ID A0A3Q1G5H7_9TELE Unreviewed; 1639 AA.
AC A0A3Q1G5H7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Low-density lipoprotein receptor-related protein 5-like {ECO:0000313|Ensembl:ENSAPOP00000013545.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000013545.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000013545.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; 80966.ENSAPOP00000013545; -.
DR Ensembl; ENSAPOT00000032462.1; ENSAPOP00000013545.1; ENSAPOG00000016483.1.
DR GeneTree; ENSGT00940000156574; -.
DR InParanoid; A0A3Q1G5H7; -.
DR OrthoDB; 3107655at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035676; P:anterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; 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 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; 11.
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; 14.
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 Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1639
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018740529"
FT TRANSMEM 1393..1413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 120..162
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 163..206
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 207..249
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 298..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 385..427
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 428..470
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 471..514
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 515..557
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 604..641
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 687..729
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 730..778
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 779..821
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 822..863
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 912..949
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1041..1083
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1084..1128
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1129..1171
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1221..1259
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1485..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1285..1300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1303..1315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1310..1328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1322..1337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1341..1353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1348..1366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1360..1375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1639 AA; 182779 MW; 97E4EB99052CE339 CRC64;
MDLQRRGLEM GILLVLLLLS VVDGSPFLLF ANRRDVRLVD ADGVRGESAI VVSDLEDAAA
VDFLYAEGLI FWTDVSEEAI KQTYWNQSSN SFKEALGTGQ TVVISGLDSP DGLACDWLGK
KLYWTDSETN RIEVANLDGT SRKVLFWMDL DQPRAIALNP AQRYMYWTDW GEEPRIERAG
MDGSNRKVIV NVDIYWPNGL TIDLVEQKLY WADAKLSFIH RANLDGSSRE TVVEGTLTHP
FALTLSEETL YWTDWQTRSI HACNKHSGDK TREILSGIYS PMDIQVLEPY RQPYIQTPCS
ENNGGCSHLC LLSPVHPFYS CACPTGVQLK PDGKTCKPGA EQVLLLARRT DLRRISLDLP
DFTDIVLQVD DIRHAIAIDY DPVEGYVYWT DDEVRAIRRS HIDGSNAMML VTTEINHPDG
IAVDWVARNL YWTDTGTDRI EVTRLNGTSR KILISENLDE PRAIVLDPVA GFMYWTDWGE
HPKIERANLD GTDRVVLLNS SLGWPNGLAI DYAAGKLYWG DAKTDKIEVI NVDGSNRQIL
LEDKLPHIFG FTLLGDYIYW TDWQRRSIER VHKATAVREI IIDQLPDLMG LKATKVTETY
GTNGCAMDNG GCSHLCFWRQ QAVSCACPMG MELLSDLHTC VVPEAFLLFT NRDNIRSISL
GTNSNDVAIP LTGVKEASAL DFDVSERRIY WTDIQAKTIS RAYMNGSSVE HVIEFGLDYP
EGMAVDWMGR NIYWADTGTN RIEVSRLDGQ HRQVLVCKDL DNPRSLDNPR SLALDPANGY
MYWTEWGGRP RIARAYMDGS TIMTLVDKVG RANGLTIDYV DHRLYWTDLD TCMIESTNMQ
GLQREIIVDD LPHPFGLTQY RDFIYWTDFN LRSIERAEKR SGLNRTVVLQ GQLELMLDIL
VFHSSRQDGT NECLHNNGNC AHLCLASPAG ARCRCASHYT LNHDGRNCSS PSSFLLFSQK
ASISRMVLGE QSPDIILPIH VLRNVRGVNY DPLDRLVYWL DGRQNIRRAR DDGAMSSMIL
SSTAHPVDNQ LHDLSLDPYS RHIYWTCETT NTINVQRMDG HTVGVVIKDD TDKPRAIVVN
AEKGYMYFTT VQERSAKIEG ASLDGTERES LFTTGLIRPV ALALDNKLGK LFWVDADLKR
IESSDLTGAN RVVLQDSNIL QPMGLTVLGD HLYWIDRQQQ MIERVGKLTG DGRTRIQGRI
SYLTSIHAVE EMDPQEFASH PCSRDNGGCS HICIAKGDGT PRCSCPMHLV LLQDLLHCGE
PPTCSTEQFT CSTGEIDCIP MAWRCDGLPE CEDSSDEDNC PVCSAFQFQC NKGGCIDAQR
RCNGEPDCAD HSDEQDCETI CPPNQFRCGD NQCITKKQQC DNFSDCPDGS DELACENVSP
PSVGISNTGP STIAPVIAII LLVFVIGGAY FVCQRVVCRR YKGPSGTFPH EYISGTPHVP
LNFITPSSSQ HATFQGISCG KSMMSSVSLM GSSSSGAPLY DRNHVTGASS SSSSSTKGVF
YPQILNPPPS PATDRSLYNT EIFYSSNSPS TTRSYRPYHP VRGTAPPTTP CSTDVCDSDY
TPHHPLAGLA SSAGRWKASN HGKHKYYMDL NSDSDPYPPP PTPRSQYMSA EESCPPSPST
ERSYFHLCPP PPSPCTDSS
//
