ID A0A3B3T0M4_9TELE Unreviewed; 1668 AA.
AC A0A3B3T0M4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Low-density lipoprotein receptor-related protein 5-like {ECO:0000313|Ensembl:ENSPKIP00000036210.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000036210.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000036210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; 1676925.ENSPKIP00000036210; -.
DR Ensembl; ENSPKIT00000017151.1; ENSPKIP00000036210.1; ENSPKIG00000014824.1.
DR GeneTree; ENSGT00940000156574; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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; 10.
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; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 13.
PE 4: Predicted;
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1439..1459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 171..213
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 214..257
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 258..300
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 349..388
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 436..478
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 479..521
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 522..565
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 566..608
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 655..692
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 738..780
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 781..823
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 824..866
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 907..949
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 956..993
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1131..1175
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1176..1218
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1268..1306
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1529..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1332..1347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1350..1362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1357..1375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1369..1384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1388..1400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1395..1413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1407..1422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1668 AA; 186912 MW; B3C97401473B8D89 CRC64;
MECSRKQMVD SQKDVIVCFL PFLLPLVLLP FFLAFGSPSF LLGLWFSFLS SWPLVLLPFL
SPLVLLPFFL ALSCSGSPLL LFANRRDVRL VDAEAGRAES TVVVSGLDAV AVDFLFSEGL
IFWTDVSEEA IKQTYYNQSS NAMKEATQAN KQRVVSGLDS PDGLACDWLG RKLYWTDSET
NRIEVANLDG SFRKVLFWQG LDQPRAIALN PAARYIYWTD WGEEPRIERA GMDGSNRKII
VETDIYWPNG LTIDLDEQKL YWADAKLSFI HRANLDGSSR ETVVEGTLTH PFALTLSGET
LYWTDWQTRS IHACNKQTGS KRREILGGIY SPMDIQVLSK ERQPDVQTPC RLDNGGCSHL
CLLSPTDPFY SCACPTGVRL QADGKTCSPG AEEVLLLARR TDLRRISLDL PDFTDIVLQV
DDIRHAIAID YDPVEGHIYW TDDEVKAIRR ARIDGSEAQT LVSTEISHPD GVAVDWIARN
LYWTDTGTDR IEVTRLNGTC RRILVSENLE EPRAIVLDPV RGYMYWTDWG EKPKIERANL
DGSDRLVLLN SSLGWPNGLA LDYAPGKLYW GDAKTDRIEV INIDGTGRKT LLEDKLPHIF
GFTLLGDYIY WTDWQRRSIE RVHKTEAVRE MIIDQLPDLM GLKATRVTET FGTNACATDN
GGCSHLCLHR PQGLVCACPM GLELLSDLHS CVVPEAFLLF TSRADIRSIS LGTKGNDVAI
PLSGVKEASA LDFDVSENRI YWTDVSAKTI SRAFMNGSLV EHVIEFGLDY PEGMAVDWMG
RNLYWADTGT NRIEVARLDG QYRQVLVCKD LDNPRSLALD PANGYMYWTE WGGKPRIKRA
YMDGSNIATL VDKLGRANGL TIDYVDQRLY WTDLDTCMIE SSNMLGQERE LVADDLPHPF
GLTQYRDYIY WTDWNLRSIE RADKRSGLNR TLIRGQLEYV MDILVFHASR QDGWNECSQD
NGHCSHLCLA TPEGARCRCA SHYTLEANTR NCSSPSSFLL FSQRASISRM VLGEQTPDII
LPIHVVRNVR VIRYDPVERA VYWVDGRQNI RKARDDGSES FVVLSNAPSH QQVPERQPHD
LSLDPYSRTV FWTCEVTNTI NIERLDGVSV GVVLRDEQDK PRAIVVNAEK GYMYFTTMQD
RSAKIERASL DGTERESLFT TGLIRPVALA LDNRLGKLFW VDAVLRRIES SDFSGANRIT
LQDGNILHPV GLTVLGEHLF WIDRQQQMIE RVEKVTGEKR TRVQGRLMYL TGIHAVEDMN
PEELASHPCS RGNGGCSHIC IAKGDGTPRC SCPMHLVLLQ DLLTCGEPPT CSPEQFTCAT
GEIDCIPKAW RCDGFAECDD QSDEESCPIC TTLQFQCDRG QCVEAHLRCN SEADCADSSD
EQDCDVICPP NQFRCGNGQC IEKRQQCDSY TDCMDSSDEL FCDILKPIPN DTPADSSTMW
PVVGIILSVV VMGGMYFVCQ RLVCRWYKGP SRAFPHDYIS GTPHVPLNFV DPVSSQHGNF
TGISCGKSMM GSVSLMGSSN SGAPLYDRTH VTGASSSSSS SSKAPFYPQI LNPPPSPATD
RSLYNAEIFY SSNSPSTTRS YRPYPVRGMA PPTTPCSTDV CDSDYTTSRW KSNKYYIDLN
WDSDPYPPPP TPRSQYLSAE ESCPPSPSTE HSYFHLSPPP PSPCTDSS
//
