LRP12_PONAB
ID LRP12_PONAB Reviewed; 859 AA.
AC Q5R662; Q5R5Y1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Low-density lipoprotein receptor-related protein 12;
DE Short=LRP-12;
DE Flags: Precursor;
GN Name=LRP12;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R662-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R662-2; Sequence=VSP_035578;
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; CR860634; CAH92754.1; -; mRNA.
DR EMBL; CR860720; CAH92835.1; -; mRNA.
DR RefSeq; NP_001126606.1; NM_001133134.1.
DR RefSeq; NP_001128879.1; NM_001135407.1.
DR AlphaFoldDB; Q5R662; -.
DR STRING; 9601.ENSPPYP00000021104; -.
DR Ensembl; ENSPPYT00000021947; ENSPPYP00000021104; ENSPPYG00000018813. [Q5R662-2]
DR Ensembl; ENSPPYT00000042947; ENSPPYP00000032230; ENSPPYG00000018813. [Q5R662-1]
DR GeneID; 100173603; -.
DR KEGG; pon:100173603; -.
DR CTD; 29967; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000158307; -.
DR HOGENOM; CLU_013747_0_0_1; -.
DR InParanoid; Q5R662; -.
DR OMA; DQFHCGN; -.
DR OrthoDB; 135036at2759; -.
DR TreeFam; TF332149; -.
DR Proteomes; UP000001595; Chromosome 8.
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; 2.
DR CDD; cd00112; LDLa; 5.
DR Gene3D; 2.60.120.290; -; 2.
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; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF57424; SSF57424; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coated pit; Disulfide bond; Endocytosis;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..859
FT /note="Low-density lipoprotein receptor-related protein 12"
FT /id="PRO_0000352672"
FT TOPO_DOM 33..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..159
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 165..201
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 214..255
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 259..372
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 374..411
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 412..449
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 450..486
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 623..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..76
FT /evidence="ECO:0000250"
FT DISULFID 103..122
FT /evidence="ECO:0000250"
FT DISULFID 166..178
FT /evidence="ECO:0000250"
FT DISULFID 173..191
FT /evidence="ECO:0000250"
FT DISULFID 185..200
FT /evidence="ECO:0000250"
FT DISULFID 215..232
FT /evidence="ECO:0000250"
FT DISULFID 222..245
FT /evidence="ECO:0000250"
FT DISULFID 239..254
FT /evidence="ECO:0000250"
FT DISULFID 259..285
FT /evidence="ECO:0000250"
FT DISULFID 375..388
FT /evidence="ECO:0000250"
FT DISULFID 382..401
FT /evidence="ECO:0000250"
FT DISULFID 395..410
FT /evidence="ECO:0000250"
FT DISULFID 413..426
FT /evidence="ECO:0000250"
FT DISULFID 420..439
FT /evidence="ECO:0000250"
FT DISULFID 433..448
FT /evidence="ECO:0000250"
FT DISULFID 451..463
FT /evidence="ECO:0000250"
FT DISULFID 458..476
FT /evidence="ECO:0000250"
FT DISULFID 470..485
FT /evidence="ECO:0000250"
FT VAR_SEQ 27..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035578"
FT CONFLICT 66
FT /note="W -> R (in Ref. 1; CAH92835)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="R -> S (in Ref. 1; CAH92835)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="Q -> H (in Ref. 1; CAH92754)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="N -> S (in Ref. 1; CAH92754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 95035 MW; 37902D89FFDC02C2 CRC64;
MARRWSTKES PRWRSALLLL FLAGVYGNGA LAEHSENVHI SGVSTACGET PEQIRAPSGI
ITSPGWPSEY PAKINCSWFI RANPGEIITI SFQDFDIQGS RRCNLDWLTI ETYKNIESYR
ACGSTIPPPY ISSQDHIWIR FHSDDNISRK GFRLAYFSGK SEEPNCACDQ FRCGNGKCIP
EAWKCNNMDE CGDSSDEEIC AKEANPPTAA AFQPCAYNQF QCLSRFTKVY TCLPESLKCD
GNIDCLDLGD EIDCDVPTCG QWLKYFYGTF NSPNYPDFYP PGSNCTWLID TGDHRKVILR
FTDFKLDGTG YGDYVKIYDG LEENPHKLLR VLTAFDSHAP LTVVSSSGQI RVHFCADKVN
AARGFNATYQ VDGFCLPWEI PCGGNWGCYT EQQRCDGYWH CPNGRDEINC TMCQKEEFPC
SRNGVCYPRS DRCNYQNHCP NGSDEKNCFF CQPGNFHCKN NRCVFESWVC DSQDDCGDGS
DEENCPVIVP TRVITAAVIG SLICGLLLVI ALGCTCKLYS LRMFERRSFE TQLSRVEAEL
LRREAPPSYG QLIAQGLIPP VEDFPVCSPN QASVLENLRL AVRSQLGFTS VRLPMAGRSS
NIWNRIFNFA RSRHSGSLAL VSADGDEVVP SQSTSREPER NHTHRSLFSV ESDDTDTENE
RRDMAGASGG VAAPLPQKVP PTTAVEATVG ACASSSTQST RGGHADNGRD VTSVEPPSVS
PARHQLTSAL SRMTQGLRWV RFTLGRSSSV SQNQSPLRQL DNGVSGREDD DDVEMLIPIS
DGSSDFDVND CSRPLLDLAS DQGQGLRQPY NATNPGVRPS NRDGPCERCG IVHTAQIPDT
CLEVTLKNET SDDEALLLC
