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UniProtKB - O88307 (SORL_MOUSE)

Entry version 182 (07 Oct 2020)
Sequence version 3 (27 Jul 2011)
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Protein

Sortilin-related receptor

Gene

Sorl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sorting receptor that directs several proteins to their correct location within the cell. Along with AP-1 complex, involved Golgi apparatus - endosome sorting. Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated. May also sort newly produced amyloid-beta peptides to lysosomes for catabolism. Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (By similarity). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor (PubMed:23977241). Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion (PubMed:21994944). Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities (PubMed:23333276). Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling (By similarity). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (By similarity). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (By similarity). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization (PubMed:27322061). Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB (PubMed:20385770, PubMed:25967121). Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (By similarity). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453). Promotes adhesion of monocytes (By similarity). Stimulates proliferation and migration of monocytes/macrophages. Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (PubMed:17332490). Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain (PubMed:23486467). Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway (PubMed:26584636). May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation (PubMed:26858303). May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R (PubMed:28265003).By similarity12 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Receptor
Biological processEndocytosis, Transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
LR111 Publication
SorLA-1
Sorting protein-related receptor containing LDLR class A repeats
Short name:
mSorLA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Sorl1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1202296, Sorl1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini82 – 2138LumenalSequence analysisAdd BLAST2057
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei2139 – 2159HelicalSequence analysisAdd BLAST21
Topological domaini2160 – 2215CytoplasmicSequence analysisAdd BLAST56

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Knockout mice are viable and fertile with no overt phenotype (PubMed:16174740). They tend to be lighter than their wild-type littermates, with reduced adiposity (PubMed:26584636, PubMed:27322061). On a high-fat diet, they show a reduced gain in body weight compared with wild-type littermates (PubMed:27322061). Mutant animals display improved serum biochemistry profiles compared to wild-type, with lower fasting glucose, insulin and triglyceride levels, particularly on high fat diet (PubMed:26584636, PubMed:27322061). On a high-fat diet, brown adipose tissue from knockout mice shows reduced lipid content and subcutaneous white adipose tissue contains smaller, less lipid replete adipocytes, with increased thermogenic markers (PubMed:26584636). Mutant animals exhibit an increased production of soluble APP and enhanced amount of neuron-associated amyloid-beta protein 40 and 42 in the brain at 10 months of age (PubMed:16174740). Following vascular injury, knockout mice placed on a high-fat diet show reduced intimal thickness and decreased infiltration of lipid-laden macrophages compared to wild-type littermates (PubMed:17332490). Mutant mice display elevated GDNF levels, altered dopaminergic function, marked hyperactivity, and reduced anxiety (PubMed:23333276). Knockout mice show a weak phenotype in the maintenance of renal ion balance. Under basal conditions, they exhibit significant urinary loss of potassium and calcium compared to controls. Serum Na+, Cl-, and K+ levels are normal, but aldosterone levels are elevated 2-fold. Mean arterial blood pressure is decreased despite the hyperaldosteronemic phenotype (PubMed:20385770). The lack of major renal phenotype in mutant mice may be explained by the fact that animals remain responsive to vasopressin endocrine stimulation (PubMed:25967121).7 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 28Sequence analysisAdd BLAST28
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000003316629 – 81Removed in mature formBy similarityAdd BLAST53
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003316782 – 2215Sortilin-related receptorAdd BLAST2134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei114PhosphoserineBy similarity1
Glycosylationi158N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi367N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi368N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi430N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi616N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi674N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi818N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi871N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1035N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1068N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
Glycosylationi1164N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1165 ↔ 1183PROSITE-ProRule annotation
Disulfide bondi1177 ↔ 1192PROSITE-ProRule annotation
Glycosylationi1191N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1246N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1367N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1458N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi1608N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1706N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1810N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1855N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1895N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1987N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2011N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2055N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2070N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2077N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2093N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei2207Phosphoserine; by ROCK2By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Within the Golgi apparatus, the propeptide may be cleaved off by FURIN or a furin-like protease. After cleavage, the propeptide interacts with the mature protein N-terminus, preventing the association with other ligands. At the cell surface, partially subjected to proteolytic shedding that releases the ectodomain in the extracellular milieu. 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.By similarity
Phosphorylation at Ser-2207 facilitates the interaction with GGA1.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O88307

MaxQB - The MaxQuant DataBase

More...MaxQBi		O88307

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O88307

PeptideAtlas

More...PeptideAtlasi		O88307

PRoteomics IDEntifications database

More...PRIDEi		O88307

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2735, 14 N-Linked glycans (12 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O88307, 28 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O88307

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O88307

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in the central nervous system, including in the brain and spinal cord, in neurons, as well as in glial cells (at protein level) (PubMed:9726247, PubMed:9510025, PubMed:11082041, PubMed:16174740, PubMed:21385844, PubMed:23333276, PubMed:23977241, PubMed:30679749). In the brain, mainly expressed in the cerebellum, hippocampus, dentate gyrus, hypothalamus, and in the cerebral cortex (at protein level) (PubMed:9726247, PubMed:9510025, PubMed:23333276, PubMed:27322061). Also detected in kidney, heart, lung and spleen (PubMed:9726247, PubMed:9510025). In the kidney, expressed in epithelial cells in the thick ascending limb of Henle's loop, the distal convoluted tubule, the connecting tubule and the cortical collecting duct (at protein level) (PubMed:20385770, PubMed:25967121). Expressed in skeletal muscle (at protein level) (PubMed:9726247, PubMed:9510025, PubMed:27322061). Expressed in adipose tissue, including in brown adipose tissue and subcutaneous white adipose tissue (PubMed:26584636, PubMed:27322061). Expressed in intimal smooth muscle cells (at protein level) (PubMed:14764453).13 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression starts at 6.5 dpc (PubMed:9726247, PubMed:9510025). At 7.5 dpc, expressed over the entire embryo, with highest levels in the amnion. Up to 8.5 dpc, expression further increases and becomes more restricted to the foregut and the amnion. At 9.5 dpc, expression increases in the somites, as well as the developing gut, and is observed over the facial-cranial mesenchyme and the branchial arches. At 10.5 dpc, expression in the mesenchyme and the somites reaches its maximal intensity. At this stage, highest expression level is observed over the ventral part of the neural tube, in the marginal zone, and extends throughout the hindbrain. Also expressed in motor neurons of the spinal cord. With ongoing development, the brain becomes the main site of expression. At 11.5 dpc, expressed in the telencephalon, being restricted to the lateral aspects of the developing cerebral cortex, with highest levels in the outer layer of the neuronal tissue of the developing cerebral cortex. Also observed in the myelencephalon and in a thin cell layer in the rhombic lip of the metencephalon. At 12.5 dpc, expression begins in the mesencephalon and the diencephalon. Up to 14.5 dpc, expression levels in the developing cerebral cortex become more even and spread to more dorsal and caudal locations. At 14.5 dpc, decreased expression in the metencephalon and the myelencephalon. At 16.5 dpc, expressed over the entire cortical area, although at a slightly lower intensity. Expressed in the hypothalamus. At this stage, expression begins in the peripheral nervous system, including in the trigeminal ganglion, the dorsal root ganglia, the cochlear-vestibular ganglia and the sympathetic ganglia chain, but at lower levels compared to the central nervous system. Expressed over the mitral cell layer of the olfactory bulb and between the 2 outer walls of the gut. The overall expression levels in the cortex decrease until birth. At 18.5 dpc, the outer aspects of the cortical plate shows lower expression levels than the subventricular zone. At 18.5 dpc, expressed in the retina and the geniculate nucleus of the thalamus; this expression increases towards P0. At P0, expression levels are higher in the outer aspects of the cortical plate than in the subventricular zone (PubMed:9510025). 1 week after birth, abundantly expressed in the cerebrum, then levels decrease and become nearly undetectable at 4 weeks. Expression increases again and reaches moderate levels at 12 weeks. In the cerebellum, expressed at high levels during the first 2 weeks. Expression decreases at 4 and 8 weeks, and then increases again at 12 weeks (PubMed:9726247). Expressed in many organs outside the nervous system during organogenesis, such as the primitive gut where expression is detected already at 8.5 dpc. Other SORL1-expressing organs include the genital bud, the mesenchymal tissue, the developing skeletal muscles, the myocardium, the pituitary, the pineal, the thyroid and the Haderian glands, as well as the developing serous glands of the nasal cavity, the salivary and the submandibular glands, the pancreas, the epithelia of the stomach, the tubules of the kidney, the tooth germ, the cochlea, the nasal cavity, the trachea, the lung, the bladder and urethra, the intestine and the rectum (PubMed:9510025).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by BDNF in cortical neurons (at protein level) (PubMed:20007471). Up-regulated under hypoxic conditions in hematopoietic stem and progenitor cells, a physiological conditions encountered by these cells in the endosteum (at protein level) (PubMed:23486467). In brown and sucutaneous white adipose tissues, down-regulated when environmental temperature rises from cold to thermoneutrality (PubMed:26584636). Up-regulated in adipose tissue by insulin through a post-transcriptional mechanism (PubMed:27322061). Expression levels increase in the fed state and decline after fasting (PubMed:26584636).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000049313, Expressed in cerebellum and 337 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O88307, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		203392, 2 interactors

Database of interacting proteins

More...DIPi		DIP-42439N

Protein interaction database and analysis system

More...IntActi		O88307, 3 interactors

Molecular INTeraction database

More...MINTi		O88307

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000058613

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O88307, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		O88307

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O88307

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati136 – 147BNR 1Add BLAST12
Repeati232 – 243BNR 2Add BLAST12
Repeati441 – 452BNR 3Add BLAST12
Repeati521 – 532BNR 4Add BLAST12
Repeati562 – 573BNR 5Add BLAST12
Repeati800 – 843LDL-receptor class B 1Add BLAST44
Repeati844 – 887LDL-receptor class B 2Add BLAST44
Repeati888 – 932LDL-receptor class B 3Add BLAST45
Repeati933 – 972LDL-receptor class B 4Add BLAST40
Repeati973 – 1013LDL-receptor class B 5Add BLAST41
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1026 – 1072EGF-likeAdd BLAST47
Domaini1076 – 1114LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini1115 – 1155LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini1156 – 1194LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini1198 – 1236LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST39
Domaini1238 – 1272LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST35
Domaini1273 – 1317LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST45
Domaini1323 – 1361LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST39
Domaini1366 – 1405LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST40
Domaini1417 – 1455LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST39
Domaini1469 – 1508LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST40
Domaini1512 – 1551LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST40
Domaini1557 – 1649Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST93
Domaini1653 – 1745Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST93
Domaini1747 – 1846Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST100
Domaini1844 – 1928Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST85
Domaini1935 – 2030Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST96
Domaini2031 – 2119Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2191 – 2215Required for efficient Golgi apparatus - endosome sortingBy similarityAdd BLAST25
Regioni2202 – 2215Required for interaction with GGA1 and GGA2By similarityAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi2162 – 2165Potential nuclear localization signal for the C-terminal fragment generated by PSEN1By similarity4
Motifi2173 – 2178Endocytosis signalSequence analysis6
Motifi2209 – 2213DXXLL motif involved in the interaction with GGA1By similarity5

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the VPS10-related sortilin family. SORL1 subfamily.Curated

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1215, Eukaryota
KOG3511, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00990000203671

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001389_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O88307

Identification of Orthologs from Complete Genome Data

More...OMAi		IEGMAFD

Database of Orthologous Groups

More...OrthoDBi		1046610at2759

TreeFam database of animal gene trees

More...TreeFami		TF324918

Family and domain databases

Conserved Domains Database

More...CDDi		cd00063, FN3, 5 hits
cd00112, LDLa, 11 hits

Gene3D Structural and Functional Annotation of Protein Families

More...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

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00261, LDLRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00060, FN3, 6 hits
SM00192, LDLa, 11 hits
SM00135, LY, 5 hits
SM00602, VPS10, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49265, SSF49265, 3 hits
SSF57424, SSF57424, 11 hits

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O88307-1 [UniParc]FASTAAdd to basket
« Hide
        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5D7F53806EFE2CB0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti706S → F in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti768S → F in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti785S → W in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti796D → G in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti953R → G in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti1268 – 1269EQ → DE in BAA31219 (PubMed:9726247).Curated2
Sequence conflicti1425H → A in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti1425H → R in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti1425H → R in CAA72732 (Ref. 4) Curated1
Sequence conflicti1468F → L in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti1468F → L in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti1468F → L in CAA72732 (Ref. 4) Curated1
Sequence conflicti1663S → R in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti1663S → R in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti1663S → R in CAA72732 (Ref. 4) Curated1
Sequence conflicti1709 – 1713EIKNL → KKKKK in CAA72732 (Ref. 4) Curated5
Sequence conflicti1807R → K in BAA31219 (PubMed:9726247).Curated1
Sequence conflicti1807R → K in AAC16739 (PubMed:9510025).Curated1
Sequence conflicti2130Q → H in BAA31219 (PubMed:9726247).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB015790 mRNA Translation: BAA31219.1
AK147303 mRNA Translation: BAE27834.1
AF031816 mRNA Translation: AAC16739.1
Y12004 mRNA Translation: CAA72732.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS40594.1

Protein sequence database of the Protein Information Resource

More...PIRi		T00348

NCBI Reference Sequences

More...RefSeqi		NP_035566.2, NM_011436.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000060989; ENSMUSP00000058613; ENSMUSG00000049313

Database of genes from NCBI RefSeq genomes

More...GeneIDi		20660

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:20660

UCSC genome browser

More...UCSCi		uc009pap.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS40594.1
PIRiT00348
RefSeqiNP_035566.2, NM_011436.3

3D structure databases

BMRBiO88307
SMRiO88307
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi203392, 2 interactors
DIPiDIP-42439N
IntActiO88307, 3 interactors
MINTiO88307
STRINGi10090.ENSMUSP00000058613

PTM databases

GlyConnecti2735, 14 N-Linked glycans (12 sites)
GlyGeniO88307, 28 sites
iPTMnetiO88307
PhosphoSitePlusiO88307

Proteomic databases

EPDiO88307
MaxQBiO88307
PaxDbiO88307
PeptideAtlasiO88307
PRIDEiO88307

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		32786, 238 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6653
MGIiMGI:1202296, Sorl1

Phylogenomic databases

eggNOGiKOG1215, Eukaryota
KOG3511, Eukaryota
GeneTreeiENSGT00990000203671
HOGENOMiCLU_001389_0_0_1
InParanoidiO88307
OMAiIEGMAFD
OrthoDBi1046610at2759
TreeFamiTF324918

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		20660, 0 hits in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Sorl1, mouse

Protein Ontology

More...PROi		PR:O88307
RNActiO88307, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000049313, Expressed in cerebellum and 337 other tissues
GenevisibleiO88307, MM

Family and domain databases

CDDicd00063, FN3, 5 hits
cd00112, LDLa, 11 hits
Gene3Di2.120.10.30, 1 hit
2.130.10.10, 1 hit
2.60.40.10, 4 hits
4.10.400.10, 11 hits
InterProiView 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
PfamiView 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
PRINTSiPR00261, LDLRECEPTOR
SMARTiView protein in SMART
SM00060, FN3, 6 hits
SM00192, LDLa, 11 hits
SM00135, LY, 5 hits
SM00602, VPS10, 1 hit
SUPFAMiSSF49265, SSF49265, 3 hits
SSF57424, SSF57424, 11 hits
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSORL_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O88307
Secondary accession number(s): O54711, O70581, Q3UHM3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: October 7, 2020
This is version 182 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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
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