ID LRP12_MACFA Reviewed; 701 AA.
AC Q9BE74;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Low-density lipoprotein receptor-related protein 12;
DE Short=LRP-12;
DE Flags: Fragment;
GN Name=LRP12; ORFNames=QnpA-21564;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable receptor, which may be involved in the
CC internalization of lipophilic molecules and/or signal transduction. May
CC act as a tumor suppressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with RACK1, ZFYVE9 and NMRK2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Membrane, coated pit {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB39320.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB056772; BAB39320.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q9BE74; -.
DR SMR; Q9BE74; -.
DR STRING; 9541.ENSMFAP00000009963; -.
DR GlyCosmos; Q9BE74; 4 sites, No reported glycans.
DR eggNOG; KOG1215; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF67; PROLOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1-LIKE PROTEIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 2: Evidence at transcript level;
KW Coated pit; Disulfide bond; Endocytosis; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN <1..701
FT /note="Low-density lipoprotein receptor-related protein 12"
FT /id="PRO_0000191078"
FT TOPO_DOM <1..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 7..43
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 56..97
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 101..214
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 216..253
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 254..291
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 292..328
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 465..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 8..20
FT /evidence="ECO:0000250"
FT DISULFID 15..33
FT /evidence="ECO:0000250"
FT DISULFID 27..42
FT /evidence="ECO:0000250"
FT DISULFID 57..74
FT /evidence="ECO:0000250"
FT DISULFID 64..87
FT /evidence="ECO:0000250"
FT DISULFID 81..96
FT /evidence="ECO:0000250"
FT DISULFID 101..127
FT /evidence="ECO:0000250"
FT DISULFID 217..230
FT /evidence="ECO:0000250"
FT DISULFID 224..243
FT /evidence="ECO:0000250"
FT DISULFID 237..252
FT /evidence="ECO:0000250"
FT DISULFID 255..268
FT /evidence="ECO:0000250"
FT DISULFID 262..281
FT /evidence="ECO:0000250"
FT DISULFID 275..290
FT /evidence="ECO:0000250"
FT DISULFID 293..305
FT /evidence="ECO:0000250"
FT DISULFID 300..318
FT /evidence="ECO:0000250"
FT DISULFID 312..327
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 701 AA; 77032 MW; 72DB95B2B690DE8D CRC64;
GKSEEPNCAC DQFRCGNGKC IPEAWKCNNM DECGDSSDEE ICAKEANPPT ATAFQPCAYN
QFQCLSRFTK VYTCLAESLK CDGNIDCLDL GDEIDCDVPT CGQWLKYFYG TFNSPNYPDF
YPPGSNCTWL IDTGDHRKVI LCFTDFKLDG TGYGDYVKIY DGLEENPHKL LRVLTAFDSH
APLTVVSSSG QIRVHFCADK VNAARGFNAT YQVDGFCLPW EIPCGGNWGC YTEQQRCDGY
WHCPNGRDEI NCTMCQKEEF PCSRNGVCYP RSDRCNYQNH CPNGSDEKNC FFCQPGNFHC
KNNRCVFESW VCDSQDDCGD GSDEENCPVI VPTRVITAAV IGSLICGLLL VIALGCTCKL
YSLRMFERRS FETQLSRVEA ELLRREAPPS YGQLIAQGLI PPVEDFPVCS PNQASVLENL
RLAVRSQLGF TSVRLPMAGR SSNIWNRIFN FARSRHSGSL ALVSADGDEV VPSQSTSREP
ERNHTHRSLF SVESDDTDTE NERRDTAGAS GGVAAPLPQK VPPTTAVEAT VGACASSSTQ
SARGGHADNG RDVTSVEPPS VSPARHQLTS ALSRMTQGLR WVRFTLGRSS SVSQNQSPLR
QLDNGVSGRE DDDDVEMLIP VSDGSSDFDV NDCSRPLLDL ASDQGQGLRQ PYSATNPGVR
PSNRDGPCER CGIVHTAQIP DTCLEVTLKN ETSDDEALLL C
//
