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Protein

Sortilin-related receptor

Gene

SORL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. Involved in APP trafficking to and from the Golgi apparatus. It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta, thereby reducing the burden of amyloidogenic peptide formation. Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization.2 Publications

GO - Molecular functioni

  • ADP-ribosylation factor binding Source: Alzheimers_University_of_Toronto
  • beta-amyloid binding Source: Alzheimers_University_of_Toronto
  • low-density lipoprotein particle binding Source: BHF-UCL
  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • lipid transport Source: UniProtKB-KW
  • negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
  • negative regulation of beta-amyloid formation Source: Alzheimers_University_of_Toronto
  • negative regulation of MAP kinase activity Source: Alzheimers_University_of_Toronto
  • negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
  • negative regulation of neurofibrillary tangle assembly Source: Alzheimers_University_of_Toronto
  • negative regulation of neurogenesis Source: Alzheimers_University_of_Toronto
  • negative regulation of neuron death Source: Alzheimers_University_of_Toronto
  • negative regulation of protein binding Source: Alzheimers_University_of_Toronto
  • negative regulation of protein oligomerization Source: Alzheimers_University_of_Toronto
  • negative regulation of tau-protein kinase activity Source: Alzheimers_University_of_Toronto
  • positive regulation of choline O-acetyltransferase activity Source: Alzheimers_University_of_Toronto
  • positive regulation of early endosome to recycling endosome transport Source: Alzheimers_University_of_Toronto
  • positive regulation of endocytic recycling Source: Alzheimers_University_of_Toronto
  • positive regulation of ER to Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
  • positive regulation of protein catabolic process Source: Alzheimers_University_of_Toronto
  • positive regulation of protein exit from endoplasmic reticulum Source: Alzheimers_University_of_Toronto
  • positive regulation of protein localization to early endosome Source: Alzheimers_University_of_Toronto
  • post-Golgi vesicle-mediated transport Source: Alzheimers_University_of_Toronto
  • protein maturation Source: Alzheimers_University_of_Toronto
  • protein retention in Golgi apparatus Source: Alzheimers_University_of_Toronto
  • protein targeting Source: UniProtKB
  • protein targeting to Golgi Source: Alzheimers_University_of_Toronto
  • protein targeting to lysosome Source: Alzheimers_University_of_Toronto
  • receptor-mediated endocytosis Source: ProtInc
  • regulation of smooth muscle cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137642-MONOMER.
ReactomeiR-HSA-977225. Amyloid fiber formation.
SIGNORiQ92673.

Names & Taxonomyi

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:
LR11
SorLA-1
Sorting protein-related receptor containing LDLR class A repeats
Short name:
SorLA
Gene namesi
Name:SORL1
Synonyms:C11orf32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11185. SORL1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini82 – 2137ExtracellularSequence analysisAdd BLAST2056
Transmembranei2138 – 2158HelicalSequence analysisAdd BLAST21
Topological domaini2159 – 2214CytoplasmicSequence analysisAdd BLAST56

GO - Cellular componenti

  • early endosome Source: Alzheimers_University_of_Toronto
  • endoplasmic reticulum Source: Alzheimers_University_of_Toronto
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi cisterna Source: Alzheimers_University_of_Toronto
  • integral component of plasma membrane Source: ProtInc
  • low-density lipoprotein particle Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nuclear envelope lumen Source: Alzheimers_University_of_Toronto
  • recycling endosome Source: Alzheimers_University_of_Toronto
  • trans-Golgi network Source: Alzheimers_University_of_Toronto
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, LDL, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Alzheimer disease (AD)3 Publications
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionAlzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
See also OMIM:104300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070012141Y → C in AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070013511G → R in AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070014924N → S in AD; unknown pathological significance. 1 PublicationCorresponds to variant rs377498269dbSNPEnsembl.1
Natural variantiVAR_0700151358N → S in AD; unknown pathological significance. 1 PublicationCorresponds to variant rs747306346dbSNPEnsembl.1
Natural variantiVAR_0700161681G → D in AD; unknown pathological significance. 1 Publication1

Keywords - Diseasei

Alzheimer disease, Amyloidosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi6653.
MalaCardsiSORL1.
MIMi104300. phenotype.
OpenTargetsiENSG00000137642.
Orphaneti1020. Early-onset autosomal dominant Alzheimer disease.
PharmGKBiPA36022.

Polymorphism and mutation databases

BioMutaiSORL1.
DMDMi296452912.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000003316429 – 81Removed in mature form1 PublicationAdd BLAST53
ChainiPRO_000003316582 – 2214Sortilin-related receptorAdd BLAST2133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi99N-linked (GlcNAc...)1 Publication1
Modified residuei114PhosphoserineCombined sources1
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Glycosylationi368N-linked (GlcNAc...)Sequence analysis1
Glycosylationi430N-linked (GlcNAc...)Sequence analysis1
Glycosylationi616N-linked (GlcNAc...)Sequence analysis1
Glycosylationi674N-linked (GlcNAc...)Sequence analysis1
Glycosylationi818N-linked (GlcNAc...)Sequence analysis1
Glycosylationi871N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1035N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1068N-linked (GlcNAc...)Sequence analysis1
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...)Sequence analysis1
Disulfide bondi1165 ↔ 1183PROSITE-ProRule annotation
Disulfide bondi1177 ↔ 1192PROSITE-ProRule annotation
Glycosylationi1191N-linked (GlcNAc...)Sequence 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...)Sequence 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...)Sequence 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...)Sequence 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...)Sequence analysis1
Glycosylationi1706N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1733N-linked (GlcNAc...)1 Publication1
Glycosylationi1809N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1854N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1894N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1986N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2010N-linked (GlcNAc...)1 Publication1
Glycosylationi2054N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2069N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2076N-linked (GlcNAc...)1 Publication1
Glycosylationi2092N-linked (GlcNAc...)1 Publication1
Modified residuei2206Phosphoserine; by ROCK21 Publication1

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

EPDiQ92673.
MaxQBiQ92673.
PaxDbiQ92673.
PeptideAtlasiQ92673.
PRIDEiQ92673.

PTM databases

iPTMnetiQ92673.
PhosphoSitePlusiQ92673.

Expressioni

Tissue specificityi

Expressed mainly in brain, where it is most abundant in the cerebellum, cerebral cortex and the occipital pole; low expression in the putamen and the thalamus. Expression is significantly reduced in the frontal cortex of patients suffering from Alzheimer disease. According to PubMed:9157966, found in spinal cord, testis, liver, kidney and pancreas with detectable levels in placenta, lung and heart. According to PubMed:8940146, expressed in the prostate, ovary, thyroid and spleen, but not found in kidney, liver, lung, skeletal muscle, bone marrow and adrenals.1 Publication

Gene expression databases

BgeeiENSG00000137642.
CleanExiHS_SORL1.
ExpressionAtlasiQ92673. baseline and differential.
GenevisibleiQ92673. HS.

Organism-specific databases

HPAiCAB011500.
HPA031321.

Interactioni

Subunit structurei

Interacts with GGA1 and ROCK2. Interacts with PLAUR. Interacts with APP.4 Publications

GO - Molecular functioni

  • ADP-ribosylation factor binding Source: Alzheimers_University_of_Toronto

Protein-protein interaction databases

BioGridi112536. 49 interactors.
DIPiDIP-41229N.
IntActiQ92673. 12 interactors.
MINTiMINT-231252.
STRINGi9606.ENSP00000260197.

Structurei

Secondary structure

12214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 51Combined sources4
Beta strandi91 – 98Combined sources8
Beta strandi103 – 109Combined sources7
Beta strandi117 – 122Combined sources6
Beta strandi125 – 128Combined sources4
Beta strandi133 – 140Combined sources8
Beta strandi145 – 147Combined sources3
Helixi149 – 151Combined sources3
Beta strandi164 – 169Combined sources6
Beta strandi177 – 192Combined sources16
Beta strandi198 – 201Combined sources4
Beta strandi207 – 211Combined sources5
Beta strandi219 – 223Combined sources5
Beta strandi230 – 236Combined sources7
Beta strandi242 – 253Combined sources12
Turni256 – 258Combined sources3
Beta strandi264 – 268Combined sources5
Beta strandi271 – 273Combined sources3
Beta strandi275 – 282Combined sources8
Helixi287 – 289Combined sources3
Beta strandi290 – 298Combined sources9
Beta strandi300 – 303Combined sources4
Beta strandi306 – 313Combined sources8
Beta strandi318 – 320Combined sources3
Beta strandi323 – 330Combined sources8
Beta strandi333 – 337Combined sources5
Beta strandi349 – 353Combined sources5
Beta strandi355 – 358Combined sources4
Beta strandi360 – 363Combined sources4
Helixi366 – 368Combined sources3
Beta strandi369 – 374Combined sources6
Beta strandi383 – 391Combined sources9
Beta strandi394 – 396Combined sources3
Turni397 – 400Combined sources4
Helixi402 – 405Combined sources4
Beta strandi411 – 416Combined sources6
Beta strandi420 – 422Combined sources3
Beta strandi424 – 428Combined sources5
Beta strandi431 – 434Combined sources4
Helixi435 – 437Combined sources3
Beta strandi439 – 445Combined sources7
Beta strandi451 – 453Combined sources3
Beta strandi460 – 462Combined sources3
Helixi469 – 471Combined sources3
Beta strandi473 – 479Combined sources7
Helixi480 – 485Combined sources6
Beta strandi492 – 495Combined sources4
Beta strandi504 – 510Combined sources7
Beta strandi519 – 525Combined sources7
Beta strandi531 – 536Combined sources6
Beta strandi538 – 543Combined sources6
Helixi544 – 546Combined sources3
Beta strandi548 – 553Combined sources6
Beta strandi560 – 566Combined sources7
Beta strandi572 – 575Combined sources4
Beta strandi577 – 579Combined sources3
Beta strandi581 – 588Combined sources8
Beta strandi596 – 602Combined sources7
Turni604 – 607Combined sources4
Beta strandi610 – 616Combined sources7
Helixi618 – 621Combined sources4
Helixi627 – 629Combined sources3
Beta strandi630 – 633Combined sources4
Helixi635 – 637Combined sources3
Turni638 – 641Combined sources4
Beta strandi647 – 654Combined sources8
Beta strandi670 – 674Combined sources5
Helixi679 – 681Combined sources3
Beta strandi682 – 684Combined sources3
Beta strandi688 – 690Combined sources3
Helixi694 – 696Combined sources3
Beta strandi699 – 701Combined sources3
Helixi703 – 705Combined sources3
Beta strandi722 – 724Combined sources3
Beta strandi727 – 730Combined sources4
Turni740 – 745Combined sources6
Beta strandi748 – 750Combined sources3
Beta strandi1655 – 1660Combined sources6
Beta strandi1669 – 1674Combined sources6
Beta strandi1683 – 1692Combined sources10
Beta strandi1699 – 1710Combined sources12
Beta strandi1718 – 1729Combined sources12
Beta strandi1731 – 1734Combined sources4
Beta strandi1738 – 1741Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DM4NMR-A1651-1745[»]
3G2SX-ray1.70C/D2202-2214[»]
3G2TX-ray2.00C/D2202-2214[»]
3WSXX-ray2.35A29-753[»]
3WSYX-ray3.11A86-753[»]
C42-56[»]
3WSZX-ray3.20A86-753[»]
ProteinModelPortaliQ92673.
SMRiQ92673.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 – 970LDL-receptor class B 4Add BLAST38
Repeati971 – 1013LDL-receptor class B 5Add BLAST43
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
Domaini1749 – 1844Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini1843 – 1927Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST85
Domaini1934 – 2029Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST96
Domaini2030 – 2118Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST89

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi63 – 65Cell attachment siteSequence analysis3
Motifi2172 – 2177Endocytosis signalSequence analysis6

Sequence similaritiesi

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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
KOG3511. Eukaryota.
ENOG410Y3W5. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000007009.
HOVERGENiHBG017830.
InParanoidiQ92673.
OMAiESDEKAC.
OrthoDBiEOG091G00GS.
PhylomeDBiQ92673.
TreeFamiTF324918.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 5 hits.
4.10.400.10. 10 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR031777. Sortilin_C.
IPR031778. Sortilin_N.
IPR006581. VPS10.
[Graphical view]
PfamiPF00041. 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.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00060. FN3. 6 hits.
SM00192. LDLa. 11 hits.
SM00135. LY. 5 hits.
SM00602. VPS10. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF57424. SSF57424. 11 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50853. FN3. 4 hits.
PS01209. LDLRA_1. 10 hits.
PS50068. LDLRA_2. 11 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQRLHGGSA PLPQDRGFLV
60 70 80 90 100
VQGDPRELRL WARGDARGAS RADEKPLRRK RSAALQPEPI KVYGQVSLND
110 120 130 140 150
SHNQMVVHWA GEKSNVIVAL ARDSLALARP KSSDVYVSYD YGKSFKKISD
160 170 180 190 200
KLNFGLGNRS EAVIAQFYHS PADNKRYIFA DAYAQYLWIT FDFCNTLQGF
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 KVVHLLGSEQ QSSVQLWVSF GRKPMRAAQF VTRHPINEYY
360 370 380 390 400
IADASEDQVF VCVSHSNNRT 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 TWGDHGGIIT
560 570 580 590 600
AIAQGMETNE LKYSTNEGET WKTFIFSEKP VFVYGLLTEP GEKSTVFTIF
610 620 630 640 650
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV
660 670 680 690 700
FKRRTPHATC FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV
710 720 730 740 750
PDPEFSGKSY SPPVPCPVGS TYRRTRGYRK ISGDTCSGGD VEARLEGELV
760 770 780 790 800
PCPLAEENEF ILYAVRKSIY RYDLASGATE QLPLTGLRAA VALDFDYEHN
810 820 830 840 850
CLYWSDLALD VIQRLCLNGS TGQEVIINSG LETVEALAFE PLSQLLYWVD
860 870 880 890 900
AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP
910 920 930 940 950
GIYRSNMDGS AAYHLVSEDV KWPNGISVDD QWIYWTDAYL ECIERITFSG
960 970 980 990 1000
QQRSVILDNL PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSQMEILANQ
1010 1020 1030 1040 1050
LTGLMDMKIF YKGKNTGSNA CVPRPCSLLC LPKANNSRSC RCPEDVSSSV
1060 1070 1080 1090 1100
LPSGDLMCDC PQGYQLKNNT CVKQENTCLR NQYRCSNGNC INSIWWCDFD
1110 1120 1130 1140 1150
NDCGDMSDER NCPTTICDLD TQFRCQESGT CIPLSYKCDL EDDCGDNSDE
1160 1170 1180 1190 1200
SHCEMHQCRS DEYNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE
1210 1220 1230 1240 1250
ASNFQCRNGH CIPQRWACDG DTDCQDGSDE DPVNCEKKCN GFRCPNGTCI
1260 1270 1280 1290 1300
PSSKHCDGLR DCSDGSDEQH CEPLCTHFMD FVCKNRQQCL FHSMVCDGII
1310 1320 1330 1340 1350
QCRDGSDEDA AFAGCSQDPE FHKVCDEFGF QCQNGVCISL IWKCDGMDDC
1360 1370 1380 1390 1400
GDYSDEANCE NPTEAPNCSR YFQFRCENGH CIPNRWKCDR ENDCGDWSDE
1410 1420 1430 1440 1450
KDCGDSHILP FSTPGPSTCL PNYYRCSSGT CVMDTWVCDG YRDCADGSDE
1460 1470 1480 1490 1500
EACPLLANVT AASTPTQLGR CDRFEFECHQ PKTCIPNWKR CDGHQDCQDG
1510 1520 1530 1540 1550
RDEANCPTHS TLTCMSREFQ CEDGEACIVL SERCDGFLDC SDESDEKACS
1560 1570 1580 1590 1600
DELTVYKVQN LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW
1610 1620 1630 1640 1650
KTLETHSNKT NTVLKVLKPD TTYQVKVQVQ CLSKAHNTND FVTLRTPEGL
1660 1670 1680 1690 1700
PDAPRNLQLS LPREAEGVIV GHWAPPIHTH GLIREYIVEY SRSGSKMWAS
1710 1720 1730 1740 1750
QRAASNFTEI KNLLVNTLYT VRVAAVTSRG IGNWSDSKSI TTIKGKVIPP
1760 1770 1780 1790 1800
PDIHIDSYGE NYLSFTLTME SDIKVNGYVV NLFWAFDTHK QERRTLNFRG
1810 1820 1830 1840 1850
SILSHKVGNL TAHTSYEISA WAKTDLGDSP LAFEHVMTRG VRPPAPSLKA
1860 1870 1880 1890 1900
KAINQTAVEC TWTGPRNVVY GIFYATSFLD LYRNPKSLTT SLHNKTVIVS
1910 1920 1930 1940 1950
KDEQYLFLVR VVVPYQGPSS DYVVVKMIPD SRLPPRHLHV VHTGKTSVVI
1960 1970 1980 1990 2000
KWESPYDSPD QDLLYAVAVK DLIRKTDRSY KVKSRNSTVE YTLNKLEPGG
2010 2020 2030 2040 2050
KYHIIVQLGN MSKDSSIKIT TVSLSAPDAL KIITENDHVL LFWKSLALKE
2060 2070 2080 2090 2100
KHFNESRGYE IHMFDSAMNI TAYLGNTTDN FFKISNLKMG HNYTFTVQAR
2110 2120 2130 2140 2150
CLFGNQICGE PAILLYDELG SGADASATQA ARSTDVAAVV VPILFLILLS
2160 2170 2180 2190 2200
LGVGFAILYT KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP
2210
MITGFSDDVP MVIA
Length:2,214
Mass (Da):248,426
Last modified:May 18, 2010 - v2
Checksum:i4C215BB33E65C0B2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036371120L → S in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_070012141Y → C in AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_070013511G → R in AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_020360528A → T.1 PublicationCorresponds to variant rs2298813dbSNPEnsembl.1
Natural variantiVAR_070014924N → S in AD; unknown pathological significance. 1 PublicationCorresponds to variant rs377498269dbSNPEnsembl.1
Natural variantiVAR_0345081074Q → E.4 PublicationsCorresponds to variant rs1699107dbSNPEnsembl.1
Natural variantiVAR_0700151358N → S in AD; unknown pathological significance. 1 PublicationCorresponds to variant rs747306346dbSNPEnsembl.1
Natural variantiVAR_0363721581M → L in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0700161681G → D in AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_0345091967V → I.4 PublicationsCorresponds to variant rs1792120dbSNPEnsembl.1
Natural variantiVAR_0363731972L → V in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs766895956dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08110 mRNA. Translation: CAA69325.1.
U60975 mRNA. Translation: AAC50891.2.
AP000664 Genomic DNA. No translation available.
AP000977 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67525.1.
BC137171 mRNA. Translation: AAI37172.1.
CCDSiCCDS8436.1.
RefSeqiNP_003096.1. NM_003105.5.
UniGeneiHs.368592.

Genome annotation databases

EnsembliENST00000260197; ENSP00000260197; ENSG00000137642.
GeneIDi6653.
KEGGihsa:6653.
UCSCiuc001pxx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08110 mRNA. Translation: CAA69325.1.
U60975 mRNA. Translation: AAC50891.2.
AP000664 Genomic DNA. No translation available.
AP000977 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67525.1.
BC137171 mRNA. Translation: AAI37172.1.
CCDSiCCDS8436.1.
RefSeqiNP_003096.1. NM_003105.5.
UniGeneiHs.368592.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DM4NMR-A1651-1745[»]
3G2SX-ray1.70C/D2202-2214[»]
3G2TX-ray2.00C/D2202-2214[»]
3WSXX-ray2.35A29-753[»]
3WSYX-ray3.11A86-753[»]
C42-56[»]
3WSZX-ray3.20A86-753[»]
ProteinModelPortaliQ92673.
SMRiQ92673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112536. 49 interactors.
DIPiDIP-41229N.
IntActiQ92673. 12 interactors.
MINTiMINT-231252.
STRINGi9606.ENSP00000260197.

PTM databases

iPTMnetiQ92673.
PhosphoSitePlusiQ92673.

Polymorphism and mutation databases

BioMutaiSORL1.
DMDMi296452912.

Proteomic databases

EPDiQ92673.
MaxQBiQ92673.
PaxDbiQ92673.
PeptideAtlasiQ92673.
PRIDEiQ92673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260197; ENSP00000260197; ENSG00000137642.
GeneIDi6653.
KEGGihsa:6653.
UCSCiuc001pxx.4. human.

Organism-specific databases

CTDi6653.
DisGeNETi6653.
GeneCardsiSORL1.
HGNCiHGNC:11185. SORL1.
HPAiCAB011500.
HPA031321.
MalaCardsiSORL1.
MIMi104300. phenotype.
602005. gene.
neXtProtiNX_Q92673.
OpenTargetsiENSG00000137642.
Orphaneti1020. Early-onset autosomal dominant Alzheimer disease.
PharmGKBiPA36022.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
KOG3511. Eukaryota.
ENOG410Y3W5. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000007009.
HOVERGENiHBG017830.
InParanoidiQ92673.
OMAiESDEKAC.
OrthoDBiEOG091G00GS.
PhylomeDBiQ92673.
TreeFamiTF324918.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137642-MONOMER.
ReactomeiR-HSA-977225. Amyloid fiber formation.
SIGNORiQ92673.

Miscellaneous databases

ChiTaRSiSORL1. human.
EvolutionaryTraceiQ92673.
GenomeRNAii6653.
PROiQ92673.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137642.
CleanExiHS_SORL1.
ExpressionAtlasiQ92673. baseline and differential.
GenevisibleiQ92673. HS.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 5 hits.
4.10.400.10. 10 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR031777. Sortilin_C.
IPR031778. Sortilin_N.
IPR006581. VPS10.
[Graphical view]
PfamiPF00041. 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.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00060. FN3. 6 hits.
SM00192. LDLa. 11 hits.
SM00135. LY. 5 hits.
SM00602. VPS10. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF57424. SSF57424. 11 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50853. FN3. 4 hits.
PS01209. LDLRA_1. 10 hits.
PS50068. LDLRA_2. 11 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSORL_HUMAN
AccessioniPrimary (citable) accession number: Q92673
Secondary accession number(s): B2RNX7, Q92856
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.