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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini82 – 21362055ExtracellularSequence analysisAdd
BLAST
Transmembranei2137 – 215721HelicalSequence analysisAdd
BLAST
Topological domaini2158 – 221356CytoplasmicSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 8153Removed in mature formBy similarityPRO_0000033168Add
BLAST
Chaini82 – 22132132Sortilin-related receptorPRO_0000033169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Modified residuei114 – 1141PhosphoserineBy similarity
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis
Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence analysis
Glycosylationi674 – 6741N-linked (GlcNAc...)Sequence analysis
Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence analysis
Glycosylationi870 – 8701N-linked (GlcNAc...)Sequence analysis
Glycosylationi1034 – 10341N-linked (GlcNAc...)Sequence analysis
Glycosylationi1067 – 10671N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1163 – 11631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1164 ↔ 1182PROSITE-ProRule annotation
Disulfide bondi1176 ↔ 1191PROSITE-ProRule annotation
Glycosylationi1190 – 11901N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1245 – 12451N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1366 – 13661N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1457 – 14571N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1569 – 15691N-linked (GlcNAc...)Sequence analysis
Glycosylationi1607 – 16071N-linked (GlcNAc...)Sequence analysis
Glycosylationi1705 – 17051N-linked (GlcNAc...)Sequence analysis
Glycosylationi1732 – 17321N-linked (GlcNAc...)Sequence analysis
Glycosylationi1808 – 18081N-linked (GlcNAc...)Sequence analysis
Glycosylationi1853 – 18531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1893 – 18931N-linked (GlcNAc...)Sequence analysis
Glycosylationi1985 – 19851N-linked (GlcNAc...)Sequence analysis
Glycosylationi2009 – 20091N-linked (GlcNAc...)Sequence analysis
Glycosylationi2053 – 20531N-linked (GlcNAc...)Sequence analysis
Glycosylationi2068 – 20681N-linked (GlcNAc...)Sequence analysis
Glycosylationi2075 – 20751N-linked (GlcNAc...)Sequence analysis
Glycosylationi2091 – 20911N-linked (GlcNAc...)Sequence analysis
Modified residuei2205 – 22051Phosphoserine; by ROCK2By similarity

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.
SMRiQ95209. Positions 1155-1192, 1650-1744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati136 – 14712BNR 1Add
BLAST
Repeati232 – 24312BNR 2Add
BLAST
Repeati441 – 45212BNR 3Add
BLAST
Repeati521 – 53212BNR 4Add
BLAST
Repeati562 – 57312BNR 5Add
BLAST
Repeati799 – 84244LDL-receptor class B 1Add
BLAST
Repeati843 – 88644LDL-receptor class B 2Add
BLAST
Repeati887 – 92943LDL-receptor class B 3Add
BLAST
Repeati930 – 97142LDL-receptor class B 4Add
BLAST
Repeati972 – 101241LDL-receptor class B 5Add
BLAST
Domaini1025 – 107147EGF-likeAdd
BLAST
Domaini1075 – 111339LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini1114 – 115441LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1155 – 119339LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini1196 – 123540LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini1237 – 127135LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini1272 – 131645LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1322 – 136039LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1365 – 140440LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1416 – 145439LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1468 – 150740LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1511 – 155040LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini1556 – 164893Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini1652 – 174493Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1748 – 184396Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1842 – 192685Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1933 – 202896Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini2029 – 211789Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi63 – 653Cell attachment siteSequence analysis
Motifi2171 – 21766Endocytosis signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi78 – 814Poly-Arg

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

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.
SMRiQ95209. Positions 1155-1192, 1650-1744.
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

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...

Publicationsi

  1. "Elements of neural adhesion molecules and a yeast vacuolar protein sorting receptor are present in a novel mammalian low density lipoprotein receptor family member."
    Yamazaki H., Bujo H., Kusunoki J., Seimiya K., Kanaki T., Morisaki N., Schneider W.J., Saito Y.
    J. Biol. Chem. 271:24761-24768(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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, SUBCELLULAR LOCATION.

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: May 11, 2016
This is version 115 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.