Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O88307 (SORL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sortilin-related receptor
Alternative name(s):
Gp250
Low-density lipoprotein receptor relative with 11 ligand-binding repeats
Short name=LDLR relative with 11 ligand-binding repeats
Short name=LR11
SorLA-1
Sorting protein-related receptor containing LDLR class A repeats
Short name=mSorLA
Gene names
Name:Sorl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. May play a role in neural organization, as well as the establishment of embryonic organ systems. 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. Ref.5

Subunit structure

Interacts with GGA1 and ROCK2 By similarity. Interacts with APP. Interacts with PLAUR By similarity. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Golgi apparatus By similarity. Endosome By similarity. Secreted By similarity.

Tissue specificity

Abundant in brain, where it is mainly expressed in adult cerebellum, hippocampal ca regions, dentate gyrus, and to a much lesser extent in the cerebral cortex. Detectable in kidney, skeletal muscle, lung and spleen, but not in the liver.

Developmental stage

Expressed as early as embryonic day 6.5 (E6.5) and peaks at E11, the main location is in the CNS during development. At early stages, it is abundant in a subpopulation of neurons in the cerebral cortex, in the hippocampus, and granular and Purkinje cell layers in the cerebellum, whereas in the adult, expression in cerebellar granular cells and in the cerebral cortex is low. Expression occurs also in a variety of glands and organs during organogenesis.

Post-translational modification

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

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 processCholesterol metabolism
Endocytosis
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentEndosome
Golgi apparatus
LDL
Membrane
Secreted
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 18362153. Source: Alzheimers_University_of_Toronto

negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process

Inferred from mutant phenotype PubMed 18362153. Source: Alzheimers_University_of_Toronto

negative regulation of beta-amyloid formation

Inferred from mutant phenotype PubMed 18362153PubMed 19036982. Source: Alzheimers_University_of_Toronto

negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process

Inferred from mutant phenotype PubMed 18362153. Source: Alzheimers_University_of_Toronto

negative regulation of neurofibrillary tangle assembly

Inferred from mutant phenotype PubMed 22986780. Source: Alzheimers_University_of_Toronto

negative regulation of neurogenesis

Inferred from mutant phenotype PubMed 18362153. Source: Alzheimers_University_of_Toronto

negative regulation of neuron death

Inferred from mutant phenotype PubMed 22986780. Source: Alzheimers_University_of_Toronto

negative regulation of protein binding

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

negative regulation of protein oligomerization

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

negative regulation of tau-protein kinase activity

Inferred from mutant phenotype PubMed 22986780. Source: Alzheimers_University_of_Toronto

positive regulation of ER to Golgi vesicle-mediated transport

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of choline O-acetyltransferase activity

Inferred from mutant phenotype PubMed 22986780. Source: Alzheimers_University_of_Toronto

positive regulation of early endosome to recycling endosome transport

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of endocytic recycling

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of protein exit from endoplasmic reticulum

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of protein localization to early endosome

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

post-Golgi vesicle-mediated transport

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

protein maturation

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

protein retention in Golgi apparatus

Inferred from mutant phenotype PubMed 18362153. Source: Alzheimers_University_of_Toronto

protein targeting

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

protein targeting to Golgi

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

protein targeting to lysosome

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi cisterna

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

early endosome

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

multivesicular body

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear envelope lumen

Inferred from direct assay PubMed 18362153. Source: Alzheimers_University_of_Toronto

perinuclear region of cytoplasm

Inferred from sequence orthology PubMed 19047013. Source: MGI

recycling endosome

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

trans-Golgi network

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

   Molecular_functionlow-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 19047013. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 8153Removed in mature form By similarity
PRO_0000033166
Chain82 – 22152134Sortilin-related receptor
PRO_0000033167

Regions

Topological domain82 – 21382057Extracellular Potential
Transmembrane2139 – 215921Helical; Potential
Topological domain2160 – 221556Cytoplasmic Potential
Repeat136 – 14712BNR 1
Repeat232 – 24312BNR 2
Repeat441 – 45212BNR 3
Repeat521 – 53212BNR 4
Repeat562 – 57312BNR 5
Repeat800 – 84344LDL-receptor class B 1
Repeat844 – 88744LDL-receptor class B 2
Repeat888 – 93245LDL-receptor class B 3
Repeat933 – 97240LDL-receptor class B 4
Repeat973 – 101341LDL-receptor class B 5
Domain1026 – 107247EGF-like
Domain1076 – 111439LDL-receptor class A 1
Domain1115 – 115541LDL-receptor class A 2
Domain1156 – 119439LDL-receptor class A 3
Domain1198 – 123639LDL-receptor class A 4
Domain1238 – 127235LDL-receptor class A 5
Domain1273 – 131745LDL-receptor class A 6
Domain1323 – 136139LDL-receptor class A 7
Domain1366 – 140540LDL-receptor class A 8
Domain1417 – 145539LDL-receptor class A 9
Domain1469 – 150840LDL-receptor class A 10
Domain1512 – 155140LDL-receptor class A 11
Domain1557 – 164993Fibronectin type-III 1
Domain1653 – 174593Fibronectin type-III 2
Domain1747 – 1846100Fibronectin type-III 3
Domain1844 – 192885Fibronectin type-III 4
Domain1935 – 203096Fibronectin type-III 5
Domain2031 – 211989Fibronectin type-III 6
Motif2173 – 21786Endocytosis signal Potential

Amino acid modifications

Modified residue1141Phosphoserine By similarity
Modified residue22071Phosphoserine; by ROCK2 By similarity
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6741N-linked (GlcNAc...) Potential
Glycosylation8181N-linked (GlcNAc...) Potential
Glycosylation8711N-linked (GlcNAc...) Potential
Glycosylation10351N-linked (GlcNAc...) Potential
Glycosylation10681N-linked (GlcNAc...) Potential
Glycosylation11641N-linked (GlcNAc...) Potential
Glycosylation11911N-linked (GlcNAc...) Potential
Glycosylation12461N-linked (GlcNAc...) Potential
Glycosylation13671N-linked (GlcNAc...) Potential
Glycosylation14581N-linked (GlcNAc...) Potential
Glycosylation16081N-linked (GlcNAc...) Potential
Glycosylation17061N-linked (GlcNAc...) Potential
Glycosylation17331N-linked (GlcNAc...) Potential
Glycosylation18101N-linked (GlcNAc...) Potential
Glycosylation18551N-linked (GlcNAc...) Potential
Glycosylation18951N-linked (GlcNAc...) Potential
Glycosylation19871N-linked (GlcNAc...) Potential
Glycosylation20111N-linked (GlcNAc...) Potential
Glycosylation20551N-linked (GlcNAc...) Potential
Glycosylation20701N-linked (GlcNAc...) Potential
Glycosylation20771N-linked (GlcNAc...) Potential
Glycosylation20931N-linked (GlcNAc...) Potential
Disulfide bond1078 ↔ 1090 By similarity
Disulfide bond1085 ↔ 1103 By similarity
Disulfide bond1097 ↔ 1112 By similarity
Disulfide bond1117 ↔ 1131 By similarity
Disulfide bond1125 ↔ 1144 By similarity
Disulfide bond1138 ↔ 1153 By similarity
Disulfide bond1158 ↔ 1170 By similarity
Disulfide bond1165 ↔ 1183 By similarity
Disulfide bond1177 ↔ 1192 By similarity
Disulfide bond1199 ↔ 1211 By similarity
Disulfide bond1206 ↔ 1224 By similarity
Disulfide bond1218 ↔ 1235 By similarity
Disulfide bond1239 ↔ 1249 By similarity
Disulfide bond1244 ↔ 1262 By similarity
Disulfide bond1256 ↔ 1271 By similarity
Disulfide bond1275 ↔ 1289 By similarity
Disulfide bond1283 ↔ 1302 By similarity
Disulfide bond1296 ↔ 1315 By similarity
Disulfide bond1325 ↔ 1337 By similarity
Disulfide bond1332 ↔ 1350 By similarity
Disulfide bond1344 ↔ 1359 By similarity
Disulfide bond1368 ↔ 1381 By similarity
Disulfide bond1376 ↔ 1394 By similarity
Disulfide bond1388 ↔ 1403 By similarity
Disulfide bond1419 ↔ 1431 By similarity
Disulfide bond1426 ↔ 1444 By similarity
Disulfide bond1438 ↔ 1453 By similarity
Disulfide bond1471 ↔ 1484 By similarity
Disulfide bond1478 ↔ 1497 By similarity
Disulfide bond1491 ↔ 1506 By similarity
Disulfide bond1514 ↔ 1527 By similarity
Disulfide bond1521 ↔ 1540 By similarity
Disulfide bond1534 ↔ 1549 By similarity

Experimental info

Sequence conflict7061S → F in AAC16739. Ref.3
Sequence conflict7681S → F in AAC16739. Ref.3
Sequence conflict7851S → W in BAA31219. Ref.1
Sequence conflict7961D → G in AAC16739. Ref.3
Sequence conflict9531R → G in BAA31219. Ref.1
Sequence conflict1268 – 12692EQ → DE in BAA31219. Ref.1
Sequence conflict14251H → A in BAA31219. Ref.1
Sequence conflict14251H → R in AAC16739. Ref.3
Sequence conflict14251H → R in CAA72732. Ref.4
Sequence conflict14681F → L in BAA31219. Ref.1
Sequence conflict14681F → L in AAC16739. Ref.3
Sequence conflict14681F → L in CAA72732. Ref.4
Sequence conflict16631S → R in BAA31219. Ref.1
Sequence conflict16631S → R in AAC16739. Ref.3
Sequence conflict16631S → R in CAA72732. Ref.4
Sequence conflict1709 – 17135EIKNL → KKKKK in CAA72732. Ref.4
Sequence conflict18071R → K in BAA31219. Ref.1
Sequence conflict18071R → K in AAC16739. Ref.3
Sequence conflict21301Q → H in BAA31219. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O88307 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 5D7F53806EFE2CB0

FASTA2,215247,086
        10         20         30         40         50         60 
MATRSSRRES RLPFLFALVA LLPRGALGGG WTQRLHGGPA PLPQDRGFFV VQGDPRDLRL 

        70         80         90        100        110        120 
GTHGDAPGAS PAARKPLRTR RSAALQPQPI QVYGQVSLND SHNQMVVHWA GEKSNVIVAL 

       130        140        150        160        170        180 
ARDSLALARP KSSDVYVSYD YGKSFSKISE KLNFGVGNNS EAVISQFYHS PADNKRYIFV 

       190        200        210        220        230        240 
DAYAQYLWIT FDFCSTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT 

       250        260        270        280        290        300 
WIMIQEHVKS FSWGIDPYDQ PNAIYIERHE PFGFSTVLRS TDFFQSRENQ EVILEEVRDF 

       310        320        330        340        350        360 
QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY IADAAEDQVF 

       370        380        390        400        410        420 
VCVSHSNNST 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 
TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF 

       610        620        630        640        650        660 
GSNKESVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC 

       670        680        690        700        710        720 
FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKPY SPPVPCPVGS 

       730        740        750        760        770        780 
SYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAMRKSIY RYDLASGATE 

       790        800        810        820        830        840 
QLPLSGLRAA VALDFDYERN CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE 

       850        860        870        880        890        900 
PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 

       910        920        930        940        950        960 
GIYRSYMDGS AAYRLVSEDV KWPNGISVDS QWIYWTDAYL DCIERITFSG QQRSVILDSL 

       970        980        990       1000       1010       1020 
PHPYAIAVFK NEIYWDDWSQ LSIFRASKHS RSQVEILASQ LTGLMDMKVF YKGKNAGSNA 

      1030       1040       1050       1060       1070       1080 
CVPQPCSLLC LPKANNSKSC RCPEGVASSV LPSGDLMCDC PQGYQRKNNT CVKEENTCLR 

      1090       1100       1110       1120       1130       1140 
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL 

      1150       1160       1170       1180       1190       1200 
EDDCGDNSDE SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 

      1210       1220       1230       1240       1250       1260 
ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI PSSKHCDGLR 

      1270       1280       1290       1300       1310       1320 
DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV QCRDGSDEDA AFAGCSQDPE 

      1330       1340       1350       1360       1370       1380 
FHKECDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFHCENGH 

      1390       1400       1410       1420       1430       1440 
CIPNRWKCDR ENDCGDWSDE KDCGDSHVLP SPTPGPSTCL PNYFHCSSGA CVMGTWVCDG 

      1450       1460       1470       1480       1490       1500 
YRDCADGSDE EACPSLANST AASTPTQFGQ CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG 

      1510       1520       1530       1540       1550       1560 
QDEANCPTHS TLTCTSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN 

      1570       1580       1590       1600       1610       1620 
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT STVLKVLKPD 

      1630       1640       1650       1660       1670       1680 
TTYQVKVQVH CLNKVHNTND FVTLRTPEGL PDAPRNLQLS LNSEEEGVIL GHWAPPVHTH 

      1690       1700       1710       1720       1730       1740 
GLIREYIVEY SRSGSKMWAS QRAASNSTEI KNLLLNALYT VRVAAVTSRG IGNWSDSKSI 

      1750       1760       1770       1780       1790       1800 
TTIKGKVIQA PNIHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLSFRG 

      1810       1820       1830       1840       1850       1860 
GSALSHRVSN LTAHTSYEIS AWAKTDLGDS PLAFEHILTR GSSPPAPSLK AKAINQTAVE 

      1870       1880       1890       1900       1910       1920 
CIWTGPKNVV YGIFYATSFL DLYRNPKSVT TSLHNKTVIV SKDEQYLFLV RVLIPYQGPS 

      1930       1940       1950       1960       1970       1980 
SDYVVVKMIP DSRLPPRHLH AVHIGKTSAL IKWESPYDSP DQDLFYAIAV KDLIRKTDRS 

      1990       2000       2010       2020       2030       2040 
YKVRSRNSTV EYSLSKLEPG GKYHIIVQLG NMSKDSSIKI TTVSLSAPDA LKIITENDHV 

      2050       2060       2070       2080       2090       2100 
LLFWKSLALK EKQFNETRGY EIHMSDSAVN LTAYLGNTTD NFFKVSNLKM GHNYTFTVQA 

      2110       2120       2130       2140       2150       2160 
RCLFGSQICG EPAVLLYDEL SSGADAAVIQ AARSTDVAAV VVPILFLILL SLGVGFAILY 

      2170       2180       2190       2200       2210 
TKHRRLQSSF SAFANSHYSS RLGSAIFSSG DDLGEDDEDA PMITGFSDDV PMVIA 

« Hide

References

« Hide 'large scale' references
[1]"Developmental regulation of LR11 expression in murine brain."
Kanaki T., Bujo H., Hirayama S., Tanaka K., Yamazaki H., Seimiya K., Morisaki N., Schneider W.J., Saito Y.
DNA Cell Biol. 17:647-657(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"Unique expression pattern of a novel mosaic receptor in the developing cerebral cortex."
Hermans-Borgmeyer I., Hampe W., Schinke B., Methner A., Nykjaer A., Suesens U., Fenger U., Herbarth B., Schaller H.C.
Mech. Dev. 70:65-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-2215.
Tissue: Brain.
[4]Boehmelt G., Antonio L., Iscove N.N.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1119-1713.
Strain: Swiss Webster.
[5]"LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration."
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.
Circ. Res. 94:752-758(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein."
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X., Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J., Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015790 mRNA. Translation: BAA31219.1.
AK147303 mRNA. Translation: BAE27834.1.
AF031816 mRNA. Translation: AAC16739.1.
Y12004 mRNA. Translation: CAA72732.1.
CCDSCCDS40594.1.
PIRT00348.
RefSeqNP_035566.2. NM_011436.3.
UniGeneMm.121920.

3D structure databases

ProteinModelPortalO88307.
SMRO88307. Positions 1156-1193, 1651-1745.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-42439N.
MINTMINT-1342356.

PTM databases

PhosphoSiteO88307.

Proteomic databases

MaxQBO88307.
PaxDbO88307.
PRIDEO88307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060989; ENSMUSP00000058613; ENSMUSG00000049313.
GeneID20660.
KEGGmmu:20660.
UCSCuc009pap.1. mouse.

Organism-specific databases

CTD6653.
MGIMGI:1202296. Sorl1.

Phylogenomic databases

eggNOGNOG281049.
GeneTreeENSGT00510000046443.
HOGENOMHOG000007009.
HOVERGENHBG017830.
InParanoidQ3UHM3.
OMATNVYISS.
OrthoDBEOG7FV3PK.
TreeFamTF324918.

Gene expression databases

ArrayExpressO88307.
BgeeO88307.
GenevestigatorO88307.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
2.60.40.10. 4 hits.
4.10.400.10. 11 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-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]
PfamPF00041. fn3. 3 hits.
PF00057. Ldl_recept_a. 10 hits.
PF00058. Ldl_recept_b. 2 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00060. FN3. 6 hits.
SM00192. LDLa. 11 hits.
SM00135. LY. 5 hits.
SM00602. VPS10. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 3 hits.
SSF57424. SSF57424. 11 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50853. FN3. 4 hits.
PS01209. LDLRA_1. 10 hits.
PS50068. LDLRA_2. 11 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio299101.
PROO88307.
SOURCESearch...

Entry information

Entry nameSORL_MOUSE
AccessionPrimary (citable) accession number: O88307
Secondary accession number(s): O54711, O70581, Q3UHM3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot