AIDWVTNKLY WTDAGTDRIE
VANTDGSMRT VLIWENLDRP RDIVVEPMGG YMYWTDWGAS PKIERAGMDA SERRVIISSN
LTWPNGLAID YGSQRLYWAD AGMKTIEFAG LDGSKRKVLI GSQLPHPFGL TLYGERIYWT
DWQTKSIQSA DRLTGLDRET LQENLENLMD IHVFHRRRPP VSTPCAMENG GCSHLCLRSP
NPNGFSCTCP TGINLLPDGK TCSPGMNSFL IFARRIDVRM VSLDIPYFAD VVVPINVTMK
NTIAIGVDPQ EGKVYWSDST LHRISRANLD GSQHEDIITT GLQTTDGLAV DAIGRKVYWT
DTGTNRIEVG NLDGSMRKVL VWQNLDSPRA IVLYHEMGFM YWTDWGENAK LERSGMDGSE
RTVLINNNLG WPNGLTVDKA SSQLLWADAH TERIEAADLN GANRHTLVSP VQHPYGLTLL
DSYIYWTDWQ TRSIHRADKS TGSNVILVRS NLPGLMDIQA VDRAQPLGFN KCGSRNGGCS
HLCLPRPSGF SCACPTGIQL KGDGKTCDPS PETYLLFSSR GSIRRISLDT SDHTDVHVPV
PELNNVISLD YDSVDGKVYY TDVFLDVIRR ADLNGSNMET VIGRGLKTTD GLAVDWVARN
LYWTDTGRNT IEASRLDGSC RKVLINNIYG QQKRDPREKR LGSCISLVLM CPCVLSTSWV
YLFWTDWGHI AKIERANLDG SERKVLINTD LGWPNGLTLD YDTRRIYWVD AHLDRIESAD
LNGKLRQVLV SHVSHPFALT QQDRWIYWTD WQTKSIQRVD KYSGRNKETV LANVEGLMDI
IVVSPQRQTG TNACGVNNGG CTHLCFARAL DFVCACPDEP DGRPCFLVPG LVPPDPRATS
MSEKSPVLPN TLPTTLHSST TRTRTSLEEV EGRCSERDAR LGLCAHSNEA VPAAPGEGLH
ISYAIGGLLS ILLILVVIAA LMLYRHKKSK FTDPGMGNLT YSNPSYRTST QEVKIEAIPK
PAMYNQLCYK KEGGPDHNYT KEKIKIVEGI CLLSGDDAEW DDLKQLRSSR GGLLRDHVCM
KTDTVSIQAS SGSLDDTETE QLLQEEQSEC SSVHTTATPE RRGSLSDTGW KHERKLSSES
QV
//
