8JXF
rat megalin RAP complex bodyA
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNmrgsFrCaC |
| Chain | Residue | Details |
| B | CYS1405-CYS1416 | |
| B | CYS3128-CYS3139 | |
| B | CYS3169-CYS3180 | |
| B | CYS4023-CYS4034 |
| site_id | PS00014 |
| Number of Residues | 4 |
| Details | ER_TARGET Endoplasmic reticulum targeting sequence. HNEL |
| Chain | Residue | Details |
| C | HIS357-LEU360 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CkCssGysGEyC |
| Chain | Residue | Details |
| B | CYS4401-CYS4412 |
| site_id | PS00615 |
| Number of Residues | 27 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVdideckespq..LCSQKCenvvgsYIC |
| Chain | Residue | Details |
| B | CYS3152-CYS3178 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. ClCeeGYilergqh.C |
| Chain | Residue | Details |
| B | CYS370-CYS384 | |
| B | CYS688-CYS703 | |
| B | CYS1374-CYS1389 | |
| B | CYS1726-CYS1741 | |
| B | CYS2044-CYS2059 | |
| B | CYS3137-CYS3152 | |
| B | CYS3178-CYS3193 | |
| B | CYS4401-CYS4412 |
| site_id | PS01187 |
| Number of Residues | 24 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiNECdipgf.........Csqh....CvNmrgsFrC |
| Chain | Residue | Details |
| B | ASP1391-CYS1414 | |
| B | ASP3154-CYS3178 | |
| B | ASP4009-CYS4032 |
| site_id | PS01209 |
| Number of Residues | 23 |
| Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpaswr.CDgtrDCldd.TDEig...C |
| Chain | Residue | Details |
| B | CYS40-CYS62 | |
| B | CYS1201-CYS1223 | |
| B | CYS1244-CYS1267 | |
| B | CYS1284-CYS1306 | |
| B | CYS1326-CYS1349 | |
| B | CYS2713-CYS2737 | |
| B | CYS2754-CYS2776 | |
| B | CYS2836-CYS2860 | |
| B | CYS2878-CYS2901 | |
| B | CYS2920-CYS2945 | |
| B | CYS3007-CYS3029 | |
| B | CYS80-CYS103 | |
| B | CYS3046-CYS3070 | |
| B | CYS3089-CYS3111 | |
| B | CYS3527-CYS3550 | |
| B | CYS3608-CYS3632 | |
| B | CYS3649-CYS3673 | |
| B | CYS3694-CYS3716 | |
| B | CYS3734-CYS3756 | |
| B | CYS3773-CYS3795 | |
| B | CYS3812-CYS3834 | |
| B | CYS3856-CYS3880 | |
| B | CYS120-CYS142 | |
| B | CYS3898-CYS3922 | |
| B | CYS3942-CYS3964 | |
| B | CYS195-CYS217 | |
| B | CYS234-CYS256 | |
| B | CYS1037-CYS1059 | |
| B | CYS1079-CYS1101 | |
| B | CYS1122-CYS1144 | |
| B | CYS1162-CYS1184 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| C | SER53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P55302 |
| Chain | Residue | Details |
| C | SER138 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| C | ASN271 |
