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Q8C142

- ARH_MOUSE

UniProt

Q8C142 - ARH_MOUSE

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Protein

Low density lipoprotein receptor adapter protein 1

Gene

Ldlrap1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications

GO - Molecular functioni

  1. beta-amyloid binding Source: BHF-UCL
  2. clathrin binding Source: UniProtKB
  3. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  4. phosphotyrosine binding Source: UniProtKB
  5. receptor binding Source: MGI
  6. signaling adaptor activity Source: Ensembl

GO - Biological processi

  1. amyloid precursor protein metabolic process Source: Ensembl
  2. cholesterol homeostasis Source: MGI
  3. cholesterol metabolic process Source: UniProtKB-KW
  4. positive regulation of receptor-mediated endocytosis Source: UniProtKB
  5. receptor internalization Source: Ensembl
  6. receptor-mediated endocytosis of low-density lipoprotein particle involved in cholesterol transport Source: Ensembl
  7. regulation of establishment of protein localization to plasma membrane Source: Ensembl
  8. regulation of protein binding Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Low density lipoprotein receptor adapter protein 1
Alternative name(s):
Autosomal recessive hypercholesterolemia protein homolog
Gene namesi
Name:Ldlrap1
Synonyms:Arh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2140175. Ldlrap1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. AP-1 adaptor complex Source: Ensembl
  2. AP-2 adaptor complex Source: Ensembl
  3. axon Source: Ensembl
  4. basal plasma membrane Source: UniProtKB
  5. cytoplasm Source: BHF-UCL
  6. cytoplasmic side of plasma membrane Source: Ensembl
  7. cytosol Source: UniProtKB
  8. early endosome Source: MGI
  9. neurofilament Source: BHF-UCL
  10. recycling endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are extremely sensitive to cholesterol intake. LDLR are expressed at normal levels, but are sequestered at the hepatocyte surface. LDL internalization defect is caused by the inability of the LDLR to enter the endocytic cycle.1 Publication

Keywords - Diseasei

Atherosclerosis, Hyperlipidemia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Low density lipoprotein receptor adapter protein 1PRO_0000064676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8C142.
PaxDbiQ8C142.
PRIDEiQ8C142.

PTM databases

PhosphoSiteiQ8C142.

Expressioni

Gene expression databases

BgeeiQ8C142.
ExpressionAtlasiQ8C142. baseline and differential.
GenevestigatoriQ8C142.

Interactioni

Subunit structurei

Interacts with LDLR. Binds to soluble clathrin trimers. Interacts with AP2B1; the interaction mediates the association with the AP-2 complex. Interacts with VLDLR.1 Publication

Protein-protein interaction databases

BioGridi221366. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8C142.
SMRiQ8C142. Positions 42-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 195155PIDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 27528AP-2 complex bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi211 – 2155Clathrin box
Motifi256 – 26510[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

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

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG305324.
GeneTreeiENSGT00530000062937.
HOGENOMiHOG000030906.
HOVERGENiHBG058060.
InParanoidiQ8C142.
KOiK12474.
OMAiWELDDGL.
OrthoDBiEOG7RZ5QP.
TreeFamiTF314159.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C142-1 [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 DKMHDKVFAY IAQSQQNESL ECHAFLCTKR
160 170 180 190 200
KVAQAVTLTV AQAFKVAFEF WQVSKEEKEK REKANQEGGD VPGTRRDSTP
210 220 230 240 250
SLKTLVATGN LLDLEEVAKA PLSTVSANTN NVDETPRPQV LGNNSVVWEL
260 270 280 290 300
DDGLDEAFSR LAQSRTNPQV LDTGLSAQDI HYAQCLSPTD WDKPDSSGID

QDDDVFTF
Length:308
Mass (Da):33,975
Last modified:July 27, 2011 - v3
Checksum:i4183DA9594FD1F2C
GO

Sequence cautioni

The sequence AAH21467.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601R → K in BAC26238. (PubMed:16141072)Curated
Sequence conflicti296 – 2961S → G in AAH66808. (PubMed:15489334)Curated
Sequence conflicti296 – 2961S → G in AAH67411. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029008 mRNA. Translation: BAC26238.1.
AK148340 mRNA. Translation: BAE28493.1.
AK159800 mRNA. Translation: BAE35380.1.
AK167290 mRNA. Translation: BAE39396.1.
AL645531 Genomic DNA. Translation: CAM17037.1.
CH466552 Genomic DNA. Translation: EDL30001.1.
BC021467 mRNA. Translation: AAH21467.1. Different initiation.
BC066808 mRNA. Translation: AAH66808.1.
BC067411 mRNA. Translation: AAH67411.1.
CCDSiCCDS51327.1.
RefSeqiNP_663529.2. NM_145554.2.
XP_006538486.1. XM_006538423.1.
UniGeneiMm.482148.

Genome annotation databases

EnsembliENSMUST00000037828; ENSMUSP00000036749; ENSMUSG00000037295.
GeneIDi100017.
KEGGimmu:100017.
UCSCiuc012dmx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029008 mRNA. Translation: BAC26238.1 .
AK148340 mRNA. Translation: BAE28493.1 .
AK159800 mRNA. Translation: BAE35380.1 .
AK167290 mRNA. Translation: BAE39396.1 .
AL645531 Genomic DNA. Translation: CAM17037.1 .
CH466552 Genomic DNA. Translation: EDL30001.1 .
BC021467 mRNA. Translation: AAH21467.1 . Different initiation.
BC066808 mRNA. Translation: AAH66808.1 .
BC067411 mRNA. Translation: AAH67411.1 .
CCDSi CCDS51327.1.
RefSeqi NP_663529.2. NM_145554.2.
XP_006538486.1. XM_006538423.1.
UniGenei Mm.482148.

3D structure databases

ProteinModelPortali Q8C142.
SMRi Q8C142. Positions 42-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 221366. 1 interaction.

PTM databases

PhosphoSitei Q8C142.

Proteomic databases

MaxQBi Q8C142.
PaxDbi Q8C142.
PRIDEi Q8C142.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037828 ; ENSMUSP00000036749 ; ENSMUSG00000037295 .
GeneIDi 100017.
KEGGi mmu:100017.
UCSCi uc012dmx.1. mouse.

Organism-specific databases

CTDi 26119.
MGIi MGI:2140175. Ldlrap1.

Phylogenomic databases

eggNOGi NOG305324.
GeneTreei ENSGT00530000062937.
HOGENOMi HOG000030906.
HOVERGENi HBG058060.
InParanoidi Q8C142.
KOi K12474.
OMAi WELDDGL.
OrthoDBi EOG7RZ5QP.
TreeFami TF314159.

Miscellaneous databases

NextBioi 354215.
PROi Q8C142.
SOURCEi Search...

Gene expression databases

Bgeei Q8C142.
ExpressionAtlasi Q8C142. baseline and differential.
Genevestigatori Q8C142.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view ]
Pfami PF00640. PID. 1 hit.
[Graphical view ]
SMARTi SM00462. PTB. 1 hit.
[Graphical view ]
PROSITEi PS01179. PID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: C3H/He and CD-1.
    Tissue: Mammary gland, Neural stem cell and Osteoblast.
  5. "Normal sorting but defective endocytosis of the low density lipoprotein receptor in mice with autosomal recessive hypercholesterolemia."
    Jones C., Hammer R.E., Li W.-P., Cohen J.C., Hobbs H.H., Herz J.
    J. Biol. Chem. 278:29024-29030(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LDLR AND VLDLR.
  6. "The modular adaptor protein ARH is required for low density lipoprotein (LDL) binding and internalization but not for LDL receptor clustering in coated pits."
    Michaely P., Li W.-P., Anderson R.G.W., Cohen J.C., Hobbs H.H.
    J. Biol. Chem. 279:34023-34031(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiARH_MOUSE
AccessioniPrimary (citable) accession number: Q8C142
Secondary accession number(s): Q3TW86, Q6NWV6, Q8VDQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3