CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018791
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sortilin-related receptor 
Protein Synonyms/Alias
 Low-density lipoprotein receptor relative with 11 ligand-binding repeats; LDLR relative with 11 ligand-binding repeats; LR11; SorLA-1; Sorting protein-related receptor containing LDLR class A repeats; SorLA 
Gene Name
 SORL1 
Gene Synonyms/Alias
 C11orf32 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
260WGIDPYDKPNTIYIEubiquitination[1]
305RDFQLRDKYMFATKVubiquitination[1]
446RSVITFDKGGTWEFLubiquitination[1]
730RRTRGYRKISGDTCSubiquitination[1]
988LSIFRASKYSGSQMEubiquitination[1]
1489KTCIPNWKRCDGHQDubiquitination[1]
1580LTWMRPKKMPSASCVubiquitination[1]
1634VQVQCLSKAHNTNDFubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 136 147 BNR 1.
 REPEAT 232 243 BNR 2.
 REPEAT 441 452 BNR 3.
 REPEAT 521 532 BNR 4.
 REPEAT 562 573 BNR 5.
 REPEAT 800 843 LDL-receptor class B 1.
 REPEAT 844 887 LDL-receptor class B 2.
 REPEAT 888 932 LDL-receptor class B 3.
 REPEAT 933 970 LDL-receptor class B 4.
 REPEAT 971 1013 LDL-receptor class B 5.
 DOMAIN 1026 1072 EGF-like.
 DOMAIN 1076 1114 LDL-receptor class A 1.
 DOMAIN 1115 1155 LDL-receptor class A 2.
 DOMAIN 1156 1194 LDL-receptor class A 3.
 DOMAIN 1198 1236 LDL-receptor class A 4.
 DOMAIN 1238 1272 LDL-receptor class A 5.
 DOMAIN 1273 1317 LDL-receptor class A 6.
 DOMAIN 1323 1361 LDL-receptor class A 7.
 DOMAIN 1366 1405 LDL-receptor class A 8.
 DOMAIN 1417 1455 LDL-receptor class A 9.
 DOMAIN 1469 1508 LDL-receptor class A 10.
 DOMAIN 1512 1551 LDL-receptor class A 11.
 DOMAIN 1554 1646 Fibronectin type-III 1.
 DOMAIN 1651 1742 Fibronectin type-III 2.
 DOMAIN 1749 1838 Fibronectin type-III 3.
 DOMAIN 1843 1927 Fibronectin type-III 4.
 DOMAIN 1934 2023 Fibronectin type-III 5.
 DOMAIN 2024 2118 Fibronectin type-III 6.
 MOTIF 63 65 Cell attachment site (Potential).
 MOTIF 2172 2177 Endocytosis signal (Potential).
 MOD_RES 114 114 Phosphoserine.
 MOD_RES 2206 2206 Phosphoserine; by ROCK2.
 CARBOHYD 99 99 N-linked (GlcNAc...).
 CARBOHYD 158 158 N-linked (GlcNAc...) (Potential).
 CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
 CARBOHYD 430 430 N-linked (GlcNAc...) (Potential).
 CARBOHYD 616 616 N-linked (GlcNAc...) (Potential).
 CARBOHYD 674 674 N-linked (GlcNAc...) (Potential).
 CARBOHYD 818 818 N-linked (GlcNAc...) (Potential).
 CARBOHYD 871 871 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1035 1035 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1068 1068 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1164 1164 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1191 1191 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1246 1246 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1367 1367 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1458 1458 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1608 1608 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1706 1706 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1733 1733 N-linked (GlcNAc...).
 CARBOHYD 1809 1809 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1854 1854 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1894 1894 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1986 1986 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2010 2010 N-linked (GlcNAc...).
 CARBOHYD 2054 2054 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2069 2069 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2076 2076 N-linked (GlcNAc...).
 CARBOHYD 2092 2092 N-linked (GlcNAc...).
 DISULFID 1078 1090 By similarity.
 DISULFID 1085 1103 By similarity.
 DISULFID 1097 1112 By similarity.
 DISULFID 1117 1131 By similarity.
 DISULFID 1125 1144 By similarity.
 DISULFID 1138 1153 By similarity.
 DISULFID 1158 1170 By similarity.
 DISULFID 1165 1183 By similarity.
 DISULFID 1177 1192 By similarity.
 DISULFID 1199 1211 By similarity.
 DISULFID 1206 1224 By similarity.
 DISULFID 1218 1235 By similarity.
 DISULFID 1239 1249 By similarity.
 DISULFID 1244 1262 By similarity.
 DISULFID 1256 1271 By similarity.
 DISULFID 1275 1289 By similarity.
 DISULFID 1283 1302 By similarity.
 DISULFID 1296 1315 By similarity.
 DISULFID 1325 1337 By similarity.
 DISULFID 1332 1350 By similarity.
 DISULFID 1344 1359 By similarity.
 DISULFID 1368 1381 By similarity.
 DISULFID 1376 1394 By similarity.
 DISULFID 1388 1403 By similarity.
 DISULFID 1419 1431 By similarity.
 DISULFID 1426 1444 By similarity.
 DISULFID 1438 1453 By similarity.
 DISULFID 1471 1484 By similarity.
 DISULFID 1478 1497 By similarity.
 DISULFID 1491 1506 By similarity.
 DISULFID 1514 1527 By similarity.
 DISULFID 1521 1540 By similarity.
 DISULFID 1534 1549 By similarity.  
Keyword
 3D-structure; Cholesterol metabolism; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; LDL; Lipid metabolism; Lipid transport; Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2214 AA 
Protein Sequence
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQRLHGGSA PLPQDRGFLV VQGDPRELRL 60
WARGDARGAS RADEKPLRRK RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL 120
ARDSLALARP KSSDVYVSYD YGKSFKKISD KLNFGLGNRS EAVIAQFYHS PADNKRYIFA 180
DAYAQYLWIT FDFCNTLQGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT 240
WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF 300
QLRDKYMFAT KVVHLLGSEQ QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF 360
VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL 420
QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR 480
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY 540
TWGDHGGIIT AIAQGMETNE LKYSTNEGET WKTFIFSEKP VFVYGLLTEP GEKSTVFTIF 600
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC 660
FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKSY SPPVPCPVGS 720
TYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAVRKSIY RYDLASGATE 780
QLPLTGLRAA VALDFDYEHN CLYWSDLALD VIQRLCLNGS TGQEVIINSG LETVEALAFE 840
PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 900
GIYRSNMDGS AAYHLVSEDV KWPNGISVDD QWIYWTDAYL ECIERITFSG QQRSVILDNL 960
PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSQMEILANQ LTGLMDMKIF YKGKNTGSNA 1020
CVPRPCSLLC LPKANNSRSC RCPEDVSSSV LPSGDLMCDC PQGYQLKNNT CVKQENTCLR 1080
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTICDLD TQFRCQESGT CIPLSYKCDL 1140
EDDCGDNSDE SHCEMHQCRS DEYNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 1200
ASNFQCRNGH CIPQRWACDG DTDCQDGSDE DPVNCEKKCN GFRCPNGTCI PSSKHCDGLR 1260
DCSDGSDEQH CEPLCTHFMD FVCKNRQQCL FHSMVCDGII QCRDGSDEDA AFAGCSQDPE 1320
FHKVCDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFRCENGH 1380
CIPNRWKCDR ENDCGDWSDE KDCGDSHILP FSTPGPSTCL PNYYRCSSGT CVMDTWVCDG 1440
YRDCADGSDE EACPLLANVT AASTPTQLGR CDRFEFECHQ PKTCIPNWKR CDGHQDCQDG 1500
RDEANCPTHS TLTCMSREFQ CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN 1560
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT NTVLKVLKPD 1620
TTYQVKVQVQ CLSKAHNTND FVTLRTPEGL PDAPRNLQLS LPREAEGVIV GHWAPPIHTH 1680
GLIREYIVEY SRSGSKMWAS QRAASNFTEI KNLLVNTLYT VRVAAVTSRG IGNWSDSKSI 1740
TTIKGKVIPP PDIHIDSYGE NYLSFTLTME SDIKVNGYVV NLFWAFDTHK QERRTLNFRG 1800
SILSHKVGNL TAHTSYEISA WAKTDLGDSP LAFEHVMTRG VRPPAPSLKA KAINQTAVEC 1860
TWTGPRNVVY GIFYATSFLD LYRNPKSLTT SLHNKTVIVS KDEQYLFLVR VVVPYQGPSS 1920
DYVVVKMIPD SRLPPRHLHV VHTGKTSVVI KWESPYDSPD QDLLYAVAVK DLIRKTDRSY 1980
KVKSRNSTVE YTLNKLEPGG KYHIIVQLGN MSKDSSIKIT TVSLSAPDAL KIITENDHVL 2040
LFWKSLALKE KHFNESRGYE IHMFDSAMNI TAYLGNTTDN FFKISNLKMG HNYTFTVQAR 2100
CLFGNQICGE PAILLYDELG SGADASATQA ARSTDVAAVV VPILFLILLS LGVGFAILYT 2160
KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP MITGFSDDVP MVIA 2214 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
 GO:0030169; F:low-density lipoprotein particle binding; IPI:BHF-UCL.
 GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
 GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
 GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
 GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR000742; EG-like_dom.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR023415; LDLR_class-A_CS.
 IPR000033; LDLR_classB_rpt.
 IPR002172; LDrepeatLR_classA_rpt.
 IPR006581; VPS10. 
Pfam
 PF00041; fn3
 PF00057; Ldl_recept_a
 PF00058; Ldl_recept_b 
SMART
 SM00181; EGF
 SM00060; FN3
 SM00192; LDLa
 SM00135; LY
 SM00602; VPS10 
PROSITE
 PS01186; EGF_2
 PS50026; EGF_3
 PS50853; FN3
 PS01209; LDLRA_1
 PS50068; LDLRA_2
 PS51120; LDLRB 
PRINTS