ID A0A452S818_URSAM Unreviewed; 1839 AA.
AC A0A452S818;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=LDL receptor related protein 4 {ECO:0000313|Ensembl:ENSUAMP00000028364.1};
GN Name=LRP4 {ECO:0000313|Ensembl:ENSUAMP00000028364.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000028364.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000028364.1}
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 Ensembl; ENSUAMT00000031681.1; ENSUAMP00000028364.1; ENSUAMG00000021602.1.
DR GeneTree; ENSGT00940000158287; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 5.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 5.
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; 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:UP000291022};
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 1658..1681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..422
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 469..511
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 512..554
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 555..598
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 599..641
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 774..816
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 817..859
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 860..903
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 904..946
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1082..1124
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1125..1167
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1356..1398
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1399..1441
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1485..1526
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1593..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1786..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 40..55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 60..72
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 67..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 79..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 99..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 106..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 137..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 144..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 156..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 180..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 187..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 199..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 220..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 227..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 259..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 266..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 301..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 308..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1839 AA; 204205 MW; E78FEF5BCFBC425A CRC64;
MPTPWNALFL NPECACGRSH 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
VRGVVQCTCH TGYRLTEDGH MCQDVNECAE EGYCSQGCTN SEGAFQCWCE AGYELRPDRR
SCKALGPEPV LLFANRIDIR QVLPHRSEYT LLLNNLENAI ALDFHHRREL VFWSDVTLDR
ILRANLNGSN VEEVVSTGLE SPGGLAVDWV HDKLYWTDSG TSRIEVANLD GAHRKVLLWQ
NLEKPRAIAL HPMEGTIYWT DWGNTPRIEA SSMDGSGRRI IADTHLFWPN GLTIDYAGHR
MYWVDAKHHV IERANLDGSH RKAVISQGLP HPFAITVFED SLYWTDWHTK SINSANKFTG
KNQEIIRNKL HFPMDIHTLH PQRQPAGKNR CGDNNGGCTH LCLPSGQNYT CACPTGFRKI
SSHACAQSLD KFLLFARRMD IRRISFDTED LSDDVIPLAD VRSAVALDWD SRDDHVYWTD
VSTDTISRAK WDGTGQEVVV DTSLESPAGL AIDWVTNKLY WTDAGTDRIE VANTDGSMRT
VLIWENLDRP RDIVVEPMGG YMYWTDWGAS PKIERAGMDA SGRQVIISSN LTWPNGLAID
YGSQRLYWAD AGMKTIEFAC LDGSKRKVLI GSQLPHPFGL TLYGERIYWT DWQTKSIQSA
DRLTGLDRET LQENLENLMD IHVFHRRRPP VSTPCARENG GCSHLCLRSP NPSGFSCTCP
TGINLMPDGK TCSPGMNSFL IFARRIDIRM VSLDIPYFAD VVVPINITMK NTIAIGVDPQ
EGKVYWSDST LHSISRANLD GSQHEDIITT GLQTTDGLAV DAIGRKVYWT DTGTNRIEVG
NLDGSMRKVL VWQNLDSPRA IVLYHEMGRH TLVSPVQHPY GLTLLDSYIY WTDWQTRSIH
RADKGTGSNV ILVRSNLPGL MDIQAVDRAQ PLGERTPQAV NLLKGDTPAP SSSLPGWVSK
LMRLSSPGFN KCGSRNGGCS HLCLPRPSGF SCACPTGIQL KRDGKTCDPS PETYLLFSSR
GSIRRISLDT SDHTDVHIPV PELNNVISLD YDSVDGKVYY TDVFLDVIRR ADLNGSNMET
VIGRGLKTTD GLAVDWVARN LYWTDTGRNT IEASRLDGSC RKVLINNSLD EPRAIARDPG
KKGLMKNWGH IAKIERANLD GSERKVLINT DLGWPNGLTL DYDTRRIYWV DAHLDRIESA
DLNGKLRQAL VSHVSHPFAL TQVLAQERAP RSEILSQTRH SSALPLGTNA CGVNNGGCTH
LCFARASDFV CACPDEPDDR PCSLVPGLVP PAPRATSLSE RSPVLPNTLP TTLRSSTTRT
RTSLEEVEGR CSEKDAQLGL CAHSNEAVPA APGEGLHISY VIGGLLSILL ILVVIAALML
YRHKKSKLTD PGMGNLTYSN PSYRTSTQEV KIEAIPKPAM YNQLCYKKEG GSDHNYTKEK
IKIVEGICLL SGDDAEWDDL KQLRSSRGGL LRDHVCMKTD TVSIQASSGS LDDTETEQLL
QEEQSECSSV HTAATPERRG SLPDTGWKHE RKLSSESQV
//
