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Entry version 136 (07 Oct 2020)
Sequence version 1 (01 Feb 1997)
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Protein

Sortilin-related receptor

Gene

SORL1

Organism
Oryctolagus cuniculus (Rabbit)
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. 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. Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion. 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. 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. Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL. 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. 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 (By similarity). 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 (By similarity). 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 acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453, PubMed:17332490). Promotes adhesion of monocytes (By similarity). Stimulates proliferation and migration of monocytes/macrophages (PubMed:17332490). Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (By similarity). 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 (By similarity). 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 (By similarity). 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. 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 (By similarity).By similarity2 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 - Biological processi

<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 functionReceptor
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):
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:
SorLA
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<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
  • UP000001811 <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: Unplaced

<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

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 – 2136LumenalSequence analysisAdd BLAST2055
<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>Transmembranei2137 – 2157HelicalSequence analysisAdd BLAST21
Topological domaini2158 – 2213CytoplasmicSequence analysisAdd BLAST56

Keywords - Cellular componenti

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

<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_000003316829 – 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_000003316982 – 2213Sortilin-related receptorAdd BLAST2132

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
Glycosylationi368N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi430N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi616N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi674N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi817N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi870N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1034N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1067N-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 bondi1077 ↔ 1089PROSITE-ProRule annotation
Disulfide bondi1084 ↔ 1102PROSITE-ProRule annotation
Disulfide bondi1096 ↔ 1111PROSITE-ProRule annotation
Disulfide bondi1116 ↔ 1130PROSITE-ProRule annotation
Disulfide bondi1124 ↔ 1143PROSITE-ProRule annotation
Disulfide bondi1137 ↔ 1152PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1169PROSITE-ProRule annotation
Glycosylationi1163N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1164 ↔ 1182PROSITE-ProRule annotation
Disulfide bondi1176 ↔ 1191PROSITE-ProRule annotation
Glycosylationi1190N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1198 ↔ 1210PROSITE-ProRule annotation
Disulfide bondi1205 ↔ 1223PROSITE-ProRule annotation
Disulfide bondi1217 ↔ 1234PROSITE-ProRule annotation
Disulfide bondi1238 ↔ 1248PROSITE-ProRule annotation
Disulfide bondi1243 ↔ 1261PROSITE-ProRule annotation
Glycosylationi1245N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1255 ↔ 1270PROSITE-ProRule annotation
Disulfide bondi1274 ↔ 1288PROSITE-ProRule annotation
Disulfide bondi1282 ↔ 1301PROSITE-ProRule annotation
Disulfide bondi1295 ↔ 1314PROSITE-ProRule annotation
Disulfide bondi1324 ↔ 1336PROSITE-ProRule annotation
Disulfide bondi1331 ↔ 1349PROSITE-ProRule annotation
Disulfide bondi1343 ↔ 1358PROSITE-ProRule annotation
Glycosylationi1366N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1367 ↔ 1380PROSITE-ProRule annotation
Disulfide bondi1375 ↔ 1393PROSITE-ProRule annotation
Disulfide bondi1387 ↔ 1402PROSITE-ProRule annotation
Disulfide bondi1418 ↔ 1430PROSITE-ProRule annotation
Disulfide bondi1425 ↔ 1443PROSITE-ProRule annotation
Disulfide bondi1437 ↔ 1452PROSITE-ProRule annotation
Glycosylationi1457N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1470 ↔ 1483PROSITE-ProRule annotation
Disulfide bondi1477 ↔ 1496PROSITE-ProRule annotation
Disulfide bondi1490 ↔ 1505PROSITE-ProRule annotation
Disulfide bondi1513 ↔ 1526PROSITE-ProRule annotation
Disulfide bondi1520 ↔ 1539PROSITE-ProRule annotation
Disulfide bondi1533 ↔ 1548PROSITE-ProRule annotation
Glycosylationi1569N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1607N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1705N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1732N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1808N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1853N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1893N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1985N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2009N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2053N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2068N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2075N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2091N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei2205Phosphoserine; 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-2205 facilitates the interaction with GGA1.By similarity

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q95209

<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

Expressed in brain, in particular the hippocampus, dentate gyrus, and cerebral cortex (at protein level) (PubMed:8798746). Also detected in liver, adrenal glands, pancreas and testis (PubMed:8798746). Expressed in smooth muscle cells, predominantly during proliferation (PubMed:14764453).2 Publications

<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.

Interacts (via N-terminal ectodomain) with APP, forming a 1:1 stoichiometric complex; this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides.

Also interacts with APP C-terminal fragment C99 and with Abeta40.

Interacts with beta-secretase BACE1/BACE; this interaction may affect BACE1-binding to APP and hence reduce BACE1-dependent APP cleavage.

Interacts with LRPAP1/RAP.

Interacts (via C-terminal cytosolic domain) with GGA1 and GGA2 (via N-terminal VHS domain).

Interacts with PACS1. 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.

Interacts with neurotensin/NTS.

Interacts (via the N-terminal ectodomain) with PDGFB homodimer.

Interacts (via N-terminal ectodomain) with the uPA receptor PLAUR.

Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to endocytosis.

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 (By similarity).

Interacts with lipoprotein lipase LPL; this interaction is optimal in slightly acidic conditions.

Interacts (via N-terminal ectodomain) with GDNF (via propeptide) and GDNF receptor alpha-1/GFRA1, either individually or in complex with each other. The interaction with GDNF occurs mostly intracellularly.

Also interacts with other GDNF receptor alpha family members, including GFRA2, GFRA3 and GFRA4.

Interacts with the insulin receptor INSR; this interaction strongly increases the surface exposure of INSR.

Interacts (via cytosolic C-terminus) with STK39/SPAK.

Interacts (via N-terminal ectodomain) with the heterodimeric complex CRLF1-CLC; within this complex, the interaction is mediated predominantly by the CRLF1 moiety.

Interacts with CNTFR, as well as with the tripartite signaling complex formed by CRLF1, CLC and CNTFR.

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.

Interacts with secreted IL6R; this interaction leads to IL6R internalization.

Also interacts with transmembrane IL6R; this interaction does not affect subcellular location.

Interacts with APOE (By similarity).

Interacts with apolipoprotein E-rich beta-VLDL (PubMed:8798746).

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.

Interacts with NTRK2/TRKB; this interaction facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling (By similarity).

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 similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
1172398, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000009783

<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
Q95209

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

More...
SMRi
Q95209

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
Repeati799 – 842LDL-receptor class B 1Add BLAST44
Repeati843 – 886LDL-receptor class B 2Add BLAST44
Repeati887 – 929LDL-receptor class B 3Add BLAST43
Repeati930 – 971LDL-receptor class B 4Add BLAST42
Repeati972 – 1012LDL-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>Domaini1025 – 1071EGF-likeAdd BLAST47
Domaini1075 – 1113LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini1114 – 1154LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini1155 – 1193LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini1196 – 1235LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST40
Domaini1237 – 1271LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST35
Domaini1272 – 1316LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST45
Domaini1322 – 1360LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST39
Domaini1365 – 1404LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST40
Domaini1416 – 1454LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST39
Domaini1468 – 1507LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST40
Domaini1511 – 1550LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST40
Domaini1556 – 1648Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST93
Domaini1652 – 1744Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST93
Domaini1748 – 1843Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini1842 – 1926Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST85
Domaini1933 – 2028Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST96
Domaini2029 – 2117Fibronectin 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>Regioni2189 – 2213Required for efficient Golgi apparatus - endosome sortingBy similarityAdd BLAST25
Regioni2200 – 2213Required 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>Motifi63 – 65Cell attachment siteSequence analysis3
Motifi2160 – 2163Potential nuclear localization signal for the C-terminal fragment generated by PSEN1By similarity4
Motifi2171 – 2176Endocytosis signalSequence analysis6
Motifi2207 – 2211DXXLL motif involved in the interaction with GGA1By similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi78 – 81Poly-Arg4

<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

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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q95209

Database of Orthologous Groups

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OrthoDBi
1046610at2759

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

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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, 1 hit
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.

Q95209-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTRTLHGGRA PLPQERGFRV
60 70 80 90 100
VQGDPRELRL WERGDARGAS RADEKPLRRR RSAALQPEPI KVYGQVSLND
110 120 130 140 150
SHNQMVVHWA GEKSNVIVAL ARDSLALARP RSSDVYVSYD YGKSFNKISE
160 170 180 190 200
KLNFGAGNNT EAVVAQFYHS PADNKRYIFA DAYAQYLWIT FDFCNTIHGF
210 220 230 240 250
SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT WIMIQEHVKS
260 270 280 290 300
FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF
310 320 330 340 350
QLRDKYMFAT KVVHLLGSPL QSSVQLWVSF GRKPMRAAQF VTRHPINEYY
360 370 380 390 400
IADASEDQVF VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYTPGGAGSD
410 420 430 440 450
TLVRYFANEP FADFHRVEGL QGVYIATLIN GSMNEENMRS VITFDKGGTW
460 470 480 490 500
EFLQAPAFTG YGEKINCELS EGCSLHLAQR LSQLLNLQLR RMPILSKESA
510 520 530 540 550
PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY TWGDHGGIIM
560 570 580 590 600
AIAQGMETNE LKYSTNEGET WKAFTFSEKP VFVYGLLTEP GEKSTVFTIF
610 620 630 640 650
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV
660 670 680 690 700
FKRRTPHATC FNGEDFDRPV VVSNCSCTRE DYECDFGFRM SEDLALEVCV
710 720 730 740 750
PDPGFSGKSS PPVPCPVGST YRRSRGYRKI SGDTCSGGDV EARLEGELVP
760 770 780 790 800
CPLAEENEFI LYATRKSIHR YDLASGTTEQ LPLTGLRAAV ALDFDYEHNC
810 820 830 840 850
LYWSDLALDV IQRLCLNGST GQEVIINSDL ETVEALAFEP LSQLLYWVDA
860 870 880 890 900
GFKKIEVANP DGDFRLTVVN SSVLDRPRAL VLVPQEGIMF WTDWGDLKPG
910 920 930 940 950
IYRSNMDGSA AYRLVSEDVK WPNGISVDDQ WIYWTDAYLD CIERITFSGQ
960 970 980 990 1000
QRSVILDRLP HPYAIAVFKN EIYWDDWSQL SIFRASKYSG SQMEILASQL
1010 1020 1030 1040 1050
TGLMDMKIFY KGKNTGSNAC VPRPCSLLCL PRANNSKSCR CPDGVASSVL
1060 1070 1080 1090 1100
PSGDLMCDCP KGYELKNNTC VKEEDTCLRN QYRCSNGNCI NSIWWCDFDN
1110 1120 1130 1140 1150
DCGDMSDEKN CPTTICDLDT QFRCQESGTC IPLSYKCDLE DDCGDNSDER
1160 1170 1180 1190 1200
HCEMHQCRSD EYNCSSGMCI RSSWVCDGDN DCRDWSDEAN CTAIYHTCEA
1210 1220 1230 1240 1250
SNFQCRNGHC IPQRWACDGD ADCQDGSDED PANCEKKCNG FRCPNGTCIP
1260 1270 1280 1290 1300
STKHCDGLHD CSDGSDEQHC EPLCTRFMDF VCKNRQQCLF HSMVCDGIIQ
1310 1320 1330 1340 1350
CRDGSDEDPA FAGCSRDPEF HKVCDEFGFQ CQNGVCISLI WKCDGMDDCG
1360 1370 1380 1390 1400
DYSDEANCEN PTEAPNCSRY FQFRCDNGHC IPNRWKCDRE NDCGDWSDEK
1410 1420 1430 1440 1450
DCGDSHVLPS TTPAPSTCLP NYYRCGGGAC VIDTWVCDGY RDCADGSDEE
1460 1470 1480 1490 1500
ACPSLPNVTA TSSPSQPGRC DRFEFECHQP KKCIPNWRRC DGHQDCQDGQ
1510 1520 1530 1540 1550
DEANCPTHST LTCMSWEFKC EDGEACIVLS ERCDGFLDCS DESDEKACSD
1560 1570 1580 1590 1600
ELTVYKVQNL QWTADFSGNV TLTWMRPKKM PSAACVYNVY YRVVGESIWK
1610 1620 1630 1640 1650
TLETHSNKTN TVLKVLKPDT TYQVKVQVQC LSKVHNTNDF VTLRTPEGLP
1660 1670 1680 1690 1700
DAPQNLQLSL HGEEEGVIVG HWSPPTHTHG LIREYIVEYS RSGSKVWTSE
1710 1720 1730 1740 1750
RAASNFTEIK NLLVNTLYTV RVAAVTSRGI GNWSDSKSIT TVKGKAIPPP
1760 1770 1780 1790 1800
NIHIDNYDEN SLSFTLTVDG NIKVNGYVVN LFWAFDTHKQ EKKTMNFQGS
1810 1820 1830 1840 1850
SVSHKVGNLT AQTAYEISAW AKTDLGDSPL SFEHVTTRGV RPPAPSLKAR
1860 1870 1880 1890 1900
AINQTAVECT WTGPRNVVYG IFYATSFLDL YRNPSSLTTP LHNATVLVGK
1910 1920 1930 1940 1950
DEQYLFLVRV VMPYQGPSSD YVVVKMIPDS RLPPRHLHAV HTGKTSAVIK
1960 1970 1980 1990 2000
WESPYDSPDQ DLFYAIAVKD LIRKTDRSYK VKSRNSTVEY TLSKLEPGGK
2010 2020 2030 2040 2050
YHVIVQLGNM SKDASVKITT VSLSAPDALK IITENDHVLL FWKSLALKEK
2060 2070 2080 2090 2100
YFNESRGYEI HMFDSAMNIT AYLGNTTDNF FKISNLKMGH NYTFTVQARC
2110 2120 2130 2140 2150
LLGSQICGEP AVLLYDELGS GGDASAMQAA RSTDVAAVVV PILFLILLSL
2160 2170 2180 2190 2200
GVGFAILYTK HRRLQSSFTA FANSHYSSRL GSAIFSSGDD LGEDDEDAPM
2210
ITGFSDDVPM VIA
Length:2,213
Mass (Da):247,766
Last modified:February 1, 1997 - v1
<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:iA54232645A5A0DDA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D86350 mRNA Translation: BAA13075.1

NCBI Reference Sequences

More...
RefSeqi
NP_001076133.1, NM_001082664.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009378

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009378

<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
D86350 mRNA Translation: BAA13075.1
RefSeqiNP_001076133.1, NM_001082664.1

3D structure databases

BMRBiQ95209
SMRiQ95209
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi1172398, 1 interactor
STRINGi9986.ENSOCUP00000009783

Proteomic databases

PRIDEiQ95209

Genome annotation databases

GeneIDi100009378
KEGGiocu:100009378

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6653

Phylogenomic databases

eggNOGiKOG1215, Eukaryota
KOG3511, Eukaryota
InParanoidiQ95209
OrthoDBi1046610at2759

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, 1 hit
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_RABIT
<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: Q95209
<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: February 1, 1997
Last modified: October 7, 2020
This is version 136 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
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