ID A0A2K6AF35_MANLE Unreviewed; 1822 AA.
AC A0A2K6AF35;
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:ENSMLEP00000038679.1};
GN Name=LRP4 {ECO:0000313|Ensembl:ENSMLEP00000038679.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038679.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000038679.1}
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; 9568.ENSMLEP00000038679; -.
DR Ensembl; ENSMLET00000062293.1; ENSMLEP00000038679.1; ENSMLEG00000043395.1.
DR GeneTree; ENSGT00940000158287; -.
DR Proteomes; UP000233140; 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:UniProtKB-KW.
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; 6.
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; 13.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
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; 13.
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:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1641..1664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 419..434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 481..523
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 524..566
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 567..610
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 611..653
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 786..833
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1010..1052
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1053..1095
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1096..1139
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1140..1181
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1314..1356
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1357..1399
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1400..1443
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1444..1485
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1576..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 64..76
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 71..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 149..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 156..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 168..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 199..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 211..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 232..244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 251..266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 271..283
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 313..325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 320..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1822 AA; 203440 MW; 69F960156ADD3E3B CRC64;
ERMEWGREQL GLASSPECAC GRSHFTCAVS ALGECTCIPA QWQCDGDNDC GDHSDEDGCM
LPTCSPLDFH CDNGKCIRRS WVCDGDNDCE DDSDEQDYPH CLQQPDSPRE CEEDEFPCQN
GYCIRSLWHC DGDNDCGDNS DEQCDMRKCS DKEFRCSDGS CIAEHWYCDG DTDCKDGSDE
ESCPSAVPAP PCNLEEFQCA YGRCILDIYH CDGDDDCGDW SDESDCSSHQ PCRSGEFMCD
SGLCINAGWR CDGDADCDDQ SDERNCTTSM CTAEQFRCRS GRCVRLSWRC DGEDDCADNS
DEENCENTGS PQCASDQFLC WNGRCIGQRK LCNGVNDCGD NSDESPQQNC RPRTGEENCN
VNNGGCAQKC QMVRGAVQCT CHTGYRLTED GHTCQDVNEC ADEGYCSQGC TNSEGAFQCW
CETGYELRPD RRSCKALGPE PVLLFANRID IRQVLPHRSE YTLLLNNLEN AIALDFHHRR
ELVFWSDVTL DRILRANLNG SNVEEVVSTG LESPGGLAVD WVHDKLYWTD SGTSRIEVAN
LDGAHRKVLL WQNLEKPRAI ALHPMEGTIY WTDWGNTPRI EASSMDGSGR RIIADTHLFW
PNGLTIDYAG RRMYWVDAKH HVIERANLDG SHRKAVISQG LPHPFAITVF EDSLYWTDWH
TKSINSANKF TGKNQEIIRN KLHFPMDIHT LHPQRQPAGK NRCGDNNGGC THLCLPSGQN
YTCACPTGFR KISSHACAQS LDKFLLFARR MDIRRISFDT EDLSDDVIPL ADVRSAVALD
WDSRDDHVYW TDVSTDTIST DRIEVANTDG SMRTVLIWEN LDRPRDIVEK WPNLMDIQGI
KSNFVEDDTV LGPWQVLIGS QLPHPFGLTL YGERIYWTDW QTKSIQSADR LTGLDRETLQ
ENLENLMDIH VFHRRRPPVS TPCAMENGGC SHLCLRSPNP SGFSCTCPTG INLLPDGKTC
SPGMNSFLIF ARRIDIRMVS LDIPYFADVV VPINITMKNT IAIGVDPQEG KVYWSDSTLH
RISRANLDGS QHEDIITTGL QTTDGLAVDA IGRKVYWTDT GTNRIEVGNL DGSMRKVLVW
QNLDSPRAIV LYHEMGFMYW TDWGENAKLE RSGMDGSDRT VLISNNLGWP NGLTVDKASS
QLLWADAHTE RIEAADLNGA NRHTLVSPVQ HPYGLTLLDS HIYWTDWQTR SIHRADKGTG
SNVILVRSNL PGLMDIQAVD RAQPLGFNKC GSRNGGCSHL CLPRPSGFSC ACPTGIQLKG
DGKTCDPSPE TYLLFSSRGS IRRISLDTSD HTDVHVPVPE LNNVISLDYD SVDGKVYYTD
VFLDVIRRAD LNGSNMETVI GRGLKTTDGL AVDWVARNLY WTDTGRNTIE ASRLDGSCRK
VLINNSLDEP RAIAVFPRKG YLFWTDWGHI AKIERANLDG SERKVLINTD LGWPNGLTLD
YDTRRIYWVD AHLDRIESAD LNGKLRQVLV SHVSHPFALT QQDRWIYWTD WQTKSIQRVD
KYSGRNKETV LANVEGLMDI IVVSPQRQTG TNACGVNNGG CTHLCFARAS DFVCACPDER
DSRPCSLVPG LVPPAPRSTG MSEKSPVLPN TLPTTLHSST TRTRMSLEEV EGRCSERDAR
LGLCARSNEA VPAAPGEGLH ISYAIGGLLS ILLILVVIAA LMLYRHKKSK FTDPGMGNLT
YSNPSYRTST QEVKIEAIPK PAMYNQLCYK KEGGPDHNYT KEKIKIVEGI CLLSGDDAEW
DDLKQLRSSR GGLLRDHVCM KTDTVSIQAS SGSLDDTETE QLLQEEQSEC SSVHTAATPE
RRGSLPDTGW KHERKLSSES QV
//
