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   25-MAY-2022, entry version 87.
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.XP_005563960.1; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 2.60.120.290; -; 1.
DR   Gene3D; 4.10.400.10; -; 5.
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   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; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF57424; SSF57424; 5.
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