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Q6PHU5

- SORT_MOUSE

UniProt

Q6PHU5 - SORT_MOUSE

Protein

Sortilin

Gene

Sort1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi.7 Publications

    GO - Molecular functioni

    1. nerve growth factor receptor activity Source: Ensembl
    2. neurotensin receptor activity, non-G-protein coupled Source: Ensembl
    3. protein binding Source: IntAct

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. endosome to lysosome transport Source: Ensembl
    3. endosome transport via multivesicular body sorting pathway Source: Ensembl
    4. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    5. glucose import Source: BHF-UCL
    6. Golgi to endosome transport Source: Ensembl
    7. multicellular organismal development Source: UniProtKB-KW
    8. myotube differentiation Source: BHF-UCL
    9. negative regulation of lipoprotein lipase activity Source: Ensembl
    10. neuropeptide signaling pathway Source: Ensembl
    11. neurotrophin TRK receptor signaling pathway Source: Ensembl
    12. ossification Source: UniProtKB-KW
    13. plasma membrane to endosome transport Source: Ensembl
    14. regulation of gene expression Source: Ensembl
    15. response to insulin Source: BHF-UCL
    16. vesicle organization Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation, Endocytosis, Osteogenesis, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sortilin
    Alternative name(s):
    Neurotensin receptor 3
    Short name:
    NTR3
    Short name:
    mNTR3
    Gene namesi
    Name:Sort1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1338015. Sort1.

    Subcellular locationi

    Membrane Curated; Single-pass type I membrane protein Curated. Endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated. Endosome membrane Curated; Single-pass type I membrane protein Curated. Golgi apparatusGolgi stack membrane Curated; Single-pass type I membrane protein Curated. Nucleus membrane Curated; Single-pass type I membrane protein Curated. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane Curated; Single-pass type I membrane protein Curated
    Note: Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. Interaction with NRADD promotes localization at the cell membrane in neurons; this promotes interaction with NGFR. Also found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes is enhanced by insulin.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. coated pit Source: Ensembl
    3. early endosome Source: Ensembl
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. endosome membrane Source: UniProtKB-SubCell
    6. Golgi cisterna membrane Source: UniProtKB-SubCell
    7. integral component of membrane Source: UniProtKB-KW
    8. lysosomal membrane Source: UniProtKB-SubCell
    9. nuclear membrane Source: UniProtKB-SubCell
    10. perinuclear region of cytoplasm Source: Ensembl
    11. plasma membrane Source: BHF-UCL
    12. trans-Golgi network transport vesicle Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 7544Removed in mature formBy similarityPRO_0000045155Add
    BLAST
    Chaini76 – 825750SortilinPRO_0000045156Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi84 ↔ 554By similarity
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi255 ↔ 275By similarity
    Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi446 ↔ 456By similarity
    Glycosylationi580 – 5801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi610 ↔ 649By similarity
    Disulfide bondi632 ↔ 664By similarity
    Disulfide bondi666 ↔ 721By similarity
    Disulfide bondi673 ↔ 686By similarity
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi700 ↔ 738By similarity
    Modified residuei813 – 8131PhosphoserineBy similarity
    Modified residuei819 – 8191Phosphoserine1 Publication

    Post-translational modificationi

    The N-terminal propeptide is cleaved by furin and possibly other homologous proteases.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ6PHU5.
    PaxDbiQ6PHU5.
    PRIDEiQ6PHU5.

    PTM databases

    PhosphoSiteiQ6PHU5.

    Expressioni

    Tissue specificityi

    Expressed in the brain, particularly the piriform cortex, the cerebral cortex and the hippocampus.1 Publication

    Developmental stagei

    Expressed in the ectoderm at E7.5 and within the germ cell layers at E8.5. Expressed within the neural epithelium and the neural tube at E9.5 and subsequently expressed in the nervous system throughout development. Expression in the proliferative zones of the central nervous system declines between E14.5 and E16.5, while expression remains high in the cerebral cortex and the neural retina. Expressed in the pituitary and the sensory epithelia throughout development.1 Publication

    Inductioni

    During adipocyte differentiation.2 Publications

    Gene expression databases

    ArrayExpressiQ6PHU5.
    BgeeiQ6PHU5.
    CleanExiMM_SORT1.
    GenevestigatoriQ6PHU5.

    Interactioni

    Subunit structurei

    Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, NTS and GM2A. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate their anterograde axonal transport and signaling By similarity. Interacts with LPL, PSAP and SLC2A4. Interacts with NRADD and NGFR. Interaction with NRADD protects against degradation in the lysosome.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NraddQ8CJ265EBI-6985663,EBI-6985725

    Protein-protein interaction databases

    BioGridi203393. 1 interaction.
    DIPiDIP-46095N.
    IntActiQ6PHU5. 4 interactions.
    MINTiMINT-4130555.
    STRINGi10090.ENSMUSP00000088052.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PHU5.
    SMRiQ6PHU5. Positions 86-747.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 754723ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini776 – 82550CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei755 – 77521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati143 – 15412BNR 1Add
    BLAST
    Repeati196 – 20712BNR 2Add
    BLAST
    Repeati238 – 24912BNR 3Add
    BLAST
    Repeati285 – 29612BNR 4Add
    BLAST
    Repeati326 – 33712BNR 5Add
    BLAST
    Repeati375 – 38612BNR 6Add
    BLAST
    Repeati426 – 43712BNR 7Add
    BLAST
    Repeati504 – 51512BNR 8Add
    BLAST
    Repeati546 – 55712BNR 9Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 5912Intrachain binding of the propeptide and the extracellular domainBy similarityAdd
    BLAST
    Regioni610 – 754145Interactions with LRPAP1 and NGFBBy similarityAdd
    BLAST
    Regioni777 – 82549Golgi to endosome transport and interactions with GGA1 and GGA2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi785 – 7906Endocytosis signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi38 – 447Poly-Pro

    Domaini

    The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding By similarity.By similarity
    The extracellular domain may be shed following protease cleavage in some cell types.By similarity

    Sequence similaritiesi

    Contains 9 BNR repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG281049.
    GeneTreeiENSGT00510000046443.
    HOGENOMiHOG000231347.
    HOVERGENiHBG080235.
    KOiK12388.
    OMAiLTQMMYS.
    OrthoDBiEOG7RBZ7S.
    PhylomeDBiQ6PHU5.
    TreeFamiTF324918.

    Family and domain databases

    InterProiIPR006581. VPS10.
    [Graphical view]
    SMARTiSM00602. VPS10. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PHU5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG    50
    PVGVSWGLRA AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ 100
    HVFDDLSGSV SLSWVGDSTG VILVLTTFQV PLVIVSFGQS KLYRSEDYGK 150
    NFKDITNLIN NTFIRTEFGM AIGPENSGKV ILTAEVSGGS RGGRVFRSSD 200
    FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS KNFGEKWEEI 250
    HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK 300
    IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS 350
    ILAANEDMVF MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET 400
    DFTNVTSLRG VYITSTLSED NSIQSMITFD QGGRWEHLRK PENSKCDATA 450
    KNKNECSLHI HASYSISQKL NVPMAPLSEP NAVGIVIAHG SVGDAISVMV 500
    PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR PINVIKFSTD 550
    EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV 600
    DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ 650
    NGRDYVVAKQ PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC 700
    LYGKEEHLTT NGYRKIPGDK CQGGMNPARE VKDLKKKCTS NFLNPTKQNS 750
    KSNSVPIILA IVGLMLVTVV AGVLIVKKYV CGGRFLVHRY SVLQQHAEAD 800
    GVEALDSTSH AKSGYHDDSD EDLLE 825
    Length:825
    Mass (Da):91,200
    Last modified:July 5, 2004 - v1
    Checksum:i9A7A73C6FE1C8201
    GO
    Isoform 2 (identifier: Q6PHU5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         748-748: Q → QDSRPQGHSLSQNPAPPPLGYTENTHFLSPTQKQ

    Note: No experimental confirmation available.

    Show »
    Length:858
    Mass (Da):94,813
    Checksum:iB4AC632F993E8E14
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti315 – 3151V → E in AAF22639. (PubMed:11322955)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei748 – 7481Q → QDSRPQGHSLSQNPAPPPLG YTENTHFLSPTQKQ in isoform 2. 1 PublicationVSP_016650

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175279 mRNA. Translation: AAF22639.1.
    AK147442 mRNA. Translation: BAE27915.1.
    AL671899 Genomic DNA. Translation: CAM19473.1.
    BC034129 mRNA. Translation: AAH34129.1.
    BC056343 mRNA. Translation: AAH56343.1.
    CCDSiCCDS17756.1. [Q6PHU5-1]
    RefSeqiNP_001258528.1. NM_001271599.1. [Q6PHU5-2]
    NP_064356.2. NM_019972.3. [Q6PHU5-1]
    UniGeneiMm.157119.

    Genome annotation databases

    EnsembliENSMUST00000102632; ENSMUSP00000099692; ENSMUSG00000068747. [Q6PHU5-1]
    GeneIDi20661.
    KEGGimmu:20661.
    UCSCiuc008qyr.1. mouse. [Q6PHU5-1]
    uc008qys.1. mouse. [Q6PHU5-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175279 mRNA. Translation: AAF22639.1 .
    AK147442 mRNA. Translation: BAE27915.1 .
    AL671899 Genomic DNA. Translation: CAM19473.1 .
    BC034129 mRNA. Translation: AAH34129.1 .
    BC056343 mRNA. Translation: AAH56343.1 .
    CCDSi CCDS17756.1. [Q6PHU5-1 ]
    RefSeqi NP_001258528.1. NM_001271599.1. [Q6PHU5-2 ]
    NP_064356.2. NM_019972.3. [Q6PHU5-1 ]
    UniGenei Mm.157119.

    3D structure databases

    ProteinModelPortali Q6PHU5.
    SMRi Q6PHU5. Positions 86-747.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203393. 1 interaction.
    DIPi DIP-46095N.
    IntActi Q6PHU5. 4 interactions.
    MINTi MINT-4130555.
    STRINGi 10090.ENSMUSP00000088052.

    PTM databases

    PhosphoSitei Q6PHU5.

    Proteomic databases

    MaxQBi Q6PHU5.
    PaxDbi Q6PHU5.
    PRIDEi Q6PHU5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102632 ; ENSMUSP00000099692 ; ENSMUSG00000068747 . [Q6PHU5-1 ]
    GeneIDi 20661.
    KEGGi mmu:20661.
    UCSCi uc008qyr.1. mouse. [Q6PHU5-1 ]
    uc008qys.1. mouse. [Q6PHU5-2 ]

    Organism-specific databases

    CTDi 6272.
    MGIi MGI:1338015. Sort1.

    Phylogenomic databases

    eggNOGi NOG281049.
    GeneTreei ENSGT00510000046443.
    HOGENOMi HOG000231347.
    HOVERGENi HBG080235.
    KOi K12388.
    OMAi LTQMMYS.
    OrthoDBi EOG7RBZ7S.
    PhylomeDBi Q6PHU5.
    TreeFami TF324918.

    Miscellaneous databases

    ChiTaRSi SORT1. mouse.
    NextBioi 299105.
    PROi Q6PHU5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PHU5.
    Bgeei Q6PHU5.
    CleanExi MM_SORT1.
    Genevestigatori Q6PHU5.

    Family and domain databases

    InterProi IPR006581. VPS10.
    [Graphical view ]
    SMARTi SM00602. VPS10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Pharmacological properties of the mouse neurotensin receptor 3. Maintenance of cell surface receptor during internalization of neurotensin."
      Navarro V., Martin S., Sarret P., Nielsen M.S., Petersen C.M., Vincent J.-P., Mazella J.
      FEBS Lett. 495:100-105(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A NEUROTENSIN RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION.
      Strain: BALB/c.
      Tissue: Brain.
    2. "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] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain and Salivary gland.
    5. "Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes."
      Morris N.J., Ross S.A., Lane W.S., Moestrup S.K., Petersen C.M., Keller S.R., Lienhard G.E.
      J. Biol. Chem. 273:3582-3587(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    6. "Expression of the 100-kDa neurotensin receptor sortilin during mouse embryonal development."
      Hermans-Borgmeyer I., Hermey G., Nykjaer A., Schaller C.
      Brain Res. Mol. Brain Res. 65:216-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase."
      Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.
      J. Biol. Chem. 274:8832-8836(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPL.
    8. "Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes."
      Hashiramoto M., James D.E.
      Mol. Cell. Biol. 20:416-427(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Study of the mouse sortilin gene: effects of its transient silencing by RNA interference in TM4 Sertoli cells."
      Zeng J., Hassan A.J., Morales C.R.
      Mol. Reprod. Dev. 68:469-475(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PSAP, SUBCELLULAR LOCATION.
    10. "The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins."
      Hassan A.J., Zeng J., Ni X., Morales C.R.
      Mol. Reprod. Dev. 68:476-483(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Neurotensin receptor-3/sortilin mediates neurotensin-induced cytokine/chemokine expression in a murine microglial cell line."
      Dicou E., Vincent J.-P., Mazella J.
      J. Neurosci. Res. 78:92-99(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes."
      Shi J., Kandror K.V.
      Dev. Cell 9:99-108(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLC2A4, SUBCELLULAR LOCATION, INDUCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death."
      Kim T., Hempstead B.L.
      EMBO J. 28:1612-1623(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NGFR AND NRADD.
    15. "Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling."
      Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S., Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L., Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A.
      Nat. Neurosci. 14:54-61(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NTRK1 SIGNALING.

    Entry informationi

    Entry nameiSORT_MOUSE
    AccessioniPrimary (citable) accession number: Q6PHU5
    Secondary accession number(s): A2AEE8
    , Q3UHE2, Q8K043, Q9QXW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 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