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O88307

- SORL_MOUSE

UniProt

O88307 - SORL_MOUSE

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Protein

Sortilin-related receptor

Gene

Sorl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. beta-amyloid binding Source: Ensembl
  2. low-density lipoprotein particle binding Source: Ensembl

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  4. Golgi cisterna Source: Alzheimers_University_of_Toronto
  5. integral component of membrane Source: UniProtKB-KW
  6. low-density lipoprotein particle Source: UniProtKB-KW
  7. multivesicular body Source: Ensembl
  8. neuronal cell body Source: Ensembl
  9. nuclear envelope lumen Source: Alzheimers_University_of_Toronto
  10. perinuclear region of cytoplasm Source: MGI
  11. recycling endosome Source: Alzheimers_University_of_Toronto
  12. trans-Golgi network Source: Alzheimers_University_of_Toronto
Complete GO annotation...

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

BgeeiO88307.
ExpressionAtlasiO88307. baseline and differential.
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.
InParanoidiO88307.
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

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        10         20         30         40         50
MATRSSRRES RLPFLFALVA LLPRGALGGG WTQRLHGGPA PLPQDRGFFV
60 70 80 90 100
VQGDPRDLRL GTHGDAPGAS PAARKPLRTR RSAALQPQPI QVYGQVSLND
110 120 130 140 150
SHNQMVVHWA GEKSNVIVAL ARDSLALARP KSSDVYVSYD YGKSFSKISE
160 170 180 190 200
KLNFGVGNNS EAVISQFYHS PADNKRYIFV DAYAQYLWIT FDFCSTIHGF
210 220 230 240 250
SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT WIMIQEHVKS
260 270 280 290 300
FSWGIDPYDQ PNAIYIERHE PFGFSTVLRS TDFFQSRENQ EVILEEVRDF
310 320 330 340 350
QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY
360 370 380 390 400
IADAAEDQVF VCVSHSNNST NLYISEAEGL KFSLSLENVL YYSPGGAGSD
410 420 430 440 450
TLVRYFANEP FADFHRVEGL QGVYIATLIN GSMNEENMRS VITFDKGGTW
460 470 480 490 500
EFLQAPAFTG YGEKINCELS QGCSLHLAQR LSQLLNLQLR RMPILSKESA
510 520 530 540 550
PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY TWGDHGGIIM
560 570 580 590 600
AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF
610 620 630 640 650
GSNKESVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV
660 670 680 690 700
FKRRTPHATC FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV
710 720 730 740 750
PDPEFSGKPY SPPVPCPVGS SYRRTRGYRK ISGDTCSGGD VEARLEGELV
760 770 780 790 800
PCPLAEENEF ILYAMRKSIY RYDLASGATE QLPLSGLRAA VALDFDYERN
810 820 830 840 850
CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE PLSQLLYWVD
860 870 880 890 900
AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP
910 920 930 940 950
GIYRSYMDGS AAYRLVSEDV KWPNGISVDS QWIYWTDAYL DCIERITFSG
960 970 980 990 1000
QQRSVILDSL PHPYAIAVFK NEIYWDDWSQ LSIFRASKHS RSQVEILASQ
1010 1020 1030 1040 1050
LTGLMDMKVF YKGKNAGSNA CVPQPCSLLC LPKANNSKSC RCPEGVASSV
1060 1070 1080 1090 1100
LPSGDLMCDC PQGYQRKNNT CVKEENTCLR NQYRCSNGNC INSIWWCDFD
1110 1120 1130 1140 1150
NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL EDDCGDNSDE
1160 1170 1180 1190 1200
SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE
1210 1220 1230 1240 1250
ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI
1260 1270 1280 1290 1300
PSSKHCDGLR DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV
1310 1320 1330 1340 1350
QCRDGSDEDA AFAGCSQDPE FHKECDEFGF QCQNGVCISL IWKCDGMDDC
1360 1370 1380 1390 1400
GDYSDEANCE NPTEAPNCSR YFQFHCENGH CIPNRWKCDR ENDCGDWSDE
1410 1420 1430 1440 1450
KDCGDSHVLP SPTPGPSTCL PNYFHCSSGA CVMGTWVCDG YRDCADGSDE
1460 1470 1480 1490 1500
EACPSLANST AASTPTQFGQ CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG
1510 1520 1530 1540 1550
QDEANCPTHS TLTCTSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS
1560 1570 1580 1590 1600
DELTVYKVQN LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW
1610 1620 1630 1640 1650
KTLETHSNKT STVLKVLKPD TTYQVKVQVH CLNKVHNTND FVTLRTPEGL
1660 1670 1680 1690 1700
PDAPRNLQLS LNSEEEGVIL GHWAPPVHTH GLIREYIVEY SRSGSKMWAS
1710 1720 1730 1740 1750
QRAASNSTEI KNLLLNALYT VRVAAVTSRG IGNWSDSKSI TTIKGKVIQA
1760 1770 1780 1790 1800
PNIHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLSFRG
1810 1820 1830 1840 1850
GSALSHRVSN LTAHTSYEIS AWAKTDLGDS PLAFEHILTR GSSPPAPSLK
1860 1870 1880 1890 1900
AKAINQTAVE CIWTGPKNVV YGIFYATSFL DLYRNPKSVT TSLHNKTVIV
1910 1920 1930 1940 1950
SKDEQYLFLV RVLIPYQGPS SDYVVVKMIP DSRLPPRHLH AVHIGKTSAL
1960 1970 1980 1990 2000
IKWESPYDSP DQDLFYAIAV KDLIRKTDRS YKVRSRNSTV EYSLSKLEPG
2010 2020 2030 2040 2050
GKYHIIVQLG NMSKDSSIKI TTVSLSAPDA LKIITENDHV LLFWKSLALK
2060 2070 2080 2090 2100
EKQFNETRGY EIHMSDSAVN LTAYLGNTTD NFFKVSNLKM GHNYTFTVQA
2110 2120 2130 2140 2150
RCLFGSQICG EPAVLLYDEL SSGADAAVIQ AARSTDVAAV VVPILFLILL
2160 2170 2180 2190 2200
SLGVGFAILY TKHRRLQSSF SAFANSHYSS RLGSAIFSSG DDLGEDDEDA
2210
PMITGFSDDV PMVIA
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 O88307.
OMAi TNVYISS.
OrthoDBi EOG7FV3PK.
TreeFami TF324918.

Miscellaneous databases

NextBioi 299101.
PROi O88307.
SOURCEi Search...

Gene expression databases

Bgeei O88307.
ExpressionAtlasi O88307. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 130 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