MPRI_MOUSE
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 03-AUG-2022, entry version 194.
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, Pancreas,
RC 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}.
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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; 10.
DR IntAct; Q07113; 7.
DR MINT; Q07113; -.
DR STRING; 10090.ENSMUSP00000024599; -.
DR GlyConnect; 2195; 7 N-Linked glycans (6 sites).
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; Q07113; -.
DR PeptideAtlas; Q07113; -.
DR PRIDE; Q07113; -.
DR ProteomicsDB; 295591; -.
DR Antibodypedia; 1396; 721 antibodies from 42 providers.
DR DNASU; 16004; -.
DR Ensembl; ENSMUST00000024599; ENSMUSP00000024599; ENSMUSG00000023830.
DR GeneID; 16004; -.
DR KEGG; mmu:16004; -.
DR UCSC; uc008aky.1; mouse.
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; MIQLNYK; -.
DR OrthoDB; 290124at2759; -.
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 75 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 296 other tissues.
DR Genevisible; Q07113; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISO:MGI.
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; IEA:InterPro.
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; -; 1.
DR Gene3D; 2.70.130.10; -; 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 Pfam; PF00878; CIMR; 14.
DR Pfam; PF00040; fn2; 1.
DR SMART; SM00059; FN2; 1.
DR SUPFAM; SSF50911; SSF50911; 15.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS51914; MRH; 15.
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
