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Protein

Sortilin-related receptor

Gene

SORL1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity). Involved in APP trafficking to and from the Golgi apparatus (By similarity). It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta (By similarity). Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

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

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini82 – 2136ExtracellularSequence analysisAdd BLAST2055
Transmembranei2137 – 2157HelicalSequence analysisAdd BLAST21
Topological domaini2158 – 2213CytoplasmicSequence analysisAdd BLAST56

GO - Cellular componenti

  • endosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • low-density lipoprotein particle Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, LDL, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000003316829 – 81Removed in mature formBy similarityAdd BLAST53
ChainiPRO_000003316982 – 2213Sortilin-related receptorAdd BLAST2132

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi99N-linked (GlcNAc...)Sequence analysis1
Modified residuei114PhosphoserineBy similarity1
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
Glycosylationi817N-linked (GlcNAc...)Sequence analysis1
Glycosylationi870N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1034N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1067N-linked (GlcNAc...)Sequence analysis1
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...)Sequence analysis1
Disulfide bondi1164 ↔ 1182PROSITE-ProRule annotation
Disulfide bondi1176 ↔ 1191PROSITE-ProRule annotation
Glycosylationi1190N-linked (GlcNAc...)Sequence 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...)Sequence 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...)Sequence 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...)Sequence 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...)Sequence analysis1
Glycosylationi1607N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1705N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1732N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1808N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1853N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1893N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1985N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2009N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2053N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2068N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2075N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2091N-linked (GlcNAc...)Sequence analysis1
Modified residuei2205Phosphoserine; by ROCK2By similarity1

Post-translational modificationi

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

Keywords - PTMi

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

Expressioni

Tissue specificityi

Expressed abundantly in brain, in particular the hippocampus, dentate gyrus, and cerebral cortex, and is present at significant levels in liver, adrenal glands and testis.

Interactioni

Subunit structurei

Interacts with GGA1 and ROCK2. Interacts with APP. Interacts with PLAUR.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009783.

Structurei

3D structure databases

ProteinModelPortaliQ95209.
ModBaseiSearch...
MobiDBiSearch...

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
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
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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi63 – 65Cell attachment siteSequence analysis3
Motifi2171 – 2176Endocytosis signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi78 – 81Poly-Arg4

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.
HOGENOMiHOG000007009.
HOVERGENiHBG017830.
InParanoidiQ95209.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
2.60.40.10. 5 hits.
4.10.400.10. 11 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.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF00041. 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.
[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.

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
Checksum:iA54232645A5A0DDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86350 mRNA. Translation: BAA13075.1.
RefSeqiNP_001076133.1. NM_001082664.1.
UniGeneiOcu.2148.

Genome annotation databases

GeneIDi100009378.
KEGGiocu:100009378.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86350 mRNA. Translation: BAA13075.1.
RefSeqiNP_001076133.1. NM_001082664.1.
UniGeneiOcu.2148.

3D structure databases

ProteinModelPortaliQ95209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009378.
KEGGiocu:100009378.

Organism-specific databases

CTDi6653.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
KOG3511. Eukaryota.
ENOG410Y3W5. LUCA.
HOGENOMiHOG000007009.
HOVERGENiHBG017830.
InParanoidiQ95209.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
2.60.40.10. 5 hits.
4.10.400.10. 11 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.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF00041. 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.
[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_RABIT
AccessioniPrimary (citable) accession number: Q95209
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.