Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O88307

- SORL_MOUSE

UniProt

O88307 - SORL_MOUSE

Protein

Sortilin-related receptor

Gene

Sorl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. May play a role in neural organization, as well as the establishment of embryonic organ systems. Involved in APP trafficking to and from the Golgi apparatus By similarity. It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta By similarity. Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization.By similarity1 Publication

    GO - Molecular functioni

    1. low-density lipoprotein particle binding Source: Ensembl
    2. protein binding Source: MGI

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. cell proliferation Source: Ensembl
    3. cholesterol metabolic process Source: UniProtKB-KW
    4. endocytosis Source: UniProtKB-KW
    5. lipid transport Source: UniProtKB-KW
    6. negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
    7. negative regulation of beta-amyloid formation Source: Alzheimers_University_of_Toronto
    8. negative regulation of MAP kinase activity Source: Alzheimers_University_of_Toronto
    9. negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
    10. negative regulation of neurofibrillary tangle assembly Source: Alzheimers_University_of_Toronto
    11. negative regulation of neurogenesis Source: Alzheimers_University_of_Toronto
    12. negative regulation of neuron death Source: Alzheimers_University_of_Toronto
    13. negative regulation of protein binding Source: Alzheimers_University_of_Toronto
    14. negative regulation of protein oligomerization Source: Alzheimers_University_of_Toronto
    15. negative regulation of tau-protein kinase activity Source: Alzheimers_University_of_Toronto
    16. positive regulation of choline O-acetyltransferase activity Source: Alzheimers_University_of_Toronto
    17. positive regulation of early endosome to recycling endosome transport Source: Alzheimers_University_of_Toronto
    18. positive regulation of endocytic recycling Source: Alzheimers_University_of_Toronto
    19. positive regulation of ER to Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
    20. positive regulation of protein catabolic process Source: Alzheimers_University_of_Toronto
    21. positive regulation of protein exit from endoplasmic reticulum Source: Alzheimers_University_of_Toronto
    22. positive regulation of protein localization to early endosome Source: Alzheimers_University_of_Toronto
    23. post-Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
    24. protein maturation Source: Alzheimers_University_of_Toronto
    25. protein retention in Golgi apparatus Source: Alzheimers_University_of_Toronto
    26. protein targeting Source: Alzheimers_University_of_Toronto
    27. protein targeting to Golgi Source: Alzheimers_University_of_Toronto
    28. protein targeting to lysosome Source: Alzheimers_University_of_Toronto
    29. regulation of smooth muscle cell migration Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Cholesterol metabolism, Endocytosis, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sortilin-related receptor
    Alternative name(s):
    Gp250
    Low-density lipoprotein receptor relative with 11 ligand-binding repeats
    Short name:
    LDLR relative with 11 ligand-binding repeats
    Short name:
    LR11
    SorLA-1
    Sorting protein-related receptor containing LDLR class A repeats
    Short name:
    mSorLA
    Gene namesi
    Name:Sorl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1202296. Sorl1.

    Subcellular locationi

    Membrane Curated; Single-pass type I membrane protein Curated. Golgi apparatus By similarity. Endosome By similarity. Secreted By similarity

    GO - Cellular componenti

    1. early endosome Source: Alzheimers_University_of_Toronto
    2. endoplasmic reticulum Source: Alzheimers_University_of_Toronto
    3. Golgi cisterna Source: Alzheimers_University_of_Toronto
    4. integral component of membrane Source: UniProtKB-KW
    5. low-density lipoprotein particle Source: UniProtKB-KW
    6. multivesicular body Source: Ensembl
    7. neuronal cell body Source: Ensembl
    8. nuclear envelope lumen Source: Alzheimers_University_of_Toronto
    9. perinuclear region of cytoplasm Source: MGI
    10. recycling endosome Source: Alzheimers_University_of_Toronto
    11. trans-Golgi network Source: Alzheimers_University_of_Toronto

    Keywords - Cellular componenti

    Endosome, Golgi apparatus, LDL, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 8153Removed in mature formBy similarityPRO_0000033166Add
    BLAST
    Chaini82 – 22152134Sortilin-related receptorPRO_0000033167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Modified residuei114 – 1141PhosphoserineBy similarity
    Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi674 – 6741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi818 – 8181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi871 – 8711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1035 – 10351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1068 – 10681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1078 ↔ 1090PROSITE-ProRule annotation
    Disulfide bondi1085 ↔ 1103PROSITE-ProRule annotation
    Disulfide bondi1097 ↔ 1112PROSITE-ProRule annotation
    Disulfide bondi1117 ↔ 1131PROSITE-ProRule annotation
    Disulfide bondi1125 ↔ 1144PROSITE-ProRule annotation
    Disulfide bondi1138 ↔ 1153PROSITE-ProRule annotation
    Disulfide bondi1158 ↔ 1170PROSITE-ProRule annotation
    Glycosylationi1164 – 11641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1165 ↔ 1183PROSITE-ProRule annotation
    Disulfide bondi1177 ↔ 1192PROSITE-ProRule annotation
    Glycosylationi1191 – 11911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1199 ↔ 1211PROSITE-ProRule annotation
    Disulfide bondi1206 ↔ 1224PROSITE-ProRule annotation
    Disulfide bondi1218 ↔ 1235PROSITE-ProRule annotation
    Disulfide bondi1239 ↔ 1249PROSITE-ProRule annotation
    Disulfide bondi1244 ↔ 1262PROSITE-ProRule annotation
    Glycosylationi1246 – 12461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1256 ↔ 1271PROSITE-ProRule annotation
    Disulfide bondi1275 ↔ 1289PROSITE-ProRule annotation
    Disulfide bondi1283 ↔ 1302PROSITE-ProRule annotation
    Disulfide bondi1296 ↔ 1315PROSITE-ProRule annotation
    Disulfide bondi1325 ↔ 1337PROSITE-ProRule annotation
    Disulfide bondi1332 ↔ 1350PROSITE-ProRule annotation
    Disulfide bondi1344 ↔ 1359PROSITE-ProRule annotation
    Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1368 ↔ 1381PROSITE-ProRule annotation
    Disulfide bondi1376 ↔ 1394PROSITE-ProRule annotation
    Disulfide bondi1388 ↔ 1403PROSITE-ProRule annotation
    Disulfide bondi1419 ↔ 1431PROSITE-ProRule annotation
    Disulfide bondi1426 ↔ 1444PROSITE-ProRule annotation
    Disulfide bondi1438 ↔ 1453PROSITE-ProRule annotation
    Glycosylationi1458 – 14581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1471 ↔ 1484PROSITE-ProRule annotation
    Disulfide bondi1478 ↔ 1497PROSITE-ProRule annotation
    Disulfide bondi1491 ↔ 1506PROSITE-ProRule annotation
    Disulfide bondi1514 ↔ 1527PROSITE-ProRule annotation
    Disulfide bondi1521 ↔ 1540PROSITE-ProRule annotation
    Disulfide bondi1534 ↔ 1549PROSITE-ProRule annotation
    Glycosylationi1608 – 16081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1706 – 17061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1733 – 17331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1810 – 18101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1855 – 18551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1895 – 18951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1987 – 19871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2011 – 20111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2055 – 20551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2070 – 20701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2077 – 20771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2093 – 20931N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2207 – 22071Phosphoserine; by ROCK2By similarity

    Post-translational modificationi

    The propeptide removed in the N-terminus may be cleaved by furin or homologous proteases.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiO88307.
    PaxDbiO88307.
    PRIDEiO88307.

    PTM databases

    PhosphoSiteiO88307.

    Expressioni

    Tissue specificityi

    Abundant in brain, where it is mainly expressed in adult cerebellum, hippocampal ca regions, dentate gyrus, and to a much lesser extent in the cerebral cortex. Detectable in kidney, skeletal muscle, lung and spleen, but not in the liver.

    Developmental stagei

    Expressed as early as embryonic day 6.5 (E6.5) and peaks at E11, the main location is in the CNS during development. At early stages, it is abundant in a subpopulation of neurons in the cerebral cortex, in the hippocampus, and granular and Purkinje cell layers in the cerebellum, whereas in the adult, expression in cerebellar granular cells and in the cerebral cortex is low. Expression occurs also in a variety of glands and organs during organogenesis.

    Gene expression databases

    ArrayExpressiO88307.
    BgeeiO88307.
    GenevestigatoriO88307.

    Interactioni

    Subunit structurei

    Interacts with GGA1 and ROCK2 By similarity. Interacts with APP. Interacts with PLAUR By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-42439N.
    MINTiMINT-1342356.

    Structurei

    3D structure databases

    ProteinModelPortaliO88307.
    SMRiO88307. Positions 1156-1193, 1651-1745.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini82 – 21382057ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2160 – 221556CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2139 – 215921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati136 – 14712BNR 1Add
    BLAST
    Repeati232 – 24312BNR 2Add
    BLAST
    Repeati441 – 45212BNR 3Add
    BLAST
    Repeati521 – 53212BNR 4Add
    BLAST
    Repeati562 – 57312BNR 5Add
    BLAST
    Repeati800 – 84344LDL-receptor class B 1Add
    BLAST
    Repeati844 – 88744LDL-receptor class B 2Add
    BLAST
    Repeati888 – 93245LDL-receptor class B 3Add
    BLAST
    Repeati933 – 97240LDL-receptor class B 4Add
    BLAST
    Repeati973 – 101341LDL-receptor class B 5Add
    BLAST
    Domaini1026 – 107247EGF-likeAdd
    BLAST
    Domaini1076 – 111439LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1115 – 115541LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1156 – 119439LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1198 – 123639LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1238 – 127235LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1273 – 131745LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1323 – 136139LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1366 – 140540LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1417 – 145539LDL-receptor class A 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1469 – 150840LDL-receptor class A 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1512 – 155140LDL-receptor class A 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1557 – 164993Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1653 – 174593Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1747 – 1846100Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1844 – 192885Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1935 – 203096Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini2031 – 211989Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2173 – 21786Endocytosis signalSequence Analysis

    Sequence similaritiesi

    Contains 5 BNR repeats.Curated
    Contains 1 EGF-like domain.Curated
    Contains 6 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 11 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 5 LDL-receptor class B repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG281049.
    GeneTreeiENSGT00510000046443.
    HOGENOMiHOG000007009.
    HOVERGENiHBG017830.
    InParanoidiQ3UHM3.
    OMAiTNVYISS.
    OrthoDBiEOG7FV3PK.
    TreeFamiTF324918.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    2.60.40.10. 4 hits.
    4.10.400.10. 11 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR006581. VPS10.
    [Graphical view]
    PfamiPF00041. fn3. 3 hits.
    PF00057. Ldl_recept_a. 10 hits.
    PF00058. Ldl_recept_b. 2 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00060. FN3. 6 hits.
    SM00192. LDLa. 11 hits.
    SM00135. LY. 5 hits.
    SM00602. VPS10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 3 hits.
    SSF57424. SSF57424. 11 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS50853. FN3. 4 hits.
    PS01209. LDLRA_1. 10 hits.
    PS50068. LDLRA_2. 11 hits.
    PS51120. LDLRB. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O88307-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATRSSRRES RLPFLFALVA LLPRGALGGG WTQRLHGGPA PLPQDRGFFV     50
    VQGDPRDLRL GTHGDAPGAS PAARKPLRTR RSAALQPQPI QVYGQVSLND 100
    SHNQMVVHWA GEKSNVIVAL ARDSLALARP KSSDVYVSYD YGKSFSKISE 150
    KLNFGVGNNS EAVISQFYHS PADNKRYIFV DAYAQYLWIT FDFCSTIHGF 200
    SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT WIMIQEHVKS 250
    FSWGIDPYDQ PNAIYIERHE PFGFSTVLRS TDFFQSRENQ EVILEEVRDF 300
    QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY 350
    IADAAEDQVF VCVSHSNNST NLYISEAEGL KFSLSLENVL YYSPGGAGSD 400
    TLVRYFANEP FADFHRVEGL QGVYIATLIN GSMNEENMRS VITFDKGGTW 450
    EFLQAPAFTG YGEKINCELS QGCSLHLAQR LSQLLNLQLR RMPILSKESA 500
    PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY TWGDHGGIIM 550
    AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF 600
    GSNKESVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV 650
    FKRRTPHATC FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV 700
    PDPEFSGKPY SPPVPCPVGS SYRRTRGYRK ISGDTCSGGD VEARLEGELV 750
    PCPLAEENEF ILYAMRKSIY RYDLASGATE QLPLSGLRAA VALDFDYERN 800
    CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE PLSQLLYWVD 850
    AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 900
    GIYRSYMDGS AAYRLVSEDV KWPNGISVDS QWIYWTDAYL DCIERITFSG 950
    QQRSVILDSL PHPYAIAVFK NEIYWDDWSQ LSIFRASKHS RSQVEILASQ 1000
    LTGLMDMKVF YKGKNAGSNA CVPQPCSLLC LPKANNSKSC RCPEGVASSV 1050
    LPSGDLMCDC PQGYQRKNNT CVKEENTCLR NQYRCSNGNC INSIWWCDFD 1100
    NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL EDDCGDNSDE 1150
    SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 1200
    ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI 1250
    PSSKHCDGLR DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV 1300
    QCRDGSDEDA AFAGCSQDPE FHKECDEFGF QCQNGVCISL IWKCDGMDDC 1350
    GDYSDEANCE NPTEAPNCSR YFQFHCENGH CIPNRWKCDR ENDCGDWSDE 1400
    KDCGDSHVLP SPTPGPSTCL PNYFHCSSGA CVMGTWVCDG YRDCADGSDE 1450
    EACPSLANST AASTPTQFGQ CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG 1500
    QDEANCPTHS TLTCTSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS 1550
    DELTVYKVQN LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW 1600
    KTLETHSNKT STVLKVLKPD TTYQVKVQVH CLNKVHNTND FVTLRTPEGL 1650
    PDAPRNLQLS LNSEEEGVIL GHWAPPVHTH GLIREYIVEY SRSGSKMWAS 1700
    QRAASNSTEI KNLLLNALYT VRVAAVTSRG IGNWSDSKSI TTIKGKVIQA 1750
    PNIHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLSFRG 1800
    GSALSHRVSN LTAHTSYEIS AWAKTDLGDS PLAFEHILTR GSSPPAPSLK 1850
    AKAINQTAVE CIWTGPKNVV YGIFYATSFL DLYRNPKSVT TSLHNKTVIV 1900
    SKDEQYLFLV RVLIPYQGPS SDYVVVKMIP DSRLPPRHLH AVHIGKTSAL 1950
    IKWESPYDSP DQDLFYAIAV KDLIRKTDRS YKVRSRNSTV EYSLSKLEPG 2000
    GKYHIIVQLG NMSKDSSIKI TTVSLSAPDA LKIITENDHV LLFWKSLALK 2050
    EKQFNETRGY EIHMSDSAVN LTAYLGNTTD NFFKVSNLKM GHNYTFTVQA 2100
    RCLFGSQICG EPAVLLYDEL SSGADAAVIQ AARSTDVAAV VVPILFLILL 2150
    SLGVGFAILY TKHRRLQSSF SAFANSHYSS RLGSAIFSSG DDLGEDDEDA 2200
    PMITGFSDDV PMVIA 2215
    Length:2,215
    Mass (Da):247,086
    Last modified:July 27, 2011 - v3
    Checksum:i5D7F53806EFE2CB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti706 – 7061S → F in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti768 – 7681S → F in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti785 – 7851S → W in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti796 – 7961D → G in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti953 – 9531R → G in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1268 – 12692EQ → DE in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1425 – 14251H → A in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1425 – 14251H → R in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti1425 – 14251H → R in CAA72732. 1 PublicationCurated
    Sequence conflicti1468 – 14681F → L in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1468 – 14681F → L in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti1468 – 14681F → L in CAA72732. 1 PublicationCurated
    Sequence conflicti1663 – 16631S → R in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1663 – 16631S → R in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti1663 – 16631S → R in CAA72732. 1 PublicationCurated
    Sequence conflicti1709 – 17135EIKNL → KKKKK in CAA72732. 1 PublicationCurated
    Sequence conflicti1807 – 18071R → K in BAA31219. (PubMed:9726247)Curated
    Sequence conflicti1807 – 18071R → K in AAC16739. (PubMed:9510025)Curated
    Sequence conflicti2130 – 21301Q → H in BAA31219. (PubMed:9726247)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015790 mRNA. Translation: BAA31219.1.
    AK147303 mRNA. Translation: BAE27834.1.
    AF031816 mRNA. Translation: AAC16739.1.
    Y12004 mRNA. Translation: CAA72732.1.
    CCDSiCCDS40594.1.
    PIRiT00348.
    RefSeqiNP_035566.2. NM_011436.3.
    UniGeneiMm.121920.

    Genome annotation databases

    EnsembliENSMUST00000060989; ENSMUSP00000058613; ENSMUSG00000049313.
    GeneIDi20660.
    KEGGimmu:20660.
    UCSCiuc009pap.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015790 mRNA. Translation: BAA31219.1 .
    AK147303 mRNA. Translation: BAE27834.1 .
    AF031816 mRNA. Translation: AAC16739.1 .
    Y12004 mRNA. Translation: CAA72732.1 .
    CCDSi CCDS40594.1.
    PIRi T00348.
    RefSeqi NP_035566.2. NM_011436.3.
    UniGenei Mm.121920.

    3D structure databases

    ProteinModelPortali O88307.
    SMRi O88307. Positions 1156-1193, 1651-1745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42439N.
    MINTi MINT-1342356.

    PTM databases

    PhosphoSitei O88307.

    Proteomic databases

    MaxQBi O88307.
    PaxDbi O88307.
    PRIDEi O88307.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000060989 ; ENSMUSP00000058613 ; ENSMUSG00000049313 .
    GeneIDi 20660.
    KEGGi mmu:20660.
    UCSCi uc009pap.1. mouse.

    Organism-specific databases

    CTDi 6653.
    MGIi MGI:1202296. Sorl1.

    Phylogenomic databases

    eggNOGi NOG281049.
    GeneTreei ENSGT00510000046443.
    HOGENOMi HOG000007009.
    HOVERGENi HBG017830.
    InParanoidi Q3UHM3.
    OMAi TNVYISS.
    OrthoDBi EOG7FV3PK.
    TreeFami TF324918.

    Miscellaneous databases

    NextBioi 299101.
    PROi O88307.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88307.
    Bgeei O88307.
    Genevestigatori O88307.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    2.60.40.10. 4 hits.
    4.10.400.10. 11 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR006581. VPS10.
    [Graphical view ]
    Pfami PF00041. fn3. 3 hits.
    PF00057. Ldl_recept_a. 10 hits.
    PF00058. Ldl_recept_b. 2 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00060. FN3. 6 hits.
    SM00192. LDLa. 11 hits.
    SM00135. LY. 5 hits.
    SM00602. VPS10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 3 hits.
    SSF57424. SSF57424. 11 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS50853. FN3. 4 hits.
    PS01209. LDLRA_1. 10 hits.
    PS50068. LDLRA_2. 11 hits.
    PS51120. LDLRB. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Unique expression pattern of a novel mosaic receptor in the developing cerebral cortex."
      Hermans-Borgmeyer I., Hampe W., Schinke B., Methner A., Nykjaer A., Suesens U., Fenger U., Herbarth B., Schaller H.C.
      Mech. Dev. 70:65-76(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-2215.
      Tissue: Brain.
    4. Boehmelt G., Antonio L., Iscove N.N.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1119-1713.
      Strain: Swiss Webster.
    5. "LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration."
      Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.
      Circ. Res. 94:752-758(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: INTERACTION WITH APP.

    Entry informationi

    Entry nameiSORL_MOUSE
    AccessioniPrimary (citable) accession number: O88307
    Secondary accession number(s): O54711, O70581, Q3UHM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 129 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