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Q99068 (AMRP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2-macroglobulin receptor-associated protein

Short name=Alpha-2-MRAP
Alternative name(s):
Gp330-binding 45 kDa protein
Low density lipoprotein receptor-related protein-associated protein 1
Short name=RAP
Gene names
Name:Lrpap1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.

Subunit structure

Present on cell surface forming a complex with the alpha-2-macroglobulin receptor heavy and light chains. Binds LRP1B; binding is followed by internalization and degradation By similarity.

Subcellular location

Endoplasmic reticulum By similarity. Cytoplasm By similarity. Cell surface By similarity. Note: Intracellular and associated with cell surface receptors. Found in the endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the alpha-2-MRAP family.

Caution

Was originally (Ref.3) thought to be Heymann nephritis antigen gp330.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 360327Alpha-2-macroglobulin receptor-associated protein
PRO_0000020726

Regions

Region240 – 356117LDL receptor binding Potential
Coiled coil222 – 30281 Potential
Motif357 – 3604Prevents secretion from ER Potential

Amino acid modifications

Glycosylation2711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict38 – 403YSR → RSA in AAA41269. Ref.3
Sequence conflict166 – 17914KFSSE…LWREF → ISVRLTSCARV Ref.3
Sequence conflict248 – 2503GYG → LR in AAA41269. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99068 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: C7CF5ECCE1BCC5DC

FASTA36042,032
        10         20         30         40         50         60 
MAPLRDRVST LPRLQLLVLL LLPLLLVPQP IAGHGGKYSR EKNEPEMAAK RESGEEFRME 

        70         80         90        100        110        120 
KLNQLWEKAK RLHLSPVRLA ELHSDLKIQE RDELNWKKLK VEGLDGDGEK EAKLVHNLNV 

       130        140        150        160        170        180 
ILARYGLDGR KDTQTVHSNA LNEDTQDELG DPRLEKLWHK AKTSGKFSSE ELDKLWREFL 

       190        200        210        220        230        240 
HYKEKIHEYN VLLDTLSRAE EGYENLLSPS DMTHIKSDTL ASKHSELKDR LRSINQGLDR 

       250        260        270        280        290        300 
LRKVSHQGYG PATEFEEPRV IDLWDLAQSA NFTEKELESF REELKHFEAK IEKHNHYQKQ 

       310        320        330        340        350        360 
LEISHQKLKH VESIGDPEHI SRNKEKYVLL EEKTKELGYK VKKHLQDLSS RVSRARHNEL 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney and Placenta.
[2]"Analysis of a 45-kDa protein that binds to the Heymann nephritis autoantigen GP330."
Kanalas J.J., Makker S.P.
J. Biol. Chem. 268:8188-8192(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-360.
Strain: Sprague-Dawley.
Tissue: Kidney.
[3]"Molecular cloning of a cDNA encoding a major pathogenic domain of the Heymann nephritis antigen gp330."
Pietromonaco S., Kerjaschki D., Binder S., Ullrich R., Farquhar M.G.
Proc. Natl. Acad. Sci. U.S.A. 87:1811-1815(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-360.
[4]"39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor."
Herz J., Goldstein J.L., Strickland D.K., Ho Y.K., Brown M.S.
J. Biol. Chem. 266:21232-21238(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-51.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC082020 mRNA. Translation: AAH82020.1.
BC098947 mRNA. Translation: AAH98947.1.
Z11994 mRNA. Translation: CAA78040.1.
Z11995 mRNA. Translation: CAA78041.1.
M31051 mRNA. Translation: AAA41269.1.
PIRA46646.
RefSeqNP_001162584.1. NM_001169113.1.
UniGeneRn.10293.

3D structure databases

ProteinModelPortalQ99068.
SMRQ99068. Positions 38-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99068. 2 interactions.
MINTMINT-4611866.

PTM databases

PhosphoSiteQ99068.

Proteomic databases

PaxDbQ99068.
PRIDEQ99068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012665; ENSRNOP00000012665; ENSRNOG00000009313.
GeneID116565.
KEGGrno:116565.

Organism-specific databases

CTD4043.
RGD620700. Lrpap1.

Phylogenomic databases

eggNOGNOG323629.
GeneTreeENSGT00390000004855.
HOGENOMHOG000033926.
HOVERGENHBG000197.
InParanoidQ99068.
OMAFRMAKLN.
OrthoDBEOG7P5T15.
PhylomeDBQ99068.
TreeFamTF320678.

Gene expression databases

GenevestigatorQ99068.

Family and domain databases

Gene3D1.20.81.10. 1 hit.
InterProIPR010483. Alpha_2_MRAP_C.
IPR009066. MG_RAP_rcpt_1.
[Graphical view]
PfamPF06401. Alpha-2-MRAP_C. 1 hit.
PF06400. Alpha-2-MRAP_N. 1 hit.
[Graphical view]
SUPFAMSSF47045. SSF47045. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619245.
PROQ99068.

Entry information

Entry nameAMRP_RAT
AccessionPrimary (citable) accession number: Q99068
Secondary accession number(s): Q4FZX8, Q642A1, Q64723
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families