| Tag | Content |
|---|
| CPLM ID | CPLM-001346 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Sortilin-related receptor |
Protein Synonyms/Alias | Gp250; 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; mSorLA |
Gene Name | Sorl1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1996 | TVEYSLSKLEPGGKY | acetylation | [1] |
|
Reference | [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation. Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ. J Biol Chem. 2013 Jul 17;. [ PMID: 23864654] |
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. May play a role in neural organization, as well as the establishment of embryonic organ systems. |
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 933 972 LDL-receptor class B 4.
REPEAT 973 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 1751 1839 Fibronectin type-III 3.
DOMAIN 1844 1928 Fibronectin type-III 4.
DOMAIN 1935 2024 Fibronectin type-III 5.
DOMAIN 2025 2119 Fibronectin type-III 6.
MOTIF 2173 2178 Endocytosis signal (Potential).
MOD_RES 114 114 Phosphoserine (By similarity).
MOD_RES 2207 2207 Phosphoserine; by ROCK2 (By similarity).
CARBOHYD 99 99 N-linked (GlcNAc...) (Potential).
CARBOHYD 158 158 N-linked (GlcNAc...) (Potential).
CARBOHYD 367 367 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...) (Potential).
CARBOHYD 1810 1810 N-linked (GlcNAc...) (Potential).
CARBOHYD 1855 1855 N-linked (GlcNAc...) (Potential).
CARBOHYD 1895 1895 N-linked (GlcNAc...) (Potential).
CARBOHYD 1987 1987 N-linked (GlcNAc...) (Potential).
CARBOHYD 2011 2011 N-linked (GlcNAc...) (Potential).
CARBOHYD 2055 2055 N-linked (GlcNAc...) (Potential).
CARBOHYD 2070 2070 N-linked (GlcNAc...) (Potential).
CARBOHYD 2077 2077 N-linked (GlcNAc...) (Potential).
CARBOHYD 2093 2093 N-linked (GlcNAc...) (Potential).
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 | Cholesterol metabolism; Cleavage on pair of basic residues; Complete proteome; Developmental protein; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; LDL; Lipid metabolism; Lipid transport; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2215 AA |
Protein Sequence | MATRSSRRES RLPFLFALVA LLPRGALGGG WTQRLHGGPA PLPQDRGFFV VQGDPRDLRL 60
GTHGDAPGAS PAARKPLRTR RSAALQPQPI QVYGQVSLND SHNQMVVHWA GEKSNVIVAL 120
ARDSLALARP KSSDVYVSYD YGKSFSKISE KLNFGVGNNS EAVISQFYHS PADNKRYIFV 180
DAYAQYLWIT FDFCSTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT 240
WIMIQEHVKS FSWGIDPYDQ PNAIYIERHE PFGFSTVLRS TDFFQSRENQ EVILEEVRDF 300
QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY IADAAEDQVF 360
VCVSHSNNST NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL 420
QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR 480
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY 540
TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF 600
GSNKESVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC 660
FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKPY SPPVPCPVGS 720
SYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAMRKSIY RYDLASGATE 780
QLPLSGLRAA VALDFDYERN CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE 840
PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 900
GIYRSYMDGS AAYRLVSEDV KWPNGISVDS QWIYWTDAYL DCIERITFSG QQRSVILDSL 960
PHPYAIAVFK NEIYWDDWSQ LSIFRASKHS RSQVEILASQ LTGLMDMKVF YKGKNAGSNA 1020
CVPQPCSLLC LPKANNSKSC RCPEGVASSV LPSGDLMCDC PQGYQRKNNT CVKEENTCLR 1080
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL 1140
EDDCGDNSDE SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 1200
ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI PSSKHCDGLR 1260
DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV QCRDGSDEDA AFAGCSQDPE 1320
FHKECDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFHCENGH 1380
CIPNRWKCDR ENDCGDWSDE KDCGDSHVLP SPTPGPSTCL PNYFHCSSGA CVMGTWVCDG 1440
YRDCADGSDE EACPSLANST AASTPTQFGQ CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG 1500
QDEANCPTHS TLTCTSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN 1560
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT STVLKVLKPD 1620
TTYQVKVQVH CLNKVHNTND FVTLRTPEGL PDAPRNLQLS LNSEEEGVIL GHWAPPVHTH 1680
GLIREYIVEY SRSGSKMWAS QRAASNSTEI KNLLLNALYT VRVAAVTSRG IGNWSDSKSI 1740
TTIKGKVIQA PNIHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLSFRG 1800
GSALSHRVSN LTAHTSYEIS AWAKTDLGDS PLAFEHILTR GSSPPAPSLK AKAINQTAVE 1860
CIWTGPKNVV YGIFYATSFL DLYRNPKSVT TSLHNKTVIV SKDEQYLFLV RVLIPYQGPS 1920
SDYVVVKMIP DSRLPPRHLH AVHIGKTSAL IKWESPYDSP DQDLFYAIAV KDLIRKTDRS 1980
YKVRSRNSTV EYSLSKLEPG GKYHIIVQLG NMSKDSSIKI TTVSLSAPDA LKIITENDHV 2040
LLFWKSLALK EKQFNETRGY EIHMSDSAVN LTAYLGNTTD NFFKVSNLKM GHNYTFTVQA 2100
RCLFGSQICG EPAVLLYDEL SSGADAAVIQ AARSTDVAAV VVPILFLILL SLGVGFAILY 2160
TKHRRLQSSF SAFANSHYSS RLGSAIFSSG DDLGEDDEDA PMITGFSDDV PMVIA 2215 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW. GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. GO:0030169; F:low-density lipoprotein particle binding; IEA:Compara. GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW. GO:0006897; P:endocytosis; IEA:UniProtKB-KW. GO:0006869; P:lipid transport; IEA:UniProtKB-KW. GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |