ID MPRI_MOUSE Reviewed; 2483 AA. AC Q07113; Q61822; Q6LED1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Cation-independent mannose-6-phosphate receptor; DE Short=CI Man-6-P receptor; DE Short=CI-MPR; DE Short=M6PR; DE AltName: Full=300 kDa mannose 6-phosphate receptor; DE Short=MPR 300; DE AltName: Full=Insulin-like growth factor 2 receptor; DE AltName: Full=Insulin-like growth factor II receptor; DE Short=IGF-II receptor; DE AltName: Full=M6P/IGF2 receptor; DE Short=M6P/IGF2R; DE AltName: CD_antigen=CD222; DE Flags: Precursor; GN Name=Igf2r; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8188212; DOI=10.1006/geno.1994.1021; RA Szebenyi G., Rotwein P.; RT "The mouse insulin-like growth factor II/cation-independent mannose 6- RT phosphate (IGF-II/MPR) receptor gene: molecular cloning and genomic RT organization."; RL Genomics 19:120-129(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=8194771; DOI=10.1016/0378-1119(94)90282-8; RA Ludwig T., Tenscher K., Remmler J., Hoflack B., Lobel P.; RT "Cloning and sequencing of cDNAs encoding the full-length mouse mannose 6- RT phosphate/insulin-like growth factor II receptor."; RL Gene 142:311-312(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 93-106. RC STRAIN=129, and C57BL/6J; RX PubMed=8462104; DOI=10.1016/0092-8674(93)90160-r; RA Stoger R., Kubicka P., Liu C.G., Kafri T., Razin A., Cedar H., Barlow D.P.; RT "Maternal-specific methylation of the imprinted mouse Igf2r locus RT identifies the expressed locus as carrying the imprinting signal."; RL Cell 73:61-71(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. RC STRAIN=129/Sv; RX PubMed=8584025; DOI=10.1210/mend.9.11.8584025; RA Liu Z., Mittanck D.W., Kim S., Rotwein P.; RT "Control of insulin-like growth factor-II/mannose 6-phosphate receptor gene RT transcription by proximal promoter elements."; RL Mol. Endocrinol. 9:1477-1487(1995). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 435-488. RC TISSUE=Liver; RX PubMed=1848553; DOI=10.1016/s0021-9258(19)67627-1; RA Szebenyi G., Rotwein P.; RT "Differential regulation of mannose 6-phosphate receptors and their ligands RT during the myogenic development of C2 cells."; RL J. Biol. Chem. 266:5534-5539(1991). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1625-2045. RC STRAIN=C57BL/6J; RA Matzner U.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2249-2483. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=8226743; DOI=10.1016/s0021-9258(18)41533-5; RA Chen H.J., Remmler J., Delaney J.C., Messner D.J., Lobel P.; RT "Mutational analysis of the cation-independent mannose 6-phosphate/insulin- RT like growth factor II receptor. A consensus casein kinase II site followed RT by 2 leucines near the carboxyl terminus is important for intracellular RT targeting of lysosomal enzymes."; RL J. Biol. Chem. 268:22338-22346(1993). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2471 AND SER-2476, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1532. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-740; ASN-1532 AND ASN-1750. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401; SER-2471 AND SER-2476, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2417, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes CC from the Golgi complex and the cell surface to lysosomes. Lysosomal CC enzymes bearing phosphomannosyl residues bind specifically to mannose- CC 6-phosphate receptors in the Golgi apparatus and the resulting CC receptor-ligand complex is transported to an acidic prelysosomal CC compartment where the low pH mediates the dissociation of the complex. CC The receptor is then recycled back to the Golgi for another round of CC trafficking through its binding to the retromer. This receptor also CC binds IGF2. Acts as a positive regulator of T-cell coactivation by CC binding DPP4. {ECO:0000250|UniProtKB:P11717}. CC -!- SUBUNIT: Binds HA-I and HA-II plasma membrane adapters (By similarity). CC Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and CC GGA3 (By similarity). Interacts with the heterotrimeric retromer cargo- CC selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and CC VPS35; which is involved in retrograde trafficking of the receptor from CC endosomes to the Golgi apparatus (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P11717}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P11717}. Endosome membrane CC {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P11717}. Note=Mainly localized in the Golgi at CC steady state and not detectable in lysosome. Colocalized with DPP4 in CC internalized cytoplasmic vesicles adjacent to the cell surface. CC {ECO:0000250|UniProtKB:P11717}. CC -!- DOMAIN: Contains 15 repeating units of approximately 147 AA harboring CC four disulfide bonds each. The most highly conserved region within the CC repeat consists of a stretch of 13 AA that contains cysteines at both CC ends. CC -!- PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes CC interaction with the retromer cargo-selective complex which mediates CC its retrograde trafficking to the Golgi apparatus. CC {ECO:0000250|UniProtKB:P11717}. CC -!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L22143; AAA39320.1; -; Genomic_DNA. DR EMBL; L22096; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22097; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22098; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22099; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22100; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22101; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22102; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22103; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22104; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22105; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22106; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22107; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22108; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22109; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22110; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22111; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22112; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22113; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22114; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22115; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22116; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22117; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22118; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22119; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22120; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22121; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22122; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22123; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22124; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22125; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22126; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22127; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22128; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22129; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22130; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22131; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22132; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22133; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22134; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22135; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22136; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22137; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22138; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22139; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22140; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22141; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; L22142; AAA39320.1; JOINED; Genomic_DNA. DR EMBL; U04710; AAA19568.1; -; mRNA. DR EMBL; L06445; AAA37921.1; -; Genomic_DNA. DR EMBL; L06446; AAA37922.1; -; Genomic_DNA. DR EMBL; U26348; AAA98844.1; -; Genomic_DNA. DR EMBL; M58586; AAA39483.1; -; Genomic_DNA. DR EMBL; X60389; CAA42940.1; -; mRNA. DR EMBL; L19500; AAA16037.1; -; mRNA. DR CCDS; CCDS37436.1; -. DR PIR; A49617; A49617. DR PIR; I48922; I48922. DR RefSeq; NP_034645.2; NM_010515.2. DR AlphaFoldDB; Q07113; -. DR SMR; Q07113; -. DR BioGRID; 200550; 12. DR IntAct; Q07113; 7. DR MINT; Q07113; -. DR STRING; 10090.ENSMUSP00000024599; -. DR GlyConnect; 2195; 7 N-Linked glycans (6 sites). DR GlyCosmos; Q07113; 20 sites, 7 glycans. DR GlyGen; Q07113; 20 sites, 7 N-linked glycans (6 sites). DR iPTMnet; Q07113; -. DR PhosphoSitePlus; Q07113; -. DR SwissPalm; Q07113; -. DR EPD; Q07113; -. DR jPOST; Q07113; -. DR MaxQB; Q07113; -. DR PaxDb; 10090-ENSMUSP00000024599; -. DR PeptideAtlas; Q07113; -. DR ProteomicsDB; 295591; -. DR Pumba; Q07113; -. DR Antibodypedia; 1396; 832 antibodies from 42 providers. DR DNASU; 16004; -. DR Ensembl; ENSMUST00000024599.14; ENSMUSP00000024599.8; ENSMUSG00000023830.15. DR GeneID; 16004; -. DR KEGG; mmu:16004; -. DR UCSC; uc008aky.1; mouse. DR AGR; MGI:96435; -. DR CTD; 3482; -. DR MGI; MGI:96435; Igf2r. DR VEuPathDB; HostDB:ENSMUSG00000023830; -. DR eggNOG; KOG4504; Eukaryota. DR GeneTree; ENSGT00390000013943; -. DR HOGENOM; CLU_001182_0_0_1; -. DR InParanoid; Q07113; -. DR OMA; DNCEVRD; -. DR OrthoDB; 2910338at2759; -. DR PhylomeDB; Q07113; -. DR TreeFam; TF328963; -. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network. DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR BioGRID-ORCS; 16004; 5 hits in 80 CRISPR screens. DR ChiTaRS; Igf2r; mouse. DR PRO; PR:Q07113; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q07113; Protein. DR Bgee; ENSMUSG00000023830; Expressed in cardiac atrium and 299 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0030118; C:clathrin coat; ISO:MGI. DR GO; GO:0005769; C:early endosome; ISO:MGI. DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0010008; C:endosome membrane; ISO:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005770; C:late endosome; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0005520; F:insulin-like growth factor binding; IPI:MGI. DR GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI. DR GO; GO:0005537; F:mannose binding; IDA:MGI. DR GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB. DR GO; GO:0001972; F:retinoic acid binding; ISO:MGI. DR GO; GO:1905394; F:retromer complex binding; ISO:MGI. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0001889; P:liver development; ISO:MGI. DR GO; GO:0007041; P:lysosomal transport; IBA:GO_Central. DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI. DR GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd00062; FN2; 1. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1. DR Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 15. DR InterPro; IPR000479; CIMR_rpt. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf. DR InterPro; IPR044865; MRH_dom. DR PANTHER; PTHR15071:SF0; CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR; 1. DR PANTHER; PTHR15071; MANNOSE-6-PHOSPHATE RECEPTOR FAMILY MEMBER; 1. DR Pfam; PF00878; CIMR; 14. DR Pfam; PF00040; fn2; 1. DR PRINTS; PR00013; FNTYPEII. DR SMART; SM01404; CIMR; 14. DR SMART; SM00059; FN2; 1. DR SUPFAM; SSF57440; Kringle-like; 1. DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 15. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 1. DR PROSITE; PS51914; MRH; 15. DR Genevisible; Q07113; MM. PE 1: Evidence at protein level; KW Acetylation; Disulfide bond; Endosome; Glycoprotein; Golgi apparatus; KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT CHAIN 36..2483 FT /note="Cation-independent mannose-6-phosphate receptor" FT /id="PRO_0000019230" FT TOPO_DOM 36..2295 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 2296..2316 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2317..2483 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 42..158 FT /note="MRH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 167..315 FT /note="MRH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 321..463 FT /note="MRH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 468..613 FT /note="MRH 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 619..755 FT /note="MRH 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 758..917 FT /note="MRH 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 925..1072 FT /note="MRH 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1075..1212 FT /note="MRH 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1218..1356 FT /note="MRH 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1360..1501 FT /note="MRH 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1507..1641 FT /note="MRH 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1643..1790 FT /note="MRH 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1795..1982 FT /note="MRH 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1891..1937 FT /note="Fibronectin type-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DOMAIN 1985..2120 FT /note="MRH 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 2128..2273 FT /note="MRH 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT REGION 2415..2483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2431..2453 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2342 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11717" FT MOD_RES 2401 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079" FT MOD_RES 2417 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2476 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 430 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 537 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 575 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 620 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 740 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 864 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 944 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1305 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1358 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1423 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1532 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 1649 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1750 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1809 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2078 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2129 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 44..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 72..79 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 112..144 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 129..156 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 169..207 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 223..230 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 270..301 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 283..313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 323..361 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 369..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 415..449 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 429..461 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 470..513 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 525..532 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 566..599 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 580..611 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 621..658 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 666..673 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 724..753 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 760..807 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 816..823 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 868..903 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 886..915 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 927..964 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 970..981 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1035..1070 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1077..1118 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1127..1135 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1170..1198 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1183..1210 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1220..1255 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1263..1275 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1312..1342 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1326..1354 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1362..1401 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1413..1420 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1454..1487 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1469..1499 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1509..1546 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1552..1559 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1591..1627 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1607..1639 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1645..1688 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1699..1706 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1743..1776 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1759..1788 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1797..1832 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1843..1849 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1886..1968 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1896..1920 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 1910..1935 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 1950..1980 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1987..2022 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2032..2039 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2075..2106 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2089..2118 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2181..2187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2225..2259 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2241..2271 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT CONFLICT 10..11 FT /note="PS -> RP (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 13 FT /note="Missing (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 209 FT /note="D -> V (in Ref. 2; AAA19568)" FT /evidence="ECO:0000305" FT CONFLICT 456..457 FT /note="DT -> VS (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 1626..1631 FT /note="TCTLFF -> GSTFFS (in Ref. 6; CAA42940)" FT /evidence="ECO:0000305" FT CONFLICT 1694..1695 FT /note="MH -> TC (in Ref. 6; CAA42940)" FT /evidence="ECO:0000305" FT CONFLICT 1699 FT /note="C -> R (in Ref. 6; CAA42940)" FT /evidence="ECO:0000305" FT CONFLICT 1759 FT /note="C -> Y (in Ref. 2; AAA19568)" FT /evidence="ECO:0000305" FT CONFLICT 2028 FT /note="G -> V (in Ref. 6; CAA42940)" FT /evidence="ECO:0000305" FT CONFLICT 2032 FT /note="C -> S (in Ref. 6; CAA42940)" FT /evidence="ECO:0000305" SQ SEQUENCE 2483 AA; 273815 MW; 8F64F6189FD05CD1 CRC64; MRAVQLGPVP SGPRVALLPP LLLLLLLAAA GSAQAQAVDL DALCSYTWEA VDSKNNAVYK INVCGNVGIS SCGPTSAICM CDLKTENCRS VGDSLLRSSA RSLLEFNTTM GCQPSDSQHR IQTSITFLCG KTLGTPEFVT ATDCVHYFEW RTTAACKKDI FKADKEVPCY AFDDKLQKHD LNPLIKLNGG YLVDDSDPDT SLFINVCRDI DSLRDPSTQL RVCPAGTAAC LLKGNQAFDV GRPKEGLKLL SKDRLVLTYV KEEGEKPDFC NGHSPAVTVT FVCPSERREG TIPKLTAKSN CRYEVEWITE YACHRDYLQS ESCSLSSEQH DITIDLSPLA QYGGSPYVSD GREYTFFINV CGDTKVSLCN NKEAAVCQEK KADSTQVKIA GRHQNQTLRY SDGDLTLIYS GGDECSSGFQ RMSVINFECN KTAGKDGRGE PVFTGEVDCT YFFTWDTKYA CIKEKEDLLC GAINGKKRYD LSVLARHSES EQNWEAVDGS QAESEKYFFI NVCHRVLQEG KARNCPEDAA VCAVDKNGSK NLGKFVSSPT KEKGHIQLSY TDGDDCGSDK KISTNITLVC KPGDLESAPV LRAARSDGCF YEFEWHTAAA CVLSKTEGEN CTVLDAQAGF SFDLSLLTKK NGAYKVETEK YDFYINVCGP VSMDPCQSNS GACQVAKSGK SWNLGLSSTK LTYYDGMIQL SYRNGTPYNN EKHTPRATLI TFLCDRDAGV GFPEYQEEDN STYNFRWYTS YACPEEPLEC MVTDPSMMEQ YDLSSLVKSE GGSGGNWYAM ENSREHVTRR KYYLNVCRPL NPVPGCDRYA SACQMKYENH EGSLAETVSI SNLGVAKIGP VVEESGSLLL EYVNGSACTT SDGQLTTYST RIHLVCGRGF MNSHPIFTFN WECVVSFLWN TEAACPIQTI TETDQACSIR DPSSGFVFNL SPLNDSAQGH VVLGIGKTFV FNICGAMPAC GTVAGKPAYG CEAETQIEDI KDLRPQRPVG MERSLQLSAE GFLTLTYKGS SPSDRGTAFI IRFICNDDIY PGAPKFLHQD IDSTRGIRNT YFEFETALAC TPSLVDCQVT DPAGNEYDLS ALSMVRKPWT AVDTSAYGKR RHFYLSVCNP LPYIPGCHGI ALGSCMVSED NSFNLGVVQI SPQATGNGSL SILYVNGDRC GDQRFSTRIV FECAQTSGSP MFQFVNNCEY VFVWRTVEAC PVIREEGDNC QVKDPRHGNL YDLKPLGLND TIVSVGEYTY YLRVCGKLSS DVCSAHDGSK AVSSCQEKKG PQGFQKVAGL LSQKLTFENG LLKMNYTGGD TCHKVYQRST TIYFYCDRTT QKPVFLKETS DCSYMFEWRT QYACPPFNVT ECSVQDAAGN SIDLSSLSRY SDNWEAVTRT GATEHYLINV CKSLSPHAGT EPCPPEAAVC LLNGSKPVNL GKVRDGPQWT DGVTVLQYVD GDLCPDKIRR RSTIIRFTCS DNQVNSRPLF ISAVQDCEYT FSWPTPSACP VKSNTHDDCQ VTNPSTGHLF DLSSLSGRAG INASYSEKGL VFMSICEENE NCGPGVGACF GQTRISVGKA SKRLSYKDQV LQLVYENGSP CPSLSDLRYK SVISFVCRPE AGPTNRPMLI SLDKQTCTLF FSWHTPLACE QATECTVRNG SSIIDLSPLI HRTGGYEAYD ESEDDTSDTT PDFYINICQP LNPMHGVPCP AGASVCKVPV DGPPIDIGRV TGPPIFNPVA NEVYLNFESS THCLADRYMN YTSLITFHCK RGVSMGTPKL IRTNDCDFVF EWETPIVCPD EVKTQGCAVT DEQLLYSFNL TSLSTSTFKV TRDARTYSIG VCTAAAGLGQ EGCKDGGVCL LSGNKGASFG RLASMQLDYR HQDEAVILSY VNGDPCPPET DDGEPCVFPF IYKGKSYDEC VLEGRAKLWC SKTANYDRDH EWGFCRQTNS YRMSAIIFTC DESEDIGRPQ VFSEDRGCEV TFEWKTKVVC PPKKMECKFV QKHKTYDLRL LSSLTGSWDF VHEGNSYFIN LCQRVYKGPL DCSERASICK KSATGQVQVL GLVHTQKLEV IDETVIVTYS KGYPCGGNKT ASSVIELTCA KTVGRPAFKR FDSVSCTYYF YWYSRAACAV RPQEVTMVNG TLTNPVTGKS FSLGEIYFKL FSASGDMRTN GDNYLYEIQL SSITSSSYPA CAGANICQVK PNDQHFSRKV GTSDMTKYYV QDGDLDVVFT SSSKCGKDKT KSVSSTIFFH CDPLVKDGIP EFSHETADCQ YLFSWYTSAV CPLGVDFEDE SAGPEYKGLS ERSQAVGAVL SLLLVALTGC LLALLLHKKE RRETVINKLT SCCRRSSGVS YKYSKVSKEE ETDENETEWL MEEIQVPAPR LGKDGQENGH ITTKAVKAEA LSSLHGDDQD SEDEVLTVPE VKVHSGRGAE VESSQPLRNP QRKVLKEREG ERLGLVRGEK ARKGKFRPGQ RKPTAPAKLV SFHDDSDEDL LHI //