AMRP_MOUSE
ID AMRP_MOUSE Reviewed; 360 AA.
AC P55302;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Alpha-2-macroglobulin receptor-associated protein;
DE Short=Alpha-2-MRAP;
DE AltName: Full=Heparin-binding protein 44;
DE Short=HBP-44;
DE AltName: Full=Low density lipoprotein receptor-related protein-associated protein 1;
DE Short=RAP;
DE Flags: Precursor;
GN Name=Lrpap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8282724; DOI=10.1093/oxfordjournals.jbchem.a124179;
RA Nakamoto M., Ozawa M., Jacinto S.D., Furukawa T., Natori Y., Shirahama H.,
RA Yonezawa S., Nakayama T., Muramatsu T.;
RT "Mouse heparin binding protein-44 (HBP-44) associates with brushin, a high-
RT molecular-weight glycoprotein antigen common to the kidney and
RT teratocarcinomas.";
RL J. Biochem. 114:344-349(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-360, AND TISSUE SPECIFICITY.
RX PubMed=2229028; DOI=10.1093/oxfordjournals.jbchem.a123197;
RA Furukawa T., Ozawa M., Huang R.P., Muramatsu T.;
RT "A heparin binding protein whose expression increases during
RT differentiation of embryonal carcinoma cells to parietal endoderm cells:
RT cDNA cloning and sequence analysis.";
RL J. Biochem. 108:297-302(1990).
RN [3]
RP PROTEIN SEQUENCE OF 310-322, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Molecular chaperone for LDL receptor-related proteins that
CC may regulate their ligand binding activity along the secretory pathway.
CC {ECO:0000250|UniProtKB:P30533}.
CC -!- SUBUNIT: Interacts with the LRP1/alpha-2-macroglobulin receptor heavy
CC and light chains; the interaction is transient and coincides with a
CC reduction of ligand binding by the receptor. Interacts with
CC LRP2/glycoprotein 330. Interacts with LRP1B; binding is followed by
CC internalization and degradation. Interacts with LDLR. Interacts with
CC SORL1 (By similarity). Interacts with LRP1; this interaction is
CC followed by rapid internalization (By similarity).
CC {ECO:0000250|UniProtKB:P30533}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P30533}. Endoplasmic reticulum-Golgi
CC intermediate compartment lumen {ECO:0000250|UniProtKB:P30533}. Golgi
CC apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P30533}. Golgi
CC apparatus lumen {ECO:0000250|UniProtKB:P30533}. Endosome lumen
CC {ECO:0000250|UniProtKB:P30533}. Cell surface
CC {ECO:0000250|UniProtKB:P30533}. Note=May be associated with receptors
CC at the cell surface. {ECO:0000250|UniProtKB:P30533}.
CC -!- TISSUE SPECIFICITY: Highly expressed in PYS-2 parietal endoderm cells
CC and in the kidney. The RNA level increased about 10-fold during
CC differentiation of F9 embryonal carcinoma cells to parietal endoderm
CC cells. {ECO:0000269|PubMed:2229028}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30533}.
CC -!- SIMILARITY: Belongs to the alpha-2-MRAP family. {ECO:0000305}.
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DR EMBL; S67967; AAC60668.1; -; mRNA.
DR EMBL; D00622; BAA00500.1; -; mRNA.
DR CCDS; CCDS19225.1; -.
DR PIR; JX0281; JX0281.
DR RefSeq; NP_038615.2; NM_013587.2.
DR AlphaFoldDB; P55302; -.
DR SMR; P55302; -.
DR BioGRID; 201205; 9.
DR IntAct; P55302; 1.
DR STRING; 10090.ENSMUSP00000030986; -.
DR GlyConnect; 2121; 1 N-Linked glycan (1 site).
DR GlyGen; P55302; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P55302; -.
DR PhosphoSitePlus; P55302; -.
DR REPRODUCTION-2DPAGE; IPI00469307; -.
DR REPRODUCTION-2DPAGE; P55302; -.
DR CPTAC; non-CPTAC-3763; -.
DR EPD; P55302; -.
DR jPOST; P55302; -.
DR PaxDb; P55302; -.
DR PeptideAtlas; P55302; -.
DR PRIDE; P55302; -.
DR ProteomicsDB; 281976; -.
DR Antibodypedia; 1334; 500 antibodies from 32 providers.
DR DNASU; 16976; -.
DR Ensembl; ENSMUST00000030986; ENSMUSP00000030986; ENSMUSG00000029103.
DR GeneID; 16976; -.
DR KEGG; mmu:16976; -.
DR UCSC; uc008xdo.1; mouse.
DR CTD; 4043; -.
DR MGI; MGI:96829; Lrpap1.
DR VEuPathDB; HostDB:ENSMUSG00000029103; -.
DR eggNOG; KOG3956; Eukaryota.
DR GeneTree; ENSGT00390000004855; -.
DR HOGENOM; CLU_064512_0_0_1; -.
DR InParanoid; P55302; -.
DR OMA; LHSKHAE; -.
DR OrthoDB; 908725at2759; -.
DR PhylomeDB; P55302; -.
DR TreeFam; TF320678; -.
DR BioGRID-ORCS; 16976; 1 hit in 74 CRISPR screens.
DR PRO; PR:P55302; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P55302; protein.
DR Bgee; ENSMUSG00000029103; Expressed in vestibular membrane of cochlear duct and 274 other tissues.
DR ExpressionAtlas; P55302; baseline and differential.
DR Genevisible; P55302; MM.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0048237; C:rough endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0035473; F:lipase binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:MGI.
DR GO; GO:0048019; F:receptor antagonist activity; ISO:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:MGI.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISO:MGI.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR CDD; cd14806; RAP_D1; 1.
DR CDD; cd14807; RAP_D2; 1.
DR CDD; cd14808; RAP_D3; 1.
DR Gene3D; 1.20.81.10; -; 3.
DR InterPro; IPR038003; A2-macroglobuin_RAP.
DR InterPro; IPR010483; Alpha_2_MRAP_C.
DR InterPro; IPR009066; MG_RAP_rcpt_1.
DR InterPro; IPR038001; RAP_D2.
DR InterPro; IPR037999; RAP_D3.
DR InterPro; IPR036744; RAP_sf.
DR PANTHER; PTHR16560; PTHR16560; 1.
DR Pfam; PF06401; Alpha-2-MRAP_C; 1.
DR Pfam; PF06400; Alpha-2-MRAP_N; 1.
DR SUPFAM; SSF47045; SSF47045; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Golgi apparatus; Heparin-binding; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..360
FT /note="Alpha-2-macroglobulin receptor-associated protein"
FT /id="PRO_0000020725"
FT REGION 240..356
FT /note="LDL receptor binding"
FT /evidence="ECO:0000255"
FT COILED 184..302
FT /evidence="ECO:0000255"
FT MOTIF 357..360
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250|UniProtKB:P30533"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99068"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 360 AA; 42215 MW; 72ED46FA0AC05D51 CRC64;
MAPRRERVST LPRLQLLVLL LLPLMLVPQP IAGHGGKYSR EKNEPEMAAK RESGEEFRME
KLNQLWEKAK RLHLSPVRLA ELHSDLKIQE RDELNWKKLK VEGLDKDGEK EAKLIHNLNV
ILARYGLDGR KDAQMVHSNA LNEDTQDELG DPRLEKLWHK AKTSGKFSSE ELDKLWREFL
HYKEKIQEYN VLLDTLSRAE EGYENLLSPS DMAHIKSDTL ISKHSELKDR LRSINQGLDR
LRKVSHQGYG STTEFEEPRV IDLWDLAQSA NFTEKELESF REELKHFEAK IEKHNHYQKQ
LEISHQKLKH VESIGDPEHI SRNKEKYVLL EEKTKELGYK VKKHLQDLSS RVSRARHNEL
