GenomeNet

Database: UniProt
Entry: Q95209
LinkDB: Q95209
Original site: Q95209 
ID   SORL_RABIT              Reviewed;        2213 AA.
AC   Q95209;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAY-2019, entry version 127.
DE   RecName: Full=Sortilin-related receptor;
DE   AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats;
DE            Short=LDLR relative with 11 ligand-binding repeats;
DE            Short=LR11;
DE   AltName: Full=SorLA-1;
DE   AltName: Full=Sorting protein-related receptor containing LDLR class A repeats;
DE            Short=SorLA;
DE   Flags: Precursor;
GN   Name=SORL1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8798746; DOI=10.1074/jbc.271.40.24761;
RA   Yamazaki H., Bujo H., Kusunoki J., Seimiya K., Kanaki T., Morisaki N.,
RA   Schneider W.J., Saito Y.;
RT   "Elements of neural adhesion molecules and a yeast vacuolar protein
RT   sorting receptor are present in a novel mammalian low density
RT   lipoprotein receptor family member.";
RL   J. Biol. Chem. 271:24761-24768(1996).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14764453; DOI=10.1161/01.RES.0000120862.79154.0F;
RA   Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S.,
RA   Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
RT   "LR11, an LDL receptor gene family member, is a novel regulator of
RT   smooth muscle cell migration.";
RL   Circ. Res. 94:752-758(2004).
CC   -!- FUNCTION: Likely to be a multifunctional endocytic receptor, that
CC       may be implicated in the uptake of lipoproteins and of proteases.
CC       Binds LDL, the major cholesterol-carrying lipoprotein of plasma,
CC       and transports it into cells by endocytosis. Binds the receptor-
CC       associated protein (RAP). Could play a role in cell-cell
CC       interaction (By similarity). Involved in APP trafficking to and
CC       from the Golgi apparatus (By similarity). It probably acts as a
CC       sorting receptor that protects APP from trafficking to late
CC       endosome and from processing into amyloid beta (By similarity).
CC       Involved in the regulation of smooth muscle cells migration,
CC       probably through PLAUR binding and decreased internalization.
CC       {ECO:0000250, ECO:0000269|PubMed:14764453}.
CC   -!- SUBUNIT: Interacts with GGA1 and ROCK2. Interacts with APP.
CC       Interacts with PLAUR. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000250}.
CC       Endosome {ECO:0000250}. Secreted {ECO:0000269|PubMed:14764453}.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in brain, in particular
CC       the hippocampus, dentate gyrus, and cerebral cortex, and is
CC       present at significant levels in liver, adrenal glands and testis.
CC   -!- PTM: The propeptide removed in the N-terminus may be cleaved by
CC       furin or homologous proteases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC       subfamily. {ECO:0000305}.
DR   EMBL; D86350; BAA13075.1; -; mRNA.
DR   RefSeq; NP_001076133.1; NM_001082664.1.
DR   SMR; Q95209; -.
DR   STRING; 9986.ENSOCUP00000009783; -.
DR   PRIDE; Q95209; -.
DR   GeneID; 100009378; -.
DR   KEGG; ocu:100009378; -.
DR   CTD; 6653; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; KOG3511; Eukaryota.
DR   eggNOG; ENOG410Y3W5; LUCA.
DR   HOGENOM; HOG000007009; -.
DR   InParanoid; Q95209; -.
DR   OrthoDB; 1046610at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR   GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:UniProtKB.
DR   CDD; cd00063; FN3; 5.
DR   CDD; cd00112; LDLa; 11.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 4.10.400.10; -; 11.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR031777; Sortilin_C.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR006581; VPS10.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00057; Ldl_recept_a; 10.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   Pfam; PF15902; Sortilin-Vps10; 1.
DR   Pfam; PF15901; Sortilin_C; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00192; LDLa; 11.
DR   SMART; SM00135; LY; 5.
DR   SMART; SM00602; VPS10; 1.
DR   SUPFAM; SSF49265; SSF49265; 3.
DR   SUPFAM; SSF57424; SSF57424; 11.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS01209; LDLRA_1; 10.
DR   PROSITE; PS50068; LDLRA_2; 11.
DR   PROSITE; PS51120; LDLRB; 5.
PE   2: Evidence at transcript level;
KW   Cholesterol metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
KW   Endosome; Glycoprotein; Golgi apparatus; LDL; Lipid metabolism;
KW   Lipid transport; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Steroid metabolism;
KW   Sterol metabolism; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   PROPEP       29     81       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000033168.
FT   CHAIN        82   2213       Sortilin-related receptor.
FT                                /FTId=PRO_0000033169.
FT   TOPO_DOM     82   2136       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2137   2157       Helical. {ECO:0000255}.
FT   TOPO_DOM   2158   2213       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      136    147       BNR 1.
FT   REPEAT      232    243       BNR 2.
FT   REPEAT      441    452       BNR 3.
FT   REPEAT      521    532       BNR 4.
FT   REPEAT      562    573       BNR 5.
FT   REPEAT      799    842       LDL-receptor class B 1.
FT   REPEAT      843    886       LDL-receptor class B 2.
FT   REPEAT      887    929       LDL-receptor class B 3.
FT   REPEAT      930    971       LDL-receptor class B 4.
FT   REPEAT      972   1012       LDL-receptor class B 5.
FT   DOMAIN     1025   1071       EGF-like.
FT   DOMAIN     1075   1113       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1114   1154       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1155   1193       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1196   1235       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1237   1271       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1272   1316       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1322   1360       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1365   1404       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1416   1454       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1468   1507       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1511   1550       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1556   1648       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1652   1744       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1748   1843       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1842   1926       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1933   2028       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2029   2117       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   MOTIF        63     65       Cell attachment site. {ECO:0000255}.
FT   MOTIF      2171   2176       Endocytosis signal. {ECO:0000255}.
FT   COMPBIAS     78     81       Poly-Arg.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q92673}.
FT   MOD_RES    2205   2205       Phosphoserine; by ROCK2.
FT                                {ECO:0000250|UniProtKB:Q92673}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    368    368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    616    616       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    674    674       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    817    817       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    870    870       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1034   1034       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1163   1163       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1190   1190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1245   1245       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1366   1366       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1457   1457       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1569   1569       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1607   1607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1705   1705       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1732   1732       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1808   1808       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1853   1853       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1893   1893       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1985   1985       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2009   2009       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2053   2053       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2068   2068       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2075   2075       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2091   2091       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1077   1089       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1084   1102       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1096   1111       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1116   1130       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1124   1143       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1137   1152       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1157   1169       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1164   1182       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1176   1191       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1198   1210       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1205   1223       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1217   1234       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1238   1248       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1243   1261       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1255   1270       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1274   1288       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1282   1301       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1295   1314       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1324   1336       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1331   1349       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1343   1358       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1367   1380       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1375   1393       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1387   1402       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1418   1430       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1425   1443       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1437   1452       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1470   1483       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1477   1496       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1490   1505       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1513   1526       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1520   1539       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1533   1548       {ECO:0000255|PROSITE-ProRule:PRU00124}.
SQ   SEQUENCE   2213 AA;  247766 MW;  A54232645A5A0DDA CRC64;
     MATRSSRRES RLPFLFTLVA LLPPGALCEV WTRTLHGGRA PLPQERGFRV VQGDPRELRL
     WERGDARGAS RADEKPLRRR RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL
     ARDSLALARP RSSDVYVSYD YGKSFNKISE KLNFGAGNNT EAVVAQFYHS PADNKRYIFA
     DAYAQYLWIT FDFCNTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT
     WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF
     QLRDKYMFAT KVVHLLGSPL QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF
     VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYTPGGAGSD TLVRYFANEP FADFHRVEGL
     QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS EGCSLHLAQR
     LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY
     TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKAFTFSEKP VFVYGLLTEP GEKSTVFTIF
     GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC
     FNGEDFDRPV VVSNCSCTRE DYECDFGFRM SEDLALEVCV PDPGFSGKSS PPVPCPVGST
     YRRSRGYRKI SGDTCSGGDV EARLEGELVP CPLAEENEFI LYATRKSIHR YDLASGTTEQ
     LPLTGLRAAV ALDFDYEHNC LYWSDLALDV IQRLCLNGST GQEVIINSDL ETVEALAFEP
     LSQLLYWVDA GFKKIEVANP DGDFRLTVVN SSVLDRPRAL VLVPQEGIMF WTDWGDLKPG
     IYRSNMDGSA AYRLVSEDVK WPNGISVDDQ WIYWTDAYLD CIERITFSGQ QRSVILDRLP
     HPYAIAVFKN EIYWDDWSQL SIFRASKYSG SQMEILASQL TGLMDMKIFY KGKNTGSNAC
     VPRPCSLLCL PRANNSKSCR CPDGVASSVL PSGDLMCDCP KGYELKNNTC VKEEDTCLRN
     QYRCSNGNCI NSIWWCDFDN DCGDMSDEKN CPTTICDLDT QFRCQESGTC IPLSYKCDLE
     DDCGDNSDER HCEMHQCRSD EYNCSSGMCI RSSWVCDGDN DCRDWSDEAN CTAIYHTCEA
     SNFQCRNGHC IPQRWACDGD ADCQDGSDED PANCEKKCNG FRCPNGTCIP STKHCDGLHD
     CSDGSDEQHC EPLCTRFMDF VCKNRQQCLF HSMVCDGIIQ CRDGSDEDPA FAGCSRDPEF
     HKVCDEFGFQ CQNGVCISLI WKCDGMDDCG DYSDEANCEN PTEAPNCSRY FQFRCDNGHC
     IPNRWKCDRE NDCGDWSDEK DCGDSHVLPS TTPAPSTCLP NYYRCGGGAC VIDTWVCDGY
     RDCADGSDEE ACPSLPNVTA TSSPSQPGRC DRFEFECHQP KKCIPNWRRC DGHQDCQDGQ
     DEANCPTHST LTCMSWEFKC EDGEACIVLS ERCDGFLDCS DESDEKACSD ELTVYKVQNL
     QWTADFSGNV TLTWMRPKKM PSAACVYNVY YRVVGESIWK TLETHSNKTN TVLKVLKPDT
     TYQVKVQVQC LSKVHNTNDF VTLRTPEGLP DAPQNLQLSL HGEEEGVIVG HWSPPTHTHG
     LIREYIVEYS RSGSKVWTSE RAASNFTEIK NLLVNTLYTV RVAAVTSRGI GNWSDSKSIT
     TVKGKAIPPP NIHIDNYDEN SLSFTLTVDG NIKVNGYVVN LFWAFDTHKQ EKKTMNFQGS
     SVSHKVGNLT AQTAYEISAW AKTDLGDSPL SFEHVTTRGV RPPAPSLKAR AINQTAVECT
     WTGPRNVVYG IFYATSFLDL YRNPSSLTTP LHNATVLVGK DEQYLFLVRV VMPYQGPSSD
     YVVVKMIPDS RLPPRHLHAV HTGKTSAVIK WESPYDSPDQ DLFYAIAVKD LIRKTDRSYK
     VKSRNSTVEY TLSKLEPGGK YHVIVQLGNM SKDASVKITT VSLSAPDALK IITENDHVLL
     FWKSLALKEK YFNESRGYEI HMFDSAMNIT AYLGNTTDNF FKISNLKMGH NYTFTVQARC
     LLGSQICGEP AVLLYDELGS GGDASAMQAA RSTDVAAVVV PILFLILLSL GVGFAILYTK
     HRRLQSSFTA FANSHYSSRL GSAIFSSGDD LGEDDEDAPM ITGFSDDVPM VIA
//
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