ID I3MDK2_ICTTR Unreviewed; 750 AA.
AC I3MDK2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=LDL receptor related protein 3 {ECO:0000313|Ensembl:ENSSTOP00000008470.3};
GN Name=LRP3 {ECO:0000313|Ensembl:ENSSTOP00000008470.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008470.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008470.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|ARBA:ARBA00037878}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; AGTP01062942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MDK2; -.
DR STRING; 43179.ENSSTOP00000008470; -.
DR Ensembl; ENSSTOT00000009443.3; ENSSTOP00000008470.3; ENSSTOG00000009443.3.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000160021; -.
DR HOGENOM; CLU_013747_1_0_1; -.
DR InParanoid; I3MDK2; -.
DR OrthoDB; 2916406at2759; -.
DR TreeFam; TF332149; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
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:SF22; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 3; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 4.
PE 4: Predicted;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 477..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..139
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 234..345
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 617..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..731
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 146..158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 153..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 165..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 214..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 417..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 435..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 442..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 454..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 750 AA; 80851 MW; 869B34A424E6B680 CRC64;
MSPTVNLFLT GKLSSAVPAL AACSGKLEQH TERRGVIYSP AWPLNYPPGT NCSWYIQGDR
GDMITISFRN FDVEESHQCS LDWLLLGPAA PPRQEAFRLC GSAIPPAFIS ARDHVWIFFH
SDASSSGQAQ GFRLSYIRGK LGQVSCQPDE FRCDNGKCLP GPWQCNTVDE CGDGSDEGNC
SAPASEPPGS LCPGGTFPCS GARSTRCLPV ERRCDGTQDC GDGSDEAGCP DLACGRRLGS
FYGSFASPDL FGAARGPSDL HCTWLVDTQD PRRVLLQLEL RLGYDDYVQV YEGLGERGDR
LLQTLSYRSN HRPVSLEAAQ GRLTVAYHAR ARSAGHGFNA TYQVKGYCLP WEQPCGSSSE
GDDSGTGDQG CFSEPQRCDG WWHCASGRDE QGCPACPPDQ YPCEGGSGLC YAPADRCNNQ
KSCPDGADEK NCFSCQPGTF HCGTNLCIFE TWRCDGQEDC QDGSDEHGCL AAVPRKVITA
ALIGSLVCGL LLVIALGCAF KLYSLRTQEY RAFETQMTRL EAEFVRREAP PSYGQLIAQG
LIPPVEDFPV YSASQASVLQ NLRTAMRRQM RRHASRRGPS RRRLGRLWNR LFHRPRAPRG
QIPLLTAART SQTVLGDGLL QPAPGAAPDP PASHTDTGSP RAAGDGPPSA PGHAPEVGTS
VSPAPSGLRD PEYGPVNKDR KACREPLVDS PAPPDTIPEP CLAQDPYPQA PTASSTPDPH
PPEPLEVCRS SPPPCSPTLE ASDDEALLVC
//
