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Q8C142

- ARH_MOUSE

UniProt

Q8C142 - ARH_MOUSE

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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. protein binding Source: BHF-UCL
    6. receptor binding Source: MGI
    7. 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

    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

    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

    ArrayExpressiQ8C142.
    BgeeiQ8C142.
    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.
    InParanoidiQ3TW86.
    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

    MDALKSAGRA LIRSPSLAKQ SWAGGRHRKL PENWTDTRET LLEGMVFSLK    50
    YLGMTLVERP KGEELSAAAV KRIVATAKAS GKKLQKVTLK VSPRGIILTD 100
    SLTSQLIENV SIYRISYCTA DKMHDKVFAY IAQSQQNESL ECHAFLCTKR 150
    KVAQAVTLTV AQAFKVAFEF WQVSKEEKEK REKANQEGGD VPGTRRDSTP 200
    SLKTLVATGN LLDLEEVAKA PLSTVSANTN NVDETPRPQV LGNNSVVWEL 250
    DDGLDEAFSR LAQSRTNPQV LDTGLSAQDI HYAQCLSPTD WDKPDSSGID 300
    QDDDVFTF 308
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 Q3TW86.
    KOi K12474.
    OMAi WELDDGL.
    OrthoDBi EOG7RZ5QP.
    TreeFami TF314159.

    Miscellaneous databases

    NextBioi 354215.
    PROi Q8C142.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C142.
    Bgeei Q8C142.
    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

    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 1, 2014
    This is version 101 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