ID M4AAA6_XIPMA Unreviewed; 977 AA.
AC M4AAA6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Low-density lipoprotein receptor-related protein 8-like {ECO:0000313|Ensembl:ENSXMAP00000011400.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000011400.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000011400.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000011400.1};
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 AlphaFoldDB; M4AAA6; -.
DR Ensembl; ENSXMAT00000011414.2; ENSXMAP00000011400.1; ENSXMAG00000011361.2.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000154819; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR Proteomes; UP000002852; 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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF3; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 8; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 4.
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:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..977
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004047770"
FT TRANSMEM 892..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 380..394
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT DOMAIN 419..434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 481..526
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 527..569
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 570..613
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 614..658
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 765..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 31..43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 38..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
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 132..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 154..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 161..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 173..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 193..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 200..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 326..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 977 AA; 107610 MW; FB6DBD4EC2A4B00C CRC64;
MWTGVGKLVL LHLLLMELSG HAKGTHTESE CEIGQFQCKS GVCIPSLWRC DDDNDCSDSS
DEENCPKKTC ATTDFACKNG QCLPARWRCD GEPECADGSD EADAICSRQT CPPEKFDCGG
VASKCVSLSW RCDGERDCEN GADEEECPAD ENACPSKDFH CRNGKCVAPI FVCDGDDDCG
DASDEDKCSS PTCGQHEFRC NDSECIPALW SCDGDPDCKD KSDESMERCS RRTEPQKPGC
PGEFQCSSGE CVHMHWKCDG DADCKDKSDE ANCPLLTCRP DEFQCGDGSC IHGTKQCNKV
HDCPDYSDEA GCVNVTKCDG PKKFRCKNGE CIDSSKVCDS VKDCKDWSDE PVKECGLNEC
ADNNGGCSHI CRDRRIGYEC DCPSGYKLLD KKTCGDIDEC ENPDACSQIC INYKGDYKCE
CYEGYEMDPA SKTCKAVGKS PCLMFTNRHE IRRIDLLKSE YTQVVPTLKN AVALDVDVST
NKMFWCDLYH RKIYSAYINK ASDSSQQVTL VDSLHSPEGL AVDWVHKNIY WTDSGNKSIS
VATGDGRKRK VLIATELSEP RAIAVDPHQG FMYWSDWGDQ AKIEKAGMNG VDRQVLVSDH
IEWPNGITLD LSNRRLYWVD SKLHLLSSVD LNGDNRKVLL SSHHHLGHPF ALTVFEDRVY
WTDLEDEAIY SANRLTGHDV AKVAEDLNNP LDLVVFHEQR QPKAPDTCNM GSLPNGGCEY
LCLKAPQITD HSPKYTCACP DGMELGPDMR RCAVVRIRTT TTVAPTTTST TIATTTTATT
TTTTSPATST TTRTPTTTST TTSAATPPRT TTRHHMTPKP PQTSRSSRIT QPPVTQAATS
TEATSLSSTS QMSTQTPLLD PVAPDSIQRE TNANLSHRAA SDHYLIGNNI TVAVLGIVIP
IVPILATVVI GLLCTGGYLV WRNWRRKNTK SMNFDNPVYR KTTEDDDDEI HIGRHSDSIG
HVYPPRVALS LEDDGYP
//
