MPRI_HUMAN
ID MPRI_HUMAN Reviewed; 2491 AA.
AC P11717; Q7Z7G9; Q96PT5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 233.
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; Synonyms=MPRI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-1619,
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-23, AND TOPOLOGY.
RX PubMed=2957598; DOI=10.1038/329301a0;
RA Morgan D.O., Edman J.C., Standring D.N., Fried V.A., Smith M.C., Roth R.A.,
RA Rutter W.J.;
RT "Insulin-like growth factor II receptor as a multifunctional binding
RT protein.";
RL Nature 329:301-307(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-1619, AND FUNCTION.
RX PubMed=2963003; DOI=10.1016/s0021-9258(18)69243-9;
RA Oshima A., Nolan C.M., Kyle J.W., Grubb J.H., Sly W.S.;
RT "The human cation-independent mannose 6-phosphate receptor. Cloning and
RT sequence of the full-length cDNA and expression of functional receptor in
RT COS cells.";
RL J. Biol. Chem. 263:2553-2562(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-1619.
RA Gemma A., Seike Y., Uematsu K., Seike M., Bennett W.P., Harris C.C.,
RA Kudoh S.;
RT "The genomic structure of the gene encoding the human mannose 6
RT phosphate/insulin-like growth factor 2 receptor (M6P/IGF2R).";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9892739; DOI=10.1007/s003359900947;
RA Killian J.K., Jirtle R.L.;
RT "Genomic structure of the human M6P/IGF2 receptor.";
RL Mamm. Genome 10:74-77(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-91; LEU-203; ASP-231;
RP VAL-252; GLY-273; GLN-512; SER-604; THR-724; VAL-817; SER-856; MET-1107;
RP ILE-1124; SER-1184; GLU-1315; HIS-1335; GLY-1619; HIS-1832; ASP-1860;
RP MET-1908; SER-2020 AND VAL-2459.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP FUNCTION, INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION.
RX PubMed=10900005; DOI=10.1073/pnas.97.15.8439;
RA Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H.,
RA Schlossman S.F., Morimoto C.;
RT "Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor
RT II receptor contributes to T cell activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000).
RN [8]
RP INTERACTION WITH GGA1; GGA2 AND GGA3.
RX PubMed=11387475; DOI=10.1126/science.1060750;
RA Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.;
RT "Sorting of mannose 6-phosphate receptors mediated by the GGAs.";
RL Science 292:1712-1716(2001).
RN [9]
RP GLYCOSYLATION AT ASN-112; ASN-581; ASN-747 AND ASN-1246.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [17]
RP FUNCTION, INTERACTION WITH THE RETROMER COMPLEX, SUBCELLULAR LOCATION, AND
RP PALMITOYLATION.
RX PubMed=18817523; DOI=10.1111/j.1600-0854.2008.00814.x;
RA McCormick P.J., Dumaresq-Doiron K., Pluviose A.S., Pichette V., Tosato G.,
RA Lefrancois S.;
RT "Palmitoylation controls recycling in lysosomal sorting and trafficking.";
RL Traffic 9:1984-1997(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-626 AND ASN-747.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2352, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1508-2128 ALONE AND IN COMPLEX
RP WITH IGF2, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=18046459; DOI=10.1038/sj.emboj.7601938;
RA Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J., van Boxel G.,
RA Denley A., Wallace J.C., Hassan A.B., Forbes B.E., Jones E.Y.;
RT "Structure and functional analysis of the IGF-II/IGF2R interaction.";
RL EMBO J. 27:265-276(2008).
CC -!- FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes
CC from the Golgi complex and the cell surface to lysosomes
CC (PubMed:2963003, PubMed:18817523). Lysosomal enzymes bearing
CC phosphomannosyl residues bind specifically to mannose-6-phosphate
CC receptors in the Golgi apparatus and the resulting receptor-ligand
CC complex is transported to an acidic prelysosomal compartment where the
CC low pH mediates the dissociation of the complex (PubMed:2963003,
CC PubMed:18817523). The receptor is then recycled back to the Golgi for
CC another round of trafficking through its binding to the retromer
CC (PubMed:18817523). This receptor also binds IGF2 (PubMed:18046459).
CC Acts as a positive regulator of T-cell coactivation by binding DPP4
CC (PubMed:10900005). {ECO:0000269|PubMed:10900005,
CC ECO:0000269|PubMed:18046459, ECO:0000269|PubMed:18817523,
CC ECO:0000269|PubMed:2963003}.
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. Interacts with the heterotrimeric retromer cargo-selective
CC complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35;
CC which is involved in retrograde trafficking of the receptor from
CC endosomes to the Golgi apparatus (Probable). {ECO:0000250,
CC ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11387475,
CC ECO:0000269|PubMed:18046459, ECO:0000305|PubMed:18817523}.
CC -!- INTERACTION:
CC P11717; Q9UJY5: GGA1; NbExp=4; IntAct=EBI-1048580, EBI-447141;
CC P11717; Q9NZ52: GGA3; NbExp=3; IntAct=EBI-1048580, EBI-447404;
CC P11717; P01344: IGF2; NbExp=17; IntAct=EBI-1048580, EBI-7178764;
CC P11717; P01344-1: IGF2; NbExp=2; IntAct=EBI-1048580, EBI-15658078;
CC P11717; P11717: IGF2R; NbExp=4; IntAct=EBI-1048580, EBI-1048580;
CC P11717; Q6VY07: PACS1; NbExp=2; IntAct=EBI-1048580, EBI-2555014;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:2957598}. Endosome membrane
CC {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:2957598}. Note=Mainly localized in the Golgi at
CC steady state and not detectable in lysosome (PubMed:18817523).
CC Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to
CC the cell surface (PubMed:10900005). {ECO:0000269|PubMed:10900005,
CC ECO:0000269|PubMed:18817523}.
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 (PubMed:18817523). Undergoes cysteine S-
CC palmitoylation which promotes interaction with the retromer cargo-
CC selective complex which mediates its retrograde trafficking to the
CC Golgi apparatus (PubMed:18817523). {ECO:0000269|PubMed:18817523}.
CC -!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IGF2RID380.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/igf2r/";
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DR EMBL; Y00285; CAA68395.1; -; mRNA.
DR EMBL; J03528; AAA59866.1; -; mRNA.
DR EMBL; AF109291; AAF16870.1; -; Genomic_DNA.
DR EMBL; AF109244; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109245; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109246; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109247; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109248; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109249; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109250; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109251; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109252; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109253; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109254; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109255; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109256; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109257; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109258; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109259; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109260; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109261; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109262; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109263; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109264; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109265; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109266; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109267; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109268; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109269; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109270; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109271; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109272; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109273; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109274; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109275; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109276; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109277; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109278; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109279; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109280; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109281; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109282; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109283; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109284; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109285; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109286; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109287; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109288; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109289; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF109290; AAF16870.1; JOINED; Genomic_DNA.
DR EMBL; AF069333; AAL04402.1; -; Genomic_DNA.
DR EMBL; AY293855; AAP37954.1; -; Genomic_DNA.
DR EMBL; AL353625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS5273.1; -.
DR PIR; A28372; A28372.
DR RefSeq; NP_000867.2; NM_000876.3.
DR PDB; 1E6F; X-ray; 1.75 A; A/B=1508-1650.
DR PDB; 1GP0; X-ray; 1.40 A; A=1508-1650.
DR PDB; 1GP3; X-ray; 1.95 A; A=1508-1650.
DR PDB; 1GQB; X-ray; 1.80 A; A/B=1508-1650.
DR PDB; 1JPL; X-ray; 2.40 A; E/F/G/H=2480-2491.
DR PDB; 1JWG; X-ray; 2.00 A; C/D=2479-2491.
DR PDB; 1LF8; X-ray; 2.30 A; E/F/G/H=2480-2491.
DR PDB; 2CNJ; NMR; -; D=1508-1650.
DR PDB; 2L29; NMR; -; A=1508-1647.
DR PDB; 2L2A; NMR; -; A=1508-1647.
DR PDB; 2M68; NMR; -; A=1508-1647.
DR PDB; 2M6T; NMR; -; A=1508-1647.
DR PDB; 2V5N; X-ray; 3.20 A; A=1508-1799.
DR PDB; 2V5O; X-ray; 2.91 A; A=1508-2128.
DR PDB; 2V5P; X-ray; 4.10 A; A/B=1508-1992.
DR PDB; 5IEI; X-ray; 2.80 A; A=1508-1647.
DR PDB; 6N5X; X-ray; 2.05 A; A=2347-2377.
DR PDB; 6N5Y; X-ray; 2.26 A; A=2347-2377.
DR PDB; 6P8I; X-ray; 2.54 A; A=36-763.
DR PDB; 6V02; X-ray; 2.46 A; A=43-763.
DR PDB; 6Z30; X-ray; 1.50 A; A=1222-1510.
DR PDB; 6Z31; X-ray; 2.56 A; A/B=1082-1220.
DR PDB; 6Z32; X-ray; 3.47 A; A/B=927-1649.
DR PDBsum; 1E6F; -.
DR PDBsum; 1GP0; -.
DR PDBsum; 1GP3; -.
DR PDBsum; 1GQB; -.
DR PDBsum; 1JPL; -.
DR PDBsum; 1JWG; -.
DR PDBsum; 1LF8; -.
DR PDBsum; 2CNJ; -.
DR PDBsum; 2L29; -.
DR PDBsum; 2L2A; -.
DR PDBsum; 2M68; -.
DR PDBsum; 2M6T; -.
DR PDBsum; 2V5N; -.
DR PDBsum; 2V5O; -.
DR PDBsum; 2V5P; -.
DR PDBsum; 5IEI; -.
DR PDBsum; 6N5X; -.
DR PDBsum; 6N5Y; -.
DR PDBsum; 6P8I; -.
DR PDBsum; 6V02; -.
DR PDBsum; 6Z30; -.
DR PDBsum; 6Z31; -.
DR PDBsum; 6Z32; -.
DR AlphaFoldDB; P11717; -.
DR SASBDB; P11717; -.
DR SMR; P11717; -.
DR BioGRID; 109703; 311.
DR CORUM; P11717; -.
DR DIP; DIP-6027N; -.
DR ELM; P11717; -.
DR IntAct; P11717; 65.
DR MINT; P11717; -.
DR STRING; 9606.ENSP00000349437; -.
DR BindingDB; P11717; -.
DR ChEMBL; CHEMBL3240; -.
DR DrugBank; DB02900; alpha-D-mannose 6-phosphate.
DR DrugBank; DB16099; Avalglucosidase alfa.
DR DrugBank; DB13173; Cerliponase alfa.
DR DrugBank; DB01277; Mecasermin.
DR DrugBank; DB14751; Mecasermin rinfabate.
DR TCDB; 9.B.247.1.2; the mannose 6-phosphate receptor (m6pr) family.
DR UniLectin; P11717; -.
DR GlyConnect; 1084; 38 N-Linked glycans (16 sites).
DR GlyGen; P11717; 27 sites, 40 N-linked glycans (16 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; P11717; -.
DR PhosphoSitePlus; P11717; -.
DR SwissPalm; P11717; -.
DR BioMuta; IGF2R; -.
DR DMDM; 317373416; -.
DR CPTAC; CPTAC-2601; -.
DR CPTAC; non-CPTAC-2642; -.
DR EPD; P11717; -.
DR jPOST; P11717; -.
DR MassIVE; P11717; -.
DR MaxQB; P11717; -.
DR PaxDb; P11717; -.
DR PeptideAtlas; P11717; -.
DR PRIDE; P11717; -.
DR ProteomicsDB; 52802; -.
DR Antibodypedia; 1396; 721 antibodies from 42 providers.
DR DNASU; 3482; -.
DR Ensembl; ENST00000356956.6; ENSP00000349437.1; ENSG00000197081.16.
DR GeneID; 3482; -.
DR KEGG; hsa:3482; -.
DR MANE-Select; ENST00000356956.6; ENSP00000349437.1; NM_000876.4; NP_000867.3.
DR UCSC; uc003qta.4; human.
DR CTD; 3482; -.
DR DisGeNET; 3482; -.
DR GeneCards; IGF2R; -.
DR HGNC; HGNC:5467; IGF2R.
DR HPA; ENSG00000197081; Tissue enhanced (skeletal).
DR MalaCards; IGF2R; -.
DR MIM; 147280; gene.
DR neXtProt; NX_P11717; -.
DR OpenTargets; ENSG00000197081; -.
DR PharmGKB; PA29701; -.
DR VEuPathDB; HostDB:ENSG00000197081; -.
DR eggNOG; KOG4504; Eukaryota.
DR GeneTree; ENSGT00390000013943; -.
DR HOGENOM; CLU_001182_0_0_1; -.
DR InParanoid; P11717; -.
DR OMA; MIQLNYK; -.
DR OrthoDB; 290124at2759; -.
DR PhylomeDB; P11717; -.
DR TreeFam; TF328963; -.
DR PathwayCommons; P11717; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P11717; -.
DR SIGNOR; P11717; -.
DR BioGRID-ORCS; 3482; 19 hits in 1091 CRISPR screens.
DR ChiTaRS; IGF2R; human.
DR EvolutionaryTrace; P11717; -.
DR GeneWiki; Insulin-like_growth_factor_2_receptor; -.
DR GenomeRNAi; 3482; -.
DR Pharos; P11717; Tchem.
DR PRO; PR:P11717; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P11717; protein.
DR Bgee; ENSG00000197081; Expressed in stromal cell of endometrium and 193 other tissues.
DR ExpressionAtlas; P11717; baseline and differential.
DR Genevisible; P11717; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030118; C:clathrin coat; IEA:Ensembl.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IMP:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IMP:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005520; F:insulin-like growth factor binding; IBA:GO_Central.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IEA:Ensembl.
DR GO; GO:0005010; F:insulin-like growth factor receptor activity; TAS:ProtInc.
DR GO; GO:0005537; F:mannose binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR GO; GO:1905394; F:retromer complex binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0007041; P:lysosomal transport; IEA:InterPro.
DR GO; GO:0044794; P:positive regulation by host of viral process; IMP:ARUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; 15.
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 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; Lipoprotein; Membrane;
KW Methylation; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:2957598"
FT CHAIN 41..2491
FT /note="Cation-independent mannose-6-phosphate receptor"
FT /id="PRO_0000019229"
FT TOPO_DOM 41..2304
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:2957598"
FT TRANSMEM 2305..2327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2328..2491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2957598"
FT DOMAIN 47..163
FT /note="MRH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 172..320
FT /note="MRH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 326..468
FT /note="MRH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 473..619
FT /note="MRH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 625..762
FT /note="MRH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 765..924
FT /note="MRH 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 932..1079
FT /note="MRH 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1082..1219
FT /note="MRH 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1225..1363
FT /note="MRH 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1367..1508
FT /note="MRH 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1514..1648
FT /note="MRH 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1650..1797
FT /note="MRH 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1802..1989
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 1992..2127
FT /note="MRH 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 2135..2280
FT /note="MRH 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 2424..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2352
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2425
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q07113"
FT MOD_RES 2479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 1312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 77..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 117..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 134..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 174..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 228..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 275..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 288..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 328..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 374..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 420..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 434..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 475..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 531..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 572..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 586..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 627..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 672..679
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 731..760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 767..814
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 823..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 875..910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 893..922
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 934..970
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 976..987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1042..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1084..1125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1134..1142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1177..1205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1190..1217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1227..1262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1270..1282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1319..1349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1333..1361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1369..1408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1420..1427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1461..1494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1476..1506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1516..1553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1559..1566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1598..1634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1614..1646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1652..1695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1706..1713
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1750..1783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1766..1795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1804..1839
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1850..1856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1893..1975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1903..1927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1917..1942
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1957..1987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 1994..2029
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2039..2046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 2082..2113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 2096..2125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262,
FT ECO:0000269|PubMed:18046459"
FT DISULFID 2188..2194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2232..2266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2248..2278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VARIANT 91
FT /note="R -> H (in dbSNP:rs8191704)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021304"
FT VARIANT 203
FT /note="P -> L (in dbSNP:rs8191746)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020470"
FT VARIANT 231
FT /note="G -> D (in dbSNP:rs8191753)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021305"
FT VARIANT 252
FT /note="L -> V (in dbSNP:rs8191754)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020471"
FT VARIANT 273
FT /note="D -> G (in dbSNP:rs8191758)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021306"
FT VARIANT 512
FT /note="K -> Q (in dbSNP:rs8191776)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021307"
FT VARIANT 529
FT /note="R -> Q (in dbSNP:rs6413489)"
FT /id="VAR_020472"
FT VARIANT 604
FT /note="G -> S (in dbSNP:rs8191797)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020473"
FT VARIANT 724
FT /note="A -> T (in dbSNP:rs6413491)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020474"
FT VARIANT 817
FT /note="L -> V (in dbSNP:rs8191808)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021308"
FT VARIANT 856
FT /note="G -> S (in dbSNP:rs8191819)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020475"
FT VARIANT 1107
FT /note="T -> M (in dbSNP:rs8191842)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020476"
FT VARIANT 1124
FT /note="V -> I (in dbSNP:rs8191843)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021309"
FT VARIANT 1184
FT /note="T -> S (in dbSNP:rs8191844)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020477"
FT VARIANT 1254
FT /note="E -> A (in dbSNP:rs2230043)"
FT /id="VAR_050428"
FT VARIANT 1315
FT /note="G -> E (in dbSNP:rs8191859)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021310"
FT VARIANT 1335
FT /note="R -> H (in dbSNP:rs8191860)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021311"
FT VARIANT 1395
FT /note="T -> S (in dbSNP:rs2230048)"
FT /id="VAR_050429"
FT VARIANT 1619
FT /note="R -> G (in dbSNP:rs629849)"
FT /evidence="ECO:0000269|PubMed:2957598,
FT ECO:0000269|PubMed:2963003, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_021312"
FT VARIANT 1696
FT /note="Q -> R (in dbSNP:rs11552587)"
FT /id="VAR_050430"
FT VARIANT 1832
FT /note="R -> H (in dbSNP:rs8191904)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021313"
FT VARIANT 1860
FT /note="G -> D (in dbSNP:rs8191905)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021314"
FT VARIANT 1908
FT /note="I -> M (in dbSNP:rs8191908)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021315"
FT VARIANT 2020
FT /note="N -> S (in dbSNP:rs1805075)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014722"
FT VARIANT 2459
FT /note="A -> V (in dbSNP:rs8191955)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021316"
FT CONFLICT 254
FT /note="L -> V (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="E -> K (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="H -> R (in Ref. 1; CAA68395 and 3; AAF16870)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="V -> A (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1489
FT /note="S -> N (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1703
FT /note="G -> A (in Ref. 1; CAA68395 and 3; AAF16870)"
FT /evidence="ECO:0000305"
FT CONFLICT 2026
FT /note="I -> M (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2075
FT /note="T -> M (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2156
FT /note="K -> N (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2160
FT /note="A -> E (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2176
FT /note="Q -> L (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2330
FT /note="E -> K (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2335
FT /note="V -> M (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2341
FT /note="T -> S (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2410
FT /note="E -> T (in Ref. 2; AAA59866)"
FT /evidence="ECO:0000305"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 273..277
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 444..452
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:6P8I"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 580..586
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:6P8I"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:6P8I"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 632..634
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 676..682
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 688..693
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 704..709
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 725..731
FT /evidence="ECO:0007829|PDB:6V02"
FT TURN 733..737
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 751..756
FT /evidence="ECO:0007829|PDB:6V02"
FT HELIX 757..759
FT /evidence="ECO:0007829|PDB:6V02"
FT STRAND 935..937
FT /evidence="ECO:0007829|PDB:6Z32"
FT TURN 939..941
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 944..946
FT /evidence="ECO:0007829|PDB:6Z32"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 956..959
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 961..967
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 979..982
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 985..989
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1002..1005
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1007..1013
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1019..1029
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1032..1042
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1047..1059
FT /evidence="ECO:0007829|PDB:6Z32"
FT HELIX 1060..1062
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1064..1074
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1085..1087
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:6Z31"
FT HELIX 1097..1099
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1102..1104
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1106..1111
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1116..1122
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1124..1126
FT /evidence="ECO:0007829|PDB:6Z31"
FT TURN 1136..1138
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1139..1145
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1148..1151
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1168..1172
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1175..1177
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1183..1190
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1198..1203
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1206..1213
FT /evidence="ECO:0007829|PDB:6Z31"
FT HELIX 1214..1216
FT /evidence="ECO:0007829|PDB:6Z31"
FT STRAND 1221..1224
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1228..1230
FT /evidence="ECO:0007829|PDB:6Z30"
FT TURN 1232..1234
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1237..1239
FT /evidence="ECO:0007829|PDB:6Z30"
FT HELIX 1241..1244
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1248..1252
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1255..1259
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1279..1285
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1287..1289
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1291..1297
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1303..1305
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1308..1313
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1317..1319
FT /evidence="ECO:0007829|PDB:6Z30"
FT TURN 1320..1322
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1326..1332
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1335..1337
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1341..1345
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1350..1357
FT /evidence="ECO:0007829|PDB:6Z30"
FT HELIX 1358..1360
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1370..1372
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1378..1380
FT /evidence="ECO:0007829|PDB:6Z30"
FT HELIX 1382..1384
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1387..1389
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1402..1405
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1407..1409
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1415..1418
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1425..1433
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1445..1447
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1450..1456
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1464..1467
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1469..1476
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1486..1491
FT /evidence="ECO:0007829|PDB:6Z30"
FT TURN 1492..1494
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1495..1502
FT /evidence="ECO:0007829|PDB:6Z30"
FT HELIX 1503..1505
FT /evidence="ECO:0007829|PDB:6Z30"
FT STRAND 1512..1514
FT /evidence="ECO:0007829|PDB:5IEI"
FT STRAND 1517..1519
FT /evidence="ECO:0007829|PDB:1GP0"
FT TURN 1521..1523
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:1GP0"
FT HELIX 1530..1532
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1533..1536
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1538..1542
FT /evidence="ECO:0007829|PDB:1GP0"
FT TURN 1543..1545
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1546..1550
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1552..1554
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1557..1560
FT /evidence="ECO:0007829|PDB:6Z32"
FT STRAND 1563..1567
FT /evidence="ECO:0007829|PDB:1GP0"
FT TURN 1568..1570
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1573..1576
FT /evidence="ECO:0007829|PDB:5IEI"
FT STRAND 1582..1584
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1587..1592
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1596..1598
FT /evidence="ECO:0007829|PDB:2L2A"
FT STRAND 1599..1601
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1607..1614
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1616..1618
FT /evidence="ECO:0007829|PDB:2L2A"
FT STRAND 1625..1630
FT /evidence="ECO:0007829|PDB:1GP0"
FT TURN 1631..1634
FT /evidence="ECO:0007829|PDB:1GP0"
FT STRAND 1635..1642
FT /evidence="ECO:0007829|PDB:1GP0"
FT HELIX 1643..1645
FT /evidence="ECO:0007829|PDB:1GP0"
FT TURN 1649..1651
FT /evidence="ECO:0007829|PDB:2CNJ"
FT STRAND 1653..1656
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1659..1662
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 1664..1666
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1669..1671
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1673..1675
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1690..1692
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1694..1696
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1711..1714
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1717..1719
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1722..1727
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1732..1734
FT /evidence="ECO:0007829|PDB:2V5N"
FT STRAND 1735..1737
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1743..1745
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1759..1766
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1775..1777
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1781..1783
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1784..1791
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 1792..1794
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1801..1804
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1805..1807
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1809..1811
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1814..1816
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 1818..1821
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1825..1829
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1832..1836
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1838..1840
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1845..1847
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1850..1858
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1863..1876
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1878..1880
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1883..1888
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1905..1909
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1912..1916
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1920..1924
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1926..1932
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 1933..1936
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1939..1943
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1950..1957
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1967..1972
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 1973..1975
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1976..1984
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 1995..2000
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2002..2004
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 2005..2007
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2011..2013
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2015..2019
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2022..2026
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2043..2048
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2054..2059
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 2060..2062
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2064..2068
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2071..2076
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2089..2096
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2098..2109
FT /evidence="ECO:0007829|PDB:2V5O"
FT TURN 2110..2113
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2114..2121
FT /evidence="ECO:0007829|PDB:2V5O"
FT HELIX 2122..2124
FT /evidence="ECO:0007829|PDB:2V5O"
FT STRAND 2350..2355
FT /evidence="ECO:0007829|PDB:6N5X"
FT STRAND 2368..2373
FT /evidence="ECO:0007829|PDB:6N5X"
SQ SEQUENCE 2491 AA; 274375 MW; 3841ADE559B48057 CRC64;
MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS YTWEAVDTKN
NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV LRSATRSLLE FNTTVSCDQQ
GTNHRVQSSI AFLCGKTLGT PEFVTATECV HYFEWRTTAA CKKDIFKANK EVPCYVFDEE
LRKHDLNPLI KLSGAYLVDD SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH
QAFDVGQPRD GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL
TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS SYISDGKEYL
FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN QTLRYSDGDL TLIYFGGDEC
SSGFQRMSVI NFECNKTAGN DGKGTPVFTG EVDCTYFFTW DTEYACVKEK EDLLCGATDG
KKRYDLSALV RHAEPEQNWE AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV
DKNGSKNLGK FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS
GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY KVETKKYDFY
INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY YDGMIQLNYR GGTPYNNERH
TPRATLITFL CDRDAGVGFP EYQEEDNSTY NFRWYTSYAC PEEPLECVVT DPSTLEQYDL
SSLAKSEGGL GGNWYAMDNS GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS
FTEVVSISNL GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS
HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL NSSQGYNVSG
IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK PARPVGIEKS LQLSTEGFIT
LTYKGPLSAK GTADAFIVRF VCNDDVYSGP LKFLHQDIDS GQGIRNTYFE FETALACVPS
PVDCQVTDLA GNEYDLTGLS TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG
SCLVSEGNSW NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ
LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV SAGEYTYYFR
VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ KLTYENGLLK MNFTGGDTCH
KVYQRSTAIF FYCDRGTQRP VFLKETSDCS YLFEWRTQYA CPPFDLTECS FKDGAGNSFD
LSSLSRYSDN WEAITGTGDP EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV
RDGPQWRDGI IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW
PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM SICGENENCP
PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS KSGLSYKSVI SFVCRPEARP
TNRPMLISLD KQTCTLFFSW HTPLACEQAT ECSVRNGSSI VDLSPLIHRT GGYEAYDESE
DDASDTNPDF YINICQPLNP MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI
YLNFESSTPC LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR
MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC KDGGVCLLSG
TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG VPCVFPFIFN GKSYEECIIE
SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT SSIIFKCDED EDIGRPQVFS EVRGCDVTFE
WKTKVVCPPK KLECKFVQKH KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS
ERASICRRTT TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV
GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL GDIYFKLFRA
SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND QHFSRKVGTS DKTKYYLQDG
DLDVVFASSS KCGKDKTKSV SSTIFFHCDP LVEDGIPEFS HETADCQYLF SWYTSAVCPL
GVGFDSENPG DDGQMHKGLS ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT
TCCRRSSNVS YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS
SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR VGLVRGEKAR
KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I
