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   02-SEP-2026, entry version 176.
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,
RC   Pancreas, 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_013587.3.
DR   AlphaFoldDB; P55302; -.
DR   SMR; P55302; -.
DR   BioGRID; 201205; 10.
DR   FunCoup; P55302; 1404.
DR   IntAct; P55302; 1.
DR   STRING; 10090.ENSMUSP00000030986; -.
DR   GlyConnect; P55302; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P55302; 1 site, 1 glycan.
DR   GlyGen; P55302; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P55302; -.
DR   PhosphoSitePlus; P55302; -.
DR   REPRODUCTION-2DPAGE; IPI00469307; -.
DR   REPRODUCTION-2DPAGE; P55302; -.
DR   CPTAC; non-CPTAC-3763; -.
DR   jPOST; P55302; -.
DR   PaxDb; 10090-ENSMUSP00000030986; -.
DR   PeptideAtlas; P55302; -.
DR   ProteomicsDB; 281976; -.
DR   Pumba; P55302; -.
DR   Antibodypedia; 1334; 498 antibodies from 34 providers.
DR   DNASU; 16976; -.
DR   Ensembl; ENSMUST00000030986.15; ENSMUSP00000030986.9; ENSMUSG00000029103.17.
DR   GeneID; 16976; -.
DR   KEGG; mmu:16976; -.
DR   UCSC; uc008xdo.1; mouse.
DR   AGR; MGI:96829; -.
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; QEFEHHQ; -.
DR   OrthoDB; 5817428at2759; -.
DR   PhylomeDB; P55302; -.
DR   BioGRID-ORCS; 16976; 1 hit in 79 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 277 other cell types or tissues.
DR   ExpressionAtlas; P55302; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0048237; C:rough endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0031982; C:vesicle; ISO:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0035473; F:lipase binding; ISO:GO_Central.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:MGI.
DR   GO; GO:0048019; F:receptor antagonist activity; ISO:GO_Central.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:GO_Central.
DR   GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISO:GO_Central.
DR   GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:GO_Central.
DR   GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:GO_Central.
DR   GO; GO:0002091; P:negative regulation of receptor internalization; ISO:GO_Central.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:GO_Central.
DR   GO; GO:0048259; P:regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISO:GO_Central.
DR   CDD; cd14806; RAP_D1; 1.
DR   CDD; cd14807; RAP_D2; 1.
DR   CDD; cd14808; RAP_D3; 1.
DR   FunFam; 1.20.81.10:FF:000001; Alpha-2-macroglobulin receptor-associated protein; 1.
DR   Gene3D; 1.20.81.10; RAP domain; 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; ALPHA-2-MACROGLOBULIN RECEPTOR-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR16560:SF2; ALPHA-2-MACROGLOBULIN RECEPTOR-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF06401; Alpha-2-MRAP_C; 1.
DR   Pfam; PF06400; Alpha-2-MRAP_N; 1.
DR   SUPFAM; SSF47045; RAP domain-like; 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
//