UniProtKB - O88307 (SORL_MOUSE)
Sortilin-related receptor
Sorl1
Functioni
GO - Molecular functioni
- ADP-ribosylation factor binding Source: MGI
- amyloid-beta binding Source: MGI
- low-density lipoprotein particle binding Source: MGI
- neuropeptide binding Source: MGI
- transmembrane signaling receptor activity Source: MGI
GO - Biological processi
- adaptive thermogenesis Source: UniProtKB
- cell migration Source: MGI
- diet induced thermogenesis Source: UniProtKB
- insulin receptor recycling Source: UniProtKB
- negative regulation of amyloid-beta formation Source: Alzheimers_University_of_Toronto
- negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
- negative regulation of BMP signaling pathway Source: UniProtKB
- negative regulation of MAP kinase activity Source: Alzheimers_University_of_Toronto
- negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
- negative regulation of neurofibrillary tangle assembly Source: Alzheimers_University_of_Toronto
- negative regulation of neurogenesis Source: Alzheimers_University_of_Toronto
- negative regulation of neuron death Source: Alzheimers_University_of_Toronto
- negative regulation of protein binding Source: Alzheimers_University_of_Toronto
- negative regulation of protein-containing complex assembly Source: Alzheimers_University_of_Toronto
- negative regulation of tau-protein kinase activity Source: Alzheimers_University_of_Toronto
- negative regulation of triglyceride catabolic process Source: UniProtKB
- neuropeptide signaling pathway Source: MGI
- positive regulation of adipose tissue development Source: UniProtKB
- positive regulation of choline O-acetyltransferase activity Source: Alzheimers_University_of_Toronto
- positive regulation of early endosome to recycling endosome transport Source: Alzheimers_University_of_Toronto
- positive regulation of endocytic recycling Source: Alzheimers_University_of_Toronto
- positive regulation of ER to Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
- positive regulation of glial cell-derived neurotrophic factor secretion Source: UniProtKB
- positive regulation of insulin receptor signaling pathway Source: UniProtKB
- positive regulation of protein catabolic process Source: Alzheimers_University_of_Toronto
- positive regulation of protein exit from endoplasmic reticulum Source: Alzheimers_University_of_Toronto
- positive regulation of protein localization to early endosome Source: Alzheimers_University_of_Toronto
- post-Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
- protein localization to Golgi apparatus Source: Alzheimers_University_of_Toronto
- protein maturation Source: Alzheimers_University_of_Toronto
- protein retention in Golgi apparatus Source: Alzheimers_University_of_Toronto
- protein targeting Source: UniProtKB
- protein targeting to lysosome Source: Alzheimers_University_of_Toronto
- receptor-mediated endocytosis Source: MGI
- regulation of smooth muscle cell migration Source: MGI
Keywordsi
Molecular function | Developmental protein, Receptor |
Biological process | Endocytosis, Transport |
Names & Taxonomyi
Protein namesi | Recommended name: Sortilin-related receptorAlternative name(s): Gp250 Low-density lipoprotein receptor relative with 11 ligand-binding repeats Short name: LDLR relative with 11 ligand-binding repeats Short name: LR111 Publication SorLA-1 Sorting protein-related receptor containing LDLR class A repeats Short name: mSorLA1 Publication |
Gene namesi | Name:Sorl1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1202296, Sorl1 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type I membrane protein By similarity
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
Golgi apparatus
- Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
- trans-Golgi network membrane By similarity; Single-pass type I membrane protein By similarity
Extracellular region or secreted
- Secreted 2 Publications
Endosome
- Endosome membrane By similarity; Single-pass type I membrane protein By similarity
- Early endosome membrane By similarity; Single-pass type I membrane protein By similarity
- Recycling endosome membrane By similarity; Single-pass type I membrane protein By similarity
- multivesicular body membrane By similarity; Single-pass type I membrane protein By similarity
Other locations
- secretory vesicle membrane By similarity; Single-pass type I membrane protein By similarity
Note: Mostly intracellular, predominantly in the trans-Golgi network (TGN) and in endosome, as well as in endosome-to-TGN recycling compartments; found at low levels on the plasma membrane (By similarity). At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain (also called soluble SORLA, solLR11 or sLR11) in the extracellular milieu (PubMed:11082041). The shedding may be catalyzed by ADAM17/TACE. Following shedding, PSEN1/presenilin-1 cleaves the remaining transmembrane fragment and catalyzes the release of a C-terminal fragment in the cytosol and of a soluble N-terminal beta fragment in the extracellular milieu. The C-terminal cytosolic fragment localizes to the nucleus. At the cell surface, the full-length protein undergoes partial clathrin-dependent endocytosis guided by clathrin adapter protein 2 (AP-2) (By similarity).By similarity1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: Alzheimers_University_of_Toronto
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Endosome
- early endosome Source: Alzheimers_University_of_Toronto
- early endosome membrane Source: UniProtKB-SubCell
- endosome Source: UniProtKB
- multivesicular body Source: UniProtKB
- multivesicular body membrane Source: UniProtKB-SubCell
- recycling endosome Source: Alzheimers_University_of_Toronto
- recycling endosome membrane Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular space Source: UniProtKB
Golgi apparatus
- Golgi apparatus Source: UniProtKB
- Golgi cisterna Source: Alzheimers_University_of_Toronto
- Golgi membrane Source: UniProtKB-SubCell
- trans-Golgi network Source: Alzheimers_University_of_Toronto
Nucleus
- nuclear envelope lumen Source: Alzheimers_University_of_Toronto
- perinucleolar compartment Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- cell surface Source: MGI
- integral component of membrane Source: UniProtKB
- membrane Source: MGI
- neuronal cell body Source: MGI
- perinuclear region of cytoplasm Source: MGI
- transport vesicle membrane Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 82 – 2138 | LumenalSequence analysisAdd BLAST | 2057 | |
Transmembranei | 2139 – 2159 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2160 – 2215 | CytoplasmicSequence analysisAdd BLAST | 56 |
Keywords - Cellular componenti
Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, SecretedPathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
PropeptideiPRO_0000033166 | 29 – 81 | Removed in mature formBy similarityAdd BLAST | 53 | |
ChainiPRO_0000033167 | 82 – 2215 | Sortilin-related receptorAdd BLAST | 2134 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 99 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 114 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 158 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 367 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 368 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 430 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 616 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 674 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 818 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 871 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1035 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1068 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1078 ↔ 1090 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1085 ↔ 1103 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1097 ↔ 1112 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1117 ↔ 1131 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1125 ↔ 1144 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1138 ↔ 1153 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1158 ↔ 1170 | PROSITE-ProRule annotation | ||
Glycosylationi | 1164 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1165 ↔ 1183 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1177 ↔ 1192 | PROSITE-ProRule annotation | ||
Glycosylationi | 1191 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1199 ↔ 1211 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1206 ↔ 1224 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1218 ↔ 1235 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1239 ↔ 1249 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1244 ↔ 1262 | PROSITE-ProRule annotation | ||
Glycosylationi | 1246 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1256 ↔ 1271 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1275 ↔ 1289 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1283 ↔ 1302 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1296 ↔ 1315 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1325 ↔ 1337 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1332 ↔ 1350 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1344 ↔ 1359 | PROSITE-ProRule annotation | ||
Glycosylationi | 1367 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1368 ↔ 1381 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1376 ↔ 1394 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1388 ↔ 1403 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1419 ↔ 1431 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1426 ↔ 1444 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1438 ↔ 1453 | PROSITE-ProRule annotation | ||
Glycosylationi | 1458 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1471 ↔ 1484 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1478 ↔ 1497 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1491 ↔ 1506 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1514 ↔ 1527 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1521 ↔ 1540 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1534 ↔ 1549 | PROSITE-ProRule annotation | ||
Glycosylationi | 1608 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1706 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1733 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1810 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1855 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1895 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1987 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2011 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2055 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2070 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2077 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2093 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 2207 | Phosphoserine; by ROCK2By similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
EPDi | O88307 |
MaxQBi | O88307 |
PaxDbi | O88307 |
PeptideAtlasi | O88307 |
PRIDEi | O88307 |
PTM databases
GlyConnecti | 2735, 14 N-Linked glycans (12 sites) |
GlyGeni | O88307, 28 sites |
iPTMneti | O88307 |
PhosphoSitePlusi | O88307 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000049313, Expressed in cerebellum and 337 other tissues |
Genevisiblei | O88307, MM |
Interactioni
Subunit structurei
After maturation cleavage, interacts (via N-terminus) with its own propeptide; this interaction prevents interaction with other ligands, including CRLF1, GDNF, GFRA1, IL6 and IL6R (By similarity).
Interacts (via N-terminal ectodomain) with APP, forming a 1:1 stoichiometric complex, including with isoforms APP695, APP751 and APP770; this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (PubMed:16174740, PubMed:16407538).
Also interacts with APP C-terminal fragment C99 and with Abeta40 (By similarity).
Interacts with beta-secretase BACE1/BACE; this interaction may affect BACE1-binding to APP and hence reduce BACE1-dependent APP cleavage (PubMed:16407538).
Interacts with LRPAP1/RAP (By similarity).
Interacts (via C-terminal cytosolic domain) with GGA1 and GGA2 (via N-terminal VHS domain) (By similarity).
Interacts with PACS1 (By similarity). May interact (via the N-terminal ectodomain) with the morphogenetic neuropeptide, also called head activator or HA; this interaction is impaired in the presence of propeptide (By similarity).
Interacts with neurotensin/NTS (By similarity).
Interacts (via the N-terminal ectodomain) with PDGFB homodimer (By similarity).
Interacts (via N-terminal ectodomain) with the uPA receptor PLAUR (By similarity).
Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to endocytosis (By similarity).
Also interacts with PAI1/SERPINE1 in complex with tPA/PLAT.
Interacts (via C-terminus) with AP-1 and AP-2 complexes (By similarity).
Interacts with BMPR1A and BMPR1B (PubMed:26584636).
Interacts with lipoprotein lipase LPL; this interaction is optimal in slightly acidic conditions (By similarity).
Interacts (via N-terminal ectodomain) with GDNF (via propeptide) and GDNF receptor alpha-1/GFRA1, either individually or in complex with each other (By similarity). The interaction with GDNF occurs mostly intracellularly (By similarity).
Also interacts with other GDNF receptor alpha family members, including GFRA2, GFRA3 and GFRA4 (By similarity).
Interacts with the insulin receptor INSR; this interaction strongly increases the surface exposure of INSR (PubMed:27322061).
Interacts (via cytosolic C-terminus) with STK39/SPAK (By similarity).
Interacts (via N-terminal ectodomain) with the heterodimeric complex CRLF1-CLC; within this complex, the interaction is mediated predominantly by the CRLF1 moiety (By similarity).
Interacts with CNTFR, as well as with the tripartite signaling complex formed by CRLF1, CLC and CNTFR (By similarity).
Interacts (via N-terminal ectodomain) with IL6; this interaction leads to IL6 internalization and lysosomal degradation. Binding of SOLRL1 secreted N-terminal ectodomain to IL6 may increase IL6 trans signaling (By similarity).
Interacts with secreted IL6R; this interaction leads to IL6R internalization (PubMed:28265003).
Also interacts with transmembrane IL6R; this interaction does not affect subcellular location.
Interacts with APOE (By similarity).
Interacts with apolipoprotein E-rich beta-VLDL (By similarity).
Interacts with APOA5; this interaction leads to APOA5 internalization and is abolished by heparin. Interaction with APOA5 results in enhanced binding to chylomicrons.
Interacts with ROCK2 (By similarity).
Interacts (via cytosolic C-terminus) with PPP3CB/calcineurin A beta (PubMed:25967121).
Interacts with NTRK2/TRKB; this interaction facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling (PubMed:23977241).
Interacts (via cytosolic C-terminus) with HSPA12A in an ADP-dependent manner; this interaction affects SORL1 internalization and subcellular localization (By similarity).
Interacts (via N-terminal ectodomain) with ERBB2/HER2 (By similarity).
By similarity7 PublicationsBinary interactionsi
Hide detailsGO - Molecular functioni
- ADP-ribosylation factor binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 203392, 2 interactors |
DIPi | DIP-42439N |
IntActi | O88307, 3 interactors |
MINTi | O88307 |
STRINGi | 10090.ENSMUSP00000058613 |
Miscellaneous databases
RNActi | O88307, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 136 – 147 | BNR 1Add BLAST | 12 | |
Repeati | 232 – 243 | BNR 2Add BLAST | 12 | |
Repeati | 441 – 452 | BNR 3Add BLAST | 12 | |
Repeati | 521 – 532 | BNR 4Add BLAST | 12 | |
Repeati | 562 – 573 | BNR 5Add BLAST | 12 | |
Repeati | 800 – 843 | LDL-receptor class B 1Add BLAST | 44 | |
Repeati | 844 – 887 | LDL-receptor class B 2Add BLAST | 44 | |
Repeati | 888 – 932 | LDL-receptor class B 3Add BLAST | 45 | |
Repeati | 933 – 972 | LDL-receptor class B 4Add BLAST | 40 | |
Repeati | 973 – 1013 | LDL-receptor class B 5Add BLAST | 41 | |
Domaini | 1026 – 1072 | EGF-likeAdd BLAST | 47 | |
Domaini | 1076 – 1114 | LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1115 – 1155 | LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 1156 – 1194 | LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1198 – 1236 | LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1238 – 1272 | LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 1273 – 1317 | LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 1323 – 1361 | LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1366 – 1405 | LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1417 – 1455 | LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1469 – 1508 | LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1512 – 1551 | LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1557 – 1649 | Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST | 93 | |
Domaini | 1653 – 1745 | Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST | 93 | |
Domaini | 1747 – 1846 | Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST | 100 | |
Domaini | 1844 – 1928 | Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST | 85 | |
Domaini | 1935 – 2030 | Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST | 96 | |
Domaini | 2031 – 2119 | Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST | 89 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2191 – 2215 | Required for efficient Golgi apparatus - endosome sortingBy similarityAdd BLAST | 25 | |
Regioni | 2202 – 2215 | Required for interaction with GGA1 and GGA2By similarityAdd BLAST | 14 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 2162 – 2165 | Potential nuclear localization signal for the C-terminal fragment generated by PSEN1By similarity | 4 | |
Motifi | 2173 – 2178 | Endocytosis signalSequence analysis | 6 | |
Motifi | 2209 – 2213 | DXXLL motif involved in the interaction with GGA1By similarity | 5 |
Sequence similaritiesi
Keywords - Domaini
EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1215, Eukaryota KOG3511, Eukaryota |
GeneTreei | ENSGT00990000203671 |
HOGENOMi | CLU_001389_0_0_1 |
InParanoidi | O88307 |
OMAi | IEGMAFD |
OrthoDBi | 1046610at2759 |
TreeFami | TF324918 |
Family and domain databases
CDDi | cd00063, FN3, 5 hits cd00112, LDLa, 11 hits |
Gene3Di | 2.120.10.30, 1 hit 2.130.10.10, 1 hit 2.60.40.10, 4 hits 4.10.400.10, 11 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR003961, FN3_dom IPR036116, FN3_sf IPR013783, Ig-like_fold IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt IPR031777, Sortilin_C IPR031778, Sortilin_N IPR006581, VPS10 IPR015943, WD40/YVTN_repeat-like_dom_sf |
Pfami | View protein in Pfam PF00041, fn3, 3 hits PF00057, Ldl_recept_a, 10 hits PF00058, Ldl_recept_b, 2 hits PF15902, Sortilin-Vps10, 1 hit PF15901, Sortilin_C, 1 hit |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00060, FN3, 6 hits SM00192, LDLa, 11 hits SM00135, LY, 5 hits SM00602, VPS10, 1 hit |
SUPFAMi | SSF49265, SSF49265, 3 hits SSF57424, SSF57424, 11 hits |
PROSITEi | View protein in PROSITE PS01186, EGF_2, 1 hit PS50853, FN3, 4 hits PS01209, LDLRA_1, 10 hits PS50068, LDLRA_2, 11 hits PS51120, LDLRB, 5 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 706 | S → F in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 768 | S → F in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 785 | S → W in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 796 | D → G in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 953 | R → G in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 1268 – 1269 | EQ → DE in BAA31219 (PubMed:9726247).Curated | 2 | |
Sequence conflicti | 1425 | H → A in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 1425 | H → R in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 1425 | H → R in CAA72732 (Ref. 4) Curated | 1 | |
Sequence conflicti | 1468 | F → L in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 1468 | F → L in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 1468 | F → L in CAA72732 (Ref. 4) Curated | 1 | |
Sequence conflicti | 1663 | S → R in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 1663 | S → R in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 1663 | S → R in CAA72732 (Ref. 4) Curated | 1 | |
Sequence conflicti | 1709 – 1713 | EIKNL → KKKKK in CAA72732 (Ref. 4) Curated | 5 | |
Sequence conflicti | 1807 | R → K in BAA31219 (PubMed:9726247).Curated | 1 | |
Sequence conflicti | 1807 | R → K in AAC16739 (PubMed:9510025).Curated | 1 | |
Sequence conflicti | 2130 | Q → H in BAA31219 (PubMed:9726247).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 |
Genome annotation databases
Ensembli | ENSMUST00000060989; ENSMUSP00000058613; ENSMUSG00000049313 |
GeneIDi | 20660 |
KEGGi | mmu:20660 |
UCSCi | uc009pap.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 |
3D structure databases
BMRBi | O88307 |
SMRi | O88307 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 203392, 2 interactors |
DIPi | DIP-42439N |
IntActi | O88307, 3 interactors |
MINTi | O88307 |
STRINGi | 10090.ENSMUSP00000058613 |
PTM databases
GlyConnecti | 2735, 14 N-Linked glycans (12 sites) |
GlyGeni | O88307, 28 sites |
iPTMneti | O88307 |
PhosphoSitePlusi | O88307 |
Proteomic databases
EPDi | O88307 |
MaxQBi | O88307 |
PaxDbi | O88307 |
PeptideAtlasi | O88307 |
PRIDEi | O88307 |
Protocols and materials databases
Antibodypediai | 32786, 238 antibodies |
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 | KOG1215, Eukaryota KOG3511, Eukaryota |
GeneTreei | ENSGT00990000203671 |
HOGENOMi | CLU_001389_0_0_1 |
InParanoidi | O88307 |
OMAi | IEGMAFD |
OrthoDBi | 1046610at2759 |
TreeFami | TF324918 |
Miscellaneous databases
BioGRID-ORCSi | 20660, 0 hits in 17 CRISPR screens |
ChiTaRSi | Sorl1, mouse |
PROi | PR:O88307 |
RNActi | O88307, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000049313, Expressed in cerebellum and 337 other tissues |
Genevisiblei | O88307, MM |
Family and domain databases
CDDi | cd00063, FN3, 5 hits cd00112, LDLa, 11 hits |
Gene3Di | 2.120.10.30, 1 hit 2.130.10.10, 1 hit 2.60.40.10, 4 hits 4.10.400.10, 11 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR003961, FN3_dom IPR036116, FN3_sf IPR013783, Ig-like_fold IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt IPR031777, Sortilin_C IPR031778, Sortilin_N IPR006581, VPS10 IPR015943, WD40/YVTN_repeat-like_dom_sf |
Pfami | View protein in Pfam PF00041, fn3, 3 hits PF00057, Ldl_recept_a, 10 hits PF00058, Ldl_recept_b, 2 hits PF15902, Sortilin-Vps10, 1 hit PF15901, Sortilin_C, 1 hit |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00060, FN3, 6 hits SM00192, LDLa, 11 hits SM00135, LY, 5 hits SM00602, VPS10, 1 hit |
SUPFAMi | SSF49265, SSF49265, 3 hits SSF57424, SSF57424, 11 hits |
PROSITEi | View protein in PROSITE PS01186, EGF_2, 1 hit PS50853, FN3, 4 hits PS01209, LDLRA_1, 10 hits PS50068, LDLRA_2, 11 hits PS51120, LDLRB, 5 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SORL_MOUSE | |
Accessioni | O88307Primary (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: | December 2, 2020 | |
This is version 183 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families