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O54861

- SORT_RAT

UniProt

O54861 - SORT_RAT

Protein

Sortilin

Gene

Sort1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (20 Dec 2005)
      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.1 Publication

    GO - Molecular functioni

    1. G-protein coupled neurotensin receptor activity Source: RGD

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. endocytosis Source: UniProtKB-KW
    3. intracellular protein transport Source: RGD
    4. multicellular organismal development Source: UniProtKB-KW
    5. neuropeptide signaling pathway Source: GOC
    6. ossification Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation, Endocytosis, Osteogenesis, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sortilin
    Alternative name(s):
    Glycoprotein 110
    Short name:
    Gp110
    Neurotensin receptor 3
    Short name:
    NTR3
    Gene namesi
    Name:Sort1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619999. 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. Lysosome 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
    Note: Localized to membranes of the endosomes, Golgi stack, lysosomes and nucleus. Interaction with NRADD promotes localization at the cell membrane in neurons; this promotes interaction with NGFR. Localization to the plasma membrane in adipocytes is enhanced by insulin By similarity. Localized to the endoplasmic reticulum and the plasma membrane. Also found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes.By similarity

    GO - Cellular componenti

    1. dendrite Source: RGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. endosome membrane Source: UniProtKB-SubCell
    4. Golgi cisterna membrane Source: UniProtKB-SubCell
    5. integral component of membrane Source: RGD
    6. intracellular membrane-bounded organelle Source: RGD
    7. lysosomal membrane Source: UniProtKB-SubCell
    8. neuronal cell body Source: RGD
    9. nuclear membrane Source: UniProtKB-SubCell
    10. plasma membrane Source: RGD

    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_0000045157Add
    BLAST
    Chaini76 – 825750SortilinPRO_0000045158Add
    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 – 8191PhosphoserineBy similarity

    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

    PaxDbiO54861.
    PRIDEiO54861.

    Expressioni

    Tissue specificityi

    Highly expressed in fat, brain, and lung. Expressed in neuronal bodies and dendrites of the piriform cortex and hippocampus. Also expressed in the islands of Calleja, medial and lateral septal nuclei, amygdaloid nuclei, thalamic nuclei, the supraoptic nucleus, the substantia nigra, the Purkinje layer of the cerebellar cortex and the cranial motor nerve nuclei of the brainstem.2 Publications

    Gene expression databases

    GenevestigatoriO54861.

    Interactioni

    Subunit structurei

    Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP and GM2A, LPL, NTS, PSAP and SLC2A4. Forms a complex with NGFR which binds specifically to the precursor form of NGFB (proNGFB). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate their anterograde axonal transport and signaling. Interacts with NRADD and NGFR. Interaction with NRADD protects against degradation in the lysosome By similarity. Interacts with the precursor form of BDNF (proBDNF).By similarity1 Publication

    Protein-protein interaction databases

    IntActiO54861. 3 interactions.
    MINTiMINT-4583532.

    Structurei

    3D structure databases

    ProteinModelPortaliO54861.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini76 – 754679ExtracellularSequence 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.
    HOGENOMiHOG000231347.
    HOVERGENiHBG080235.
    KOiK12388.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    O54861-1 [UniParc]FASTAAdd to Basket

    « 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
    ILAANDDMVF MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET 400
    DFTNVTSLRG VYITSTLSED NSIQSMITFD QGGRWEHLQK PENSKCDATA 450
    KNKNECSLHI HASYSISQKL NVPMAPLSEP NAVGIVIAHG SVGDAISVMV 500
    PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR PINVIKFSTD 550
    EGQCWQSYVF SQEPVYFTGL ASEPGARSMN ISIWGFTESF LTRQWVSYTI 600
    DFKDILERNC EENDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ 650
    NGRDYVVAKQ PSICPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC 700
    LYGKEEHLTT NGYRKIPGDR CQGGMNPARE VKDLKKKCTS NFLNPKKQNS 750
    KSSSVPIILA IVGLMLVTVV AGVLIVKKYV CGGRFLVHRY SVLQQHAEAD 800
    GVEALDTASH AKSGYHDDSD EDLLE 825
    Length:825
    Mass (Da):91,169
    Last modified:December 20, 2005 - v3
    Checksum:i060B43A54993EF06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911I → V in AAC02932. (PubMed:9452485)Curated
    Sequence conflicti276 – 2772KA → T in AAB81864. (PubMed:9305862)Curated
    Sequence conflicti433 – 4331G → R in AAB81864. (PubMed:9305862)Curated
    Sequence conflicti507 – 5071D → Y in AAC02932. (PubMed:9452485)Curated
    Sequence conflicti659 – 6591K → Q AA sequence (PubMed:9305862)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03012291 Genomic DNA. No translation available.
    AABR03012896 Genomic DNA. No translation available.
    AABR03017724 Genomic DNA. No translation available.
    AABR03019134 Genomic DNA. No translation available.
    AABR03020083 Genomic DNA. No translation available.
    AF019109 mRNA. Translation: AAC02932.1.
    AF023621 mRNA. Translation: AAB81864.1.
    RefSeqiNP_113955.1. NM_031767.1.
    UniGeneiRn.11286.

    Genome annotation databases

    GeneIDi83576.
    KEGGirno:83576.
    UCSCiRGD:619999. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03012291 Genomic DNA. No translation available.
    AABR03012896 Genomic DNA. No translation available.
    AABR03017724 Genomic DNA. No translation available.
    AABR03019134 Genomic DNA. No translation available.
    AABR03020083 Genomic DNA. No translation available.
    AF019109 mRNA. Translation: AAC02932.1 .
    AF023621 mRNA. Translation: AAB81864.1 .
    RefSeqi NP_113955.1. NM_031767.1.
    UniGenei Rn.11286.

    3D structure databases

    ProteinModelPortali O54861.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O54861. 3 interactions.
    MINTi MINT-4583532.

    Proteomic databases

    PaxDbi O54861.
    PRIDEi O54861.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 83576.
    KEGGi rno:83576.
    UCSCi RGD:619999. rat.

    Organism-specific databases

    CTDi 6272.
    RGDi 619999. Sort1.

    Phylogenomic databases

    eggNOGi NOG281049.
    HOGENOMi HOG000231347.
    HOVERGENi HBG080235.
    KOi K12388.

    Miscellaneous databases

    NextBioi 616085.
    PROi O54861.

    Gene expression databases

    Genevestigatori O54861.

    Family and domain databases

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

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 89-825, PROTEIN SEQUENCE OF 78-93, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
      Strain: Sprague-Dawley.
      Tissue: Adipocyte.
    3. "Sortilin is a major protein component of Glut4-containing vesicles."
      Lin B.-Z., Pilch P.F., Kandror K.V.
      J. Biol. Chem. 272:24145-24147(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-745, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Skeletal muscle.
    4. "The prodomain of a secreted hydrophobic mini-protein facilitates its export from the endoplasmic reticulum by hitchhiking on sorting receptors."
      Conticello S.G., Kowalsman N.D., Jacobsen C., Yudkovsky G., Sato K., Elazar Z., Petersen C.M., Aronheim A., Fainzilber M.
      J. Biol. Chem. 278:26311-26314(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Distribution of NTS3 receptor/sortilin mRNA and protein in the rat central nervous system."
      Sarret P., Krzywkowski P., Segal L., Nielsen M.S., Petersen C.M., Mazella J., Stroh T., Beaudet A.
      J. Comp. Neurol. 461:483-505(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway."
      Chen Z.-Y., Ieraci A., Teng H., Dall H., Meng C.-X., Herrera D.G., Nykjaer A., Hempstead B.L., Lee F.S.
      J. Neurosci. 25:6156-6166(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BDNF.

    Entry informationi

    Entry nameiSORT_RAT
    AccessioniPrimary (citable) accession number: O54861
    Secondary accession number(s): O35389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 115 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3