Q92673 (SORL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SORL1
Synonyms:	C11orf32

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2214 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with GGA1 and ROCK2. Ref.8 Ref.10
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	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. According to Ref.1, found in spinal cord, testis, liver, kidney and pancreas with detectable levels in placenta, lung and heart. According to Ref.2, expressed in the prostate, ovary, thyroid and spleen, but not found in kidney, liver, lung, skeletal muscle, bone marrow and adrenals.
Post-translational modification	The propeptide removed in the N-terminus may be cleaved by furin or homologous proteases.
Miscellaneous	Genetic variations in SORL1 may be associated with increased risk for late onset Alzheimer disease in some populations.
Sequence similarities	Belongs to the VPS10-related sortilin family. SORL1 subfamily. Contains 5 BNR repeats. Contains 1 EGF-like domain. Contains 6 fibronectin type-III domains. Contains 11 LDL-receptor class A domains. Contains 5 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Cholesterol metabolism Endocytosis Lipid metabolism Lipid transport Steroid metabolism Transport
Cellular component	LDL Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid transport Inferred from electronic annotation. Source: UniProtKB-KW receptor-mediated endocytosis Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	low-density lipoprotein particle binding Inferred from physical interaction. Source: BHF-UCL transmembrane signaling receptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Propeptide

29 – 81

53

Removed in mature form

PRO_0000033164

Chain

82 – 2214

2133

Sortilin-related receptor

PRO_0000033165

Regions

Topological domain

82 – 2137

2056

Extracellular Potential

Transmembrane

2138 – 2158

21

Helical; Potential

Topological domain

2159 – 2214

56

Cytoplasmic Potential

Repeat

136 – 147

12

BNR 1

Repeat

232 – 243

12

BNR 2

Repeat

441 – 452

12

BNR 3

Repeat

521 – 532

12

BNR 4

Repeat

562 – 573

12

BNR 5

Repeat

800 – 843

44

LDL-receptor class B 1

Repeat

844 – 887

44

LDL-receptor class B 2

Repeat

888 – 932

45

LDL-receptor class B 3

Repeat

933 – 970

38

LDL-receptor class B 4

Repeat

971 – 1013

43

LDL-receptor class B 5

Domain

1026 – 1072

47

EGF-like

Domain

1076 – 1114

39

LDL-receptor class A 1

Domain

1115 – 1155

41

LDL-receptor class A 2

Domain

1156 – 1194

39

LDL-receptor class A 3

Domain

1198 – 1236

39

LDL-receptor class A 4

Domain

1238 – 1272

35

LDL-receptor class A 5

Domain

1273 – 1317

45

LDL-receptor class A 6

Domain

1323 – 1361

39

LDL-receptor class A 7

Domain

1366 – 1405

40

LDL-receptor class A 8

Domain

1417 – 1455

39

LDL-receptor class A 9

Domain

1469 – 1508

40

LDL-receptor class A 10

Domain

1512 – 1551

40

LDL-receptor class A 11

Domain

1554 – 1646

93

Fibronectin type-III 1

Domain

1651 – 1742

92

Fibronectin type-III 2

Domain

1749 – 1838

90

Fibronectin type-III 3

Domain

1843 – 1927

85

Fibronectin type-III 4

Domain

1934 – 2023

90

Fibronectin type-III 5

Domain

2024 – 2118

95

Fibronectin type-III 6

Motif

63 – 65

3

Cell attachment site Potential

Motif

2172 – 2177

6

Endocytosis signal Potential

Amino acid modifications

Modified residue

2206

1

Phosphoserine; by ROCK2 Ref.8

Glycosylation

99

1

N-linked (GlcNAc...) Ref.7

Glycosylation

158

1

N-linked (GlcNAc...) Potential

Glycosylation

368

1

N-linked (GlcNAc...) Potential

Glycosylation

430

1

N-linked (GlcNAc...) Potential

Glycosylation

616

1

N-linked (GlcNAc...) Potential

Glycosylation

674

1

N-linked (GlcNAc...) Potential

Glycosylation

818

1

N-linked (GlcNAc...) Potential

Glycosylation

871

1

N-linked (GlcNAc...) Potential

Glycosylation

1035

1

N-linked (GlcNAc...) Potential

Glycosylation

1068

1

N-linked (GlcNAc...) Potential

Glycosylation

1164

1

N-linked (GlcNAc...) Potential

Glycosylation

1191

1

N-linked (GlcNAc...) Potential

Glycosylation

1246

1

N-linked (GlcNAc...) Potential

Glycosylation

1367

1

N-linked (GlcNAc...) Potential

Glycosylation

1458

1

N-linked (GlcNAc...) Potential

Glycosylation

1608

1

N-linked (GlcNAc...) Potential

Glycosylation

1706

1

N-linked (GlcNAc...) Potential

Glycosylation

1733

1

N-linked (GlcNAc...) Ref.7

Glycosylation

1809

1

N-linked (GlcNAc...) Potential

Glycosylation

1854

1

N-linked (GlcNAc...) Potential

Glycosylation

1894

1

N-linked (GlcNAc...) Potential

Glycosylation

1986

1

N-linked (GlcNAc...) Potential

Glycosylation

2010

1

N-linked (GlcNAc...) Ref.7

Glycosylation

2054

1

N-linked (GlcNAc...) Potential

Glycosylation

2069

1

N-linked (GlcNAc...) Potential

Glycosylation

2076

1

N-linked (GlcNAc...) Ref.7

Glycosylation

2092

1

N-linked (GlcNAc...) Ref.7

Disulfide bond

1078 ↔ 1090

By similarity

Disulfide bond

1085 ↔ 1103

By similarity

Disulfide bond

1097 ↔ 1112

By similarity

Disulfide bond

1117 ↔ 1131

By similarity

Disulfide bond

1125 ↔ 1144

By similarity

Disulfide bond

1138 ↔ 1153

By similarity

Disulfide bond

1158 ↔ 1170

By similarity

Disulfide bond

1165 ↔ 1183

By similarity

Disulfide bond

1177 ↔ 1192

By similarity

Disulfide bond

1199 ↔ 1211

By similarity

Disulfide bond

1206 ↔ 1224

By similarity

Disulfide bond

1218 ↔ 1235

By similarity

Disulfide bond

1239 ↔ 1249

By similarity

Disulfide bond

1244 ↔ 1262

By similarity

Disulfide bond

1256 ↔ 1271

By similarity

Disulfide bond

1275 ↔ 1289

By similarity

Disulfide bond

1283 ↔ 1302

By similarity

Disulfide bond

1296 ↔ 1315

By similarity

Disulfide bond

1325 ↔ 1337

By similarity

Disulfide bond

1332 ↔ 1350

By similarity

Disulfide bond

1344 ↔ 1359

By similarity

Disulfide bond

1368 ↔ 1381

By similarity

Disulfide bond

1376 ↔ 1394

By similarity

Disulfide bond

1388 ↔ 1403

By similarity

Disulfide bond

1419 ↔ 1431

By similarity

Disulfide bond

1426 ↔ 1444

By similarity

Disulfide bond

1438 ↔ 1453

By similarity

Disulfide bond

1471 ↔ 1484

By similarity

Disulfide bond

1478 ↔ 1497

By similarity

Disulfide bond

1491 ↔ 1506

By similarity

Disulfide bond

1514 ↔ 1527

By similarity

Disulfide bond

1521 ↔ 1540

By similarity

Disulfide bond

1534 ↔ 1549

By similarity

Natural variations

Natural variant

120

1

L → S in a breast cancer sample; somatic mutation. Ref.11

VAR_036371

Natural variant

528

1

A → T. Ref.12
Corresponds to variant rs2298813 [ dbSNP | Ensembl ].

VAR_020360

Natural variant

1074

1

Q → E. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs1699107 [ dbSNP | Ensembl ].

VAR_034508

Natural variant

1581

1

M → L in a breast cancer sample; somatic mutation. Ref.11

VAR_036372

Natural variant

1967

1

V → I. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs1792120 [ dbSNP | Ensembl ].

VAR_034509

Natural variant

1972

1

L → V in a colorectal cancer sample; somatic mutation. Ref.11

VAR_036373

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2214

Helix Strand Turn

Details...

Beta strand

1655 – 1660

6

Beta strand

1669 – 1674

6

Beta strand

1683 – 1692

10

Beta strand

1699 – 1710

12

Beta strand

1718 – 1729

12

Beta strand

1731 – 1734

4

Beta strand

1738 – 1741

4

Sequences

	Sequence		Length	Mass (Da)
	Q92673 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 4C215BB33E65C0B2	FASTA	2,214	248,426
	10 20 30 40 50 60 MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQRLHGGSA PLPQDRGFLV VQGDPRELRL 70 80 90 100 110 120 WARGDARGAS RADEKPLRRK RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL 130 140 150 160 170 180 ARDSLALARP KSSDVYVSYD YGKSFKKISD KLNFGLGNRS EAVIAQFYHS PADNKRYIFA 190 200 210 220 230 240 DAYAQYLWIT FDFCNTLQGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT 250 260 270 280 290 300 WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF 310 320 330 340 350 360 QLRDKYMFAT KVVHLLGSEQ QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF 370 380 390 400 410 420 VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL 430 440 450 460 470 480 QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR 490 500 510 520 530 540 LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY 550 560 570 580 590 600 TWGDHGGIIT AIAQGMETNE LKYSTNEGET WKTFIFSEKP VFVYGLLTEP GEKSTVFTIF 610 620 630 640 650 660 GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC 670 680 690 700 710 720 FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKSY SPPVPCPVGS 730 740 750 760 770 780 TYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAVRKSIY RYDLASGATE 790 800 810 820 830 840 QLPLTGLRAA VALDFDYEHN CLYWSDLALD VIQRLCLNGS TGQEVIINSG LETVEALAFE 850 860 870 880 890 900 PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 910 920 930 940 950 960 GIYRSNMDGS AAYHLVSEDV KWPNGISVDD QWIYWTDAYL ECIERITFSG QQRSVILDNL 970 980 990 1000 1010 1020 PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSQMEILANQ LTGLMDMKIF YKGKNTGSNA 1030 1040 1050 1060 1070 1080 CVPRPCSLLC LPKANNSRSC RCPEDVSSSV LPSGDLMCDC PQGYQLKNNT CVKQENTCLR 1090 1100 1110 1120 1130 1140 NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTICDLD TQFRCQESGT CIPLSYKCDL 1150 1160 1170 1180 1190 1200 EDDCGDNSDE SHCEMHQCRS DEYNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 1210 1220 1230 1240 1250 1260 ASNFQCRNGH CIPQRWACDG DTDCQDGSDE DPVNCEKKCN GFRCPNGTCI PSSKHCDGLR 1270 1280 1290 1300 1310 1320 DCSDGSDEQH CEPLCTHFMD FVCKNRQQCL FHSMVCDGII QCRDGSDEDA AFAGCSQDPE 1330 1340 1350 1360 1370 1380 FHKVCDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFRCENGH 1390 1400 1410 1420 1430 1440 CIPNRWKCDR ENDCGDWSDE KDCGDSHILP FSTPGPSTCL PNYYRCSSGT CVMDTWVCDG 1450 1460 1470 1480 1490 1500 YRDCADGSDE EACPLLANVT AASTPTQLGR CDRFEFECHQ PKTCIPNWKR CDGHQDCQDG 1510 1520 1530 1540 1550 1560 RDEANCPTHS TLTCMSREFQ CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN 1570 1580 1590 1600 1610 1620 LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT NTVLKVLKPD 1630 1640 1650 1660 1670 1680 TTYQVKVQVQ CLSKAHNTND FVTLRTPEGL PDAPRNLQLS LPREAEGVIV GHWAPPIHTH 1690 1700 1710 1720 1730 1740 GLIREYIVEY SRSGSKMWAS QRAASNFTEI KNLLVNTLYT VRVAAVTSRG IGNWSDSKSI 1750 1760 1770 1780 1790 1800 TTIKGKVIPP PDIHIDSYGE NYLSFTLTME SDIKVNGYVV NLFWAFDTHK QERRTLNFRG 1810 1820 1830 1840 1850 1860 SILSHKVGNL TAHTSYEISA WAKTDLGDSP LAFEHVMTRG VRPPAPSLKA KAINQTAVEC 1870 1880 1890 1900 1910 1920 TWTGPRNVVY GIFYATSFLD LYRNPKSLTT SLHNKTVIVS KDEQYLFLVR VVVPYQGPSS 1930 1940 1950 1960 1970 1980 DYVVVKMIPD SRLPPRHLHV VHTGKTSVVI KWESPYDSPD QDLLYAVAVK DLIRKTDRSY 1990 2000 2010 2020 2030 2040 KVKSRNSTVE YTLNKLEPGG KYHIIVQLGN MSKDSSIKIT TVSLSAPDAL KIITENDHVL 2050 2060 2070 2080 2090 2100 LFWKSLALKE KHFNESRGYE IHMFDSAMNI TAYLGNTTDN FFKISNLKMG HNYTFTVQAR 2110 2120 2130 2140 2150 2160 CLFGNQICGE PAILLYDELG SGADASATQA ARSTDVAAVV VPILFLILLS LGVGFAILYT 2170 2180 2190 2200 2210 KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP MITGFSDDVP MVIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel mosaic protein containing LDL receptor elements is highly conserved in humans and chickens." Morwald S., Yamazaki H., Bujo H., Kusunoki J., Kanaki T., Seimiya K., Morisaki N., Nimpf J., Schneider W.J., Saito Y. Arterioscler. Thromb. Vasc. Biol. 17:996-1002(1997) [PubMed: 9157966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLU-1074 AND ILE-1967. Tissue: Brain.
[2]	"Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein." Jacobsen L., Madsen P., Moestrup S.K., Lund A.H., Tommerup N., Nykjaer A., Sottrup-Jensen L., Gliemann J., Petersen C.M. J. Biol. Chem. 271:31379-31383(1996) [PubMed: 8940146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, VARIANTS GLU-1074 AND ILE-1967. Tissue: Brain and T-cell.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-1074 AND ILE-1967.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-1074 AND ILE-1967. Tissue: Brain.
[6]	"No association of SORL1 SNPs with Alzheimer's disease." Minster R.L., DeKosky S.T., Kamboh M.I. Neurosci. Lett. 440:190-192(2008) [PubMed: 18562096] [Abstract] Cited for: LACK OF ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASE.
[7]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-1733; ASN-2010; ASN-2076 AND ASN-2092, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production." Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J., Levey A.I., Lah J.J. J. Biol. Chem. 286:6117-6127(2011) [PubMed: 21147781] [Abstract] Cited for: PHOSPHORYLATION AT SER-2206, INTERACTION WITH ROCK2.
[9]	"Solution structure of the second FN3 domain of human SORLA/LR11." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1651-1745.
[10]	"GGA autoinhibition revisited." Cramer J.F., Gustafsen C., Behrens M.A., Oliveira C.L., Pedersen J.S., Madsen P., Petersen C.M., Thirup S.S. Traffic 11:259-273(2010) [PubMed: 20015111] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2202-2214 IN COMPLEX WITH GGA1, INTERACTION WITH GGA1.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-120; LEU-1581 AND VAL-1972.
[12]	"SORL1 is genetically associated with increased risk for late-onset Alzheimer disease in the Belgian population." Bettens K., Brouwers N., Engelborghs S., De Deyn P.P., Van Broeckhoven C., Sleegers K. Hum. Mutat. 29:769-770(2008) [PubMed: 18407551] [Abstract] Cited for: POSSIBLE ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASE, VARIANT THR-528.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00022608.

RefSeq

NP_003096.1. NM_003105.5.

UniGene

Hs.368592.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DM4	NMR	-	A	1651-1745	[»]
3G2S	X-ray	1.70	C/D	2202-2214	[»]
3G2T	X-ray	2.00	C/D	2202-2214	[»]

ProteinModelPortal

Q92673.

SMR

Q92673. Positions 85-757, 759-1049, 1075-1553, 1555-1745, 1800-1832, 1917-2017, 2024-2115.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92673. 3 interactions.

MINT

MINT-231252.

STRING

Q92673.

PTM databases

PhosphoSite

Q92673.

Polymorphism databases

DMDM

296452912.

Proteomic databases

PRIDE

Q92673.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260197; ENSP00000260197; ENSG00000137642.

GeneID

6653.

KEGG

hsa:6653.

UCSC

uc001pxx.2. human.

Organism-specific databases

CTD

6653.

GeneCards

GC11P121356.

H-InvDB

HIX0010207.

HGNC

HGNC:11185. SORL1.

HPA

CAB011500.

MIM

602005. gene.

neXtProt

NX_Q92673.

PharmGKB

PA36022.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12092.

GeneTree

ENSGT00580000081234.

HOGENOM

HBG357060.

HOVERGEN

HBG017830.

InParanoid

Q92673.

OMA

IFGSNKE.

OrthoDB

EOG46DM1T.

PhylomeDB

Q92673.

Gene expression databases

ArrayExpress

Q92673.

Bgee

Q92673.

CleanEx

HS_SORL1.

Genevestigator

Q92673.

GermOnline

ENSG00000137642. Homo sapiens.

Family and domain databases

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR006210. EGF-like.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR006581. VPS10.
[Graphical view]

Gene3D

G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 5 hits.
G3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 11 hits.

Pfam

PF00041. fn3. 3 hits.
PF00057. Ldl_recept_a. 10 hits.
PF00058. Ldl_recept_b. 2 hits.
[Graphical view]

SMART

SM00181. EGF. 1 hit.
SM00060. FN3. 6 hits.
SM00192. LDLa. 11 hits.
SM00135. LY. 5 hits.
SM00602. VPS10. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 5 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 11 hits.

PROSITE

PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
PS50853. FN3. 6 hits.
PS01209. LDLRA_1. 10 hits.
PS50068. LDLRA_2. 11 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

ProtoNet

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Other

NextBio

25935.

SOURCE

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Entry information

Entry name

SORL_HUMAN

Accession

Primary (citable) accession number: Q92673
Secondary accession number(s): B2RNX7, Q92856

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.