Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Low density lipoprotein receptor adapter protein 1

Gene

Ldlrap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Endocytosis, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

ReactomeiR-RNO-171052. LDL-mediated lipid transport.
R-RNO-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-RNO-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Low density lipoprotein receptor adapter protein 1Curated
Alternative name(s):
Autosomal recessive hypercholesterolemia protein homolog1 Publication
Gene namesi
Name:Ldlrap1Imported
Synonyms:Arh1 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1563417. Ldlrap1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi55T → M: 10-fold reduced affinity for LDLR. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004384141 – 306Low density lipoprotein receptor adapter protein 1Add BLAST306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei14PhosphoserineBy similarity1
Modified residuei200PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiD3ZAR1.
PeptideAtlasiD3ZAR1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000000151.
GenevisibleiD3ZAR1. RN.

Interactioni

Subunit structurei

Interacts (via PID domain) with LDLR (via NPXY motifs) (PubMed:22509010). Binds to soluble clathrin trimers. Interacts with AP2B1; the interaction mediates the association with the AP-2 complex. Interacts with VLDLR (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Lrp2P981583EBI-9250714,EBI-9251342

Protein-protein interaction databases

DIPiDIP-60041N.
IntActiD3ZAR1. 3 interactors.
STRINGi10116.ENSRNOP00000000163.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SO6X-ray1.37A43-173[»]
SMRiD3ZAR1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 168PIDPROSITE-ProRule annotationAdd BLAST125

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni247 – 274AP-2 complex bindingBy similarityAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi210 – 214Clathrin boxBy similarity5
Motifi255 – 264[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motifBy similarity10

Domaini

The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1.By similarity
The PID domain mediates interaction with the NPXY internalization motif of LDLR.1 Publication

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3536. Eukaryota.
ENOG410ZHJT. LUCA.
GeneTreeiENSGT00530000062937.
InParanoidiD3ZAR1.
OMAiAQDIHYA.
OrthoDBiEOG091G0TOH.
TreeFamiTF314159.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZAR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDALKSAGRA LIRSPSLAKQ SWAGGRHRKL PENWTDTRET LLEGMVFSLK
60 70 80 90 100
YLGMTLVERP KGEELSAAAV KRIVATAKAS GKKLQKVTLK VSPRGIILTD
110 120 130 140 150
SLTSQLIENV SIYRISYCTA QMHDKVFAYI AQSQQNESLE CHAFLCTKRK
160 170 180 190 200
VAQAVTLTVA QAFKVAFEFW QVSKEEKEKR EKANQEGGDV PGTRRDSTPS
210 220 230 240 250
LKTSVATGNL LDLEELAKAP LSTVSANTKN MDDALRPQVL GNNSVVWELD
260 270 280 290 300
DGLDEAFSRL AQSRTNPQVL DTGLTAQDIH YAQCLSPTDW DKPDSSGFDQ

DDVFSF
Length:306
Mass (Da):33,785
Last modified:April 3, 2013 - v2
Checksum:iFD73C718AED585F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07050129 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000000163; ENSRNOP00000000163; ENSRNOG00000000151.
UCSCiRGD:1563417. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07050129 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SO6X-ray1.37A43-173[»]
SMRiD3ZAR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60041N.
IntActiD3ZAR1. 3 interactors.
STRINGi10116.ENSRNOP00000000163.

Proteomic databases

PaxDbiD3ZAR1.
PeptideAtlasiD3ZAR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000163; ENSRNOP00000000163; ENSRNOG00000000151.
UCSCiRGD:1563417. rat.

Organism-specific databases

RGDi1563417. Ldlrap1.

Phylogenomic databases

eggNOGiKOG3536. Eukaryota.
ENOG410ZHJT. LUCA.
GeneTreeiENSGT00530000062937.
InParanoidiD3ZAR1.
OMAiAQDIHYA.
OrthoDBiEOG091G0TOH.
TreeFamiTF314159.

Enzyme and pathway databases

ReactomeiR-RNO-171052. LDL-mediated lipid transport.
R-RNO-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-RNO-8856828. Clathrin-mediated endocytosis.

Gene expression databases

BgeeiENSRNOG00000000151.
GenevisibleiD3ZAR1. RN.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARH_RAT
AccessioniPrimary (citable) accession number: D3ZAR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2016
Last sequence update: April 3, 2013
Last modified: November 30, 2016
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.