IGF2_HUMAN
ID IGF2_HUMAN Reviewed; 180 AA.
AC P01344; B3KX48; B7WP08; C9JAF2; E3UN45; P78449; Q14299; Q1WM26; Q9UC68;
AC Q9UC69;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 252.
DE RecName: Full=Insulin-like growth factor II;
DE Short=IGF-II;
DE AltName: Full=Somatomedin-A;
DE AltName: Full=T3M-11-derived growth factor;
DE Contains:
DE RecName: Full=Insulin-like growth factor II;
DE Contains:
DE RecName: Full=Insulin-like growth factor II Ala-25 Del;
DE Contains:
DE RecName: Full=Preptin;
DE Flags: Precursor;
GN Name=IGF2; ORFNames=PP1446;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=6382022; DOI=10.1038/310777a0;
RA Dull T.J., Gray A., Hayflick J.S., Ullrich A.;
RT "Insulin-like growth factor II precursor gene organization in relation to
RT insulin gene family.";
RL Nature 310:777-781(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MISCELLANEOUS.
RX PubMed=6382021; DOI=10.1038/310775a0;
RA Bell G.I., Merryweather J.P., Sanchez-Pescador R., Stempien M.M.,
RA Priestley L., Scott J., Rall L.B.;
RT "Sequence of a cDNA clone encoding human preproinsulin-like growth factor
RT II.";
RL Nature 310:775-777(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2450353; DOI=10.1073/pnas.85.6.1947;
RA Shen S.-J., Daimon M., Wang C.-Y., Jansen M., Ilan J.;
RT "Isolation of an insulin-like growth factor II cDNA with a unique 5'
RT untranslated region from human placenta.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1947-1951(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=3002851; DOI=10.1016/0014-5793(86)80156-9;
RA de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M.,
RA van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.;
RT "Organization of the human genes for insulin-like growth factors I and
RT II.";
RL FEBS Lett. 195:179-184(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3476948; DOI=10.1073/pnas.84.18.6330;
RA Irminger J.C., Rosen K.M., Humbel R.E., Villa-Komaroff L.;
RT "Tissue-specific expression of insulin-like growth factor II mRNAs with
RT distinct 5' untranslated regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6330-6334(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3683205; DOI=10.1016/s0076-6879(87)46026-6;
RA Rall L.B., Scott J., Bell G.I.;
RT "Human insulin-like growth factor I and II messenger RNA: isolation of
RT complementary DNA and analysis of expression.";
RL Methods Enzymol. 146:239-248(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=3881277; DOI=10.1016/0014-5793(85)80527-5;
RA Jansen M., van Schaik F.M.A., van Tol H., van den Brande J.L.,
RA Sussenbach J.S.;
RT "Nucleotide sequences of cDNAs encoding precursors of human insulin-like
RT growth factor II (IGF-II) and an IGF-II variant.";
RL FEBS Lett. 179:243-246(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7730145; DOI=10.1111/j.1349-7006.1995.tb03040.x;
RA Hagiwara K., Kobayashi T., Tobita M., Kikyo N., Yazaki Y., Okabe T.;
RT "Isolation of a cDNA for a growth factor of vascular endothelial cells from
RT human lung cancer cells: its identity with insulin-like growth factor II.";
RL Jpn. J. Cancer Res. 86:202-207(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16531418; DOI=10.1093/hmg/ddl041;
RA Monk D., Sanches R., Arnaud P., Apostolidou S., Hills F.A., Abu-Amero S.,
RA Murrell A., Friess H., Reik W., Stanier P., Constancia M., Moore G.E.;
RT "Imprinting of IGF2 P0 transcript and novel alternatively spliced INS-IGF2
RT isoforms show differences between mouse and human.";
RL Hum. Mol. Genet. 15:1259-1269(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-165 (ISOFORM 3), AND ALTERNATIVE SPLICING.
RX PubMed=20842449; DOI=10.1007/s11033-010-0259-z;
RA Li J., Neumann I., Volkmer I., Staege M.S.;
RT "Down-regulation of achaete-scute complex homolog 1 (ASCL1) in
RT neuroblastoma cells induces up-regulation of insulin-like growth factor 2
RT (IGF2).";
RL Mol. Biol. Rep. 38:1515-1521(2011).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-180.
RX PubMed=3167054; DOI=10.1016/0167-4781(88)90124-8;
RA de Pagter-Holthuizen P., van der Kammen R.A., Jansen M., van Schaik F.M.A.,
RA Sussenbach J.S.;
RT "Differential expression of the human insulin-like growth factor II gene.
RT Characterization of the IGF-II mRNAs and an mRNA encoding a putative IGF-
RT II-associated protein.";
RL Biochim. Biophys. Acta 950:282-295(1988).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-161 (ISOFORM 2).
RX PubMed=3653397; DOI=10.1016/0014-5793(87)80216-8;
RA le Bouc Y., Noguiez P., Sondermeijer P., Dreyer D., Girard F., Binoux M.;
RT "A new 5'-non-coding region for human placental insulin-like growth factor
RT II mRNA expression.";
RL FEBS Lett. 222:181-185(1987).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC TISSUE=Liver;
RX PubMed=3652904; DOI=10.1089/dna.1987.6.283;
RA Gray A., Tam A.W., Dull T.J., Hayflick J.S., Pintar J., Cavenee W.K.,
RA Koufos A., Ullrich A.;
RT "Tissue-specific and developmentally regulated transcription of the
RT insulin-like growth factor 2 gene.";
RL DNA 6:283-295(1987).
RN [21]
RP PROTEIN SEQUENCE OF 25-91.
RX PubMed=658418; DOI=10.1016/0014-5793(78)80237-3;
RA Rinderknecht E., Humbel R.E.;
RT "Primary structure of human insulin-like growth factor II.";
RL FEBS Lett. 89:283-286(1978).
RN [22]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=2722836; DOI=10.1016/s0021-9258(18)60533-2;
RA Smith M.C., Cook J.A., Furman T.C., Occolowitz J.L.;
RT "Structure and activity dependence of recombinant human insulin-like growth
RT factor II on disulfide bond pairing.";
RL J. Biol. Chem. 264:9314-9321(1989).
RN [23]
RP PROTEIN SEQUENCE OF 25-68.
RX PubMed=7633596; DOI=10.1016/0378-4347(94)00576-q;
RA De Ceuninck F., Willeput J., Corvol M.;
RT "Purification and characterization of insulin-like growth factor II (IGF
RT II) and an IGF II variant from human placenta.";
RL J. Chromatogr. B 666:203-214(1995).
RN [24]
RP GLYCOSYLATION AT THR-99.
RX PubMed=1569071; DOI=10.1016/s0021-9258(18)42420-9;
RA Hudgins W.R., Hampton B., Burgess W.H., Perdue J.F.;
RT "The identification of O-glycosylated precursors of insulin-like growth
RT factor II.";
RL J. Biol. Chem. 267:8153-8160(1992).
RN [25]
RP POLYMORPHISM, AND ASSOCIATION WITH BODY MASS INDEX.
RX PubMed=11448941; DOI=10.1093/hmg/10.14.1491;
RA Gaunt T.R., Cooper J.A., Miller G.J., Day I.N.M., O'Dell S.D.;
RT "Positive associations between single nucleotide polymorphisms in the IGF2
RT gene region and body mass index in adult males.";
RL Hum. Mol. Genet. 10:1491-1501(2001).
RN [26]
RP MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
RX PubMed=12586351; DOI=10.1016/s0014-5793(03)00042-5;
RA Nedelkov D., Nelson R.W., Kiernan U.A., Niederkofler E.E., Tubbs K.A.;
RT "Detection of bound and free IGF-1 and IGF-2 in human plasma via
RT biomolecular interaction analysis mass spectrometry.";
RL FEBS Lett. 536:130-134(2003).
RN [27]
RP MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
RX PubMed=15359740; DOI=10.1021/pr0499388;
RA Nelson R.W., Nedelkov D., Tubbs K.A., Kiernan U.A.;
RT "Quantitative mass spectrometric immunoassay of insulin like growth factor
RT 1.";
RL J. Proteome Res. 3:851-855(2004).
RN [28]
RP PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS
RP OF ARG-92; LYS-112 AND ARG-128, AND GLYCOSYLATION.
RX PubMed=16040806; DOI=10.1073/pnas.0502357102;
RA Qiu Q., Basak A., Mbikay M., Tsang B.K., Gruslin A.;
RT "Role of pro-IGF-II processing by proprotein convertase 4 in human
RT placental development.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11047-11052(2005).
RN [29]
RP OSTEOGENIC FUNCTION OF PREPTIN.
RX PubMed=16912056; DOI=10.1152/ajpendo.00642.2005;
RA Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M., Chan V.A.,
RA Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.;
RT "Preptin, another peptide product of the pancreatic beta-cell, is
RT osteogenic in vitro and in vivo.";
RL Am. J. Physiol. 292:E117-E122(2007).
RN [30]
RP INVOLVEMENT IN SRS1.
RX PubMed=19066168; DOI=10.1136/jmg.2008.061820;
RA Bartholdi D., Krajewska-Walasek M., Ounap K., Gaspar H., Chrzanowska K.H.,
RA Ilyana H., Kayserili H., Lurie I.W., Schinzel A., Baumer A.;
RT "Epigenetic mutations of the imprinted IGF2-H19 domain in Silver-Russell
RT syndrome (SRS): results from a large cohort of patients with SRS and SRS-
RT like phenotypes.";
RL J. Med. Genet. 46:192-197(2009).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-163, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [32]
RP GLYCOSYLATION AT THR-96; THR-99 AND THR-163, STRUCTURE OF CARBOHYDRATES,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [33]
RP GLYCOSYLATION AT THR-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [34]
RP REVIEW OF FUNCTION.
RX PubMed=24593700; DOI=10.1111/cen.12446;
RA Livingstone C., Borai A.;
RT "Insulin-like growth factor-II: its role in metabolic and endocrine
RT disease.";
RL Clin. Endocrinol. (Oxf.) 80:773-781(2014).
RN [35]
RP INVOLVEMENT IN SRS3.
RX PubMed=26154720; DOI=10.1056/nejmoa1415227;
RA Begemann M., Zirn B., Santen G., Wirthgen E., Soellner L., Buettel H.M.,
RA Schweizer R., van Workum W., Binder G., Eggermann T.;
RT "Paternally inherited IGF2 mutation and growth restriction.";
RL N. Engl. J. Med. 373:349-356(2015).
RN [36]
RP FUNCTION, INTERACTION WITH INTEGRINS ITGAV:ITGB3 AND ITGA6:ITGB4, SITES
RP IMPORTANT FOR INTEGRIN BINDING, AND MUTAGENESIS OF ARG-48; ARG-58; ARG-61;
RP ARG-62 AND ARG-64.
RX PubMed=28873464; DOI=10.1371/journal.pone.0184285;
RA Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K., Takada Y.;
RT "Direct integrin binding to insulin-like growth factor-2 through the C-
RT domain is required for insulin-like growth factor receptor type 1 (IGF1R)
RT signaling.";
RL PLoS ONE 12:E0184285-E0184285(2017).
RN [37]
RP 3D-STRUCTURE MODELING.
RX PubMed=6189745;
RA Blundell T.L., Bedarkar S., Humbel R.E.;
RT "Tertiary structures, receptor binding, and antigenicity of insulinlike
RT growth factors.";
RL Fed. Proc. 42:2592-2597(1983).
RN [38]
RP STRUCTURE BY NMR.
RX PubMed=7527339; DOI=10.1002/j.1460-2075.1994.tb06896.x;
RA Terasawa H., Kohda D., Hatanaka H., Nagata K., Higashihashi N.,
RA Fujiwara H., Sakano K., Inagaki F.;
RT "Solution structure of human insulin-like growth factor II; recognition
RT sites for receptors and binding proteins.";
RL EMBO J. 13:5590-5597(1994).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 25-91 IN COMPLEX WITH IGF2R, AND
RP DISULFIDE BONDS.
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).
RN [40]
RP VARIANT SRS3 26-TYR--LYS-180 DEL.
RX PubMed=28796236; DOI=10.1038/gim.2017.105;
RA Abi Habib W., Brioude F., Edouard T., Bennett J.T., Lienhardt-Roussie A.,
RA Tixier F., Salem J., Yuen T., Azzi S., Le Bouc Y., Harbison M.D.,
RA Netchine I.;
RT "Genetic disruption of the oncogenic HMGA2-PLAG1-IGF2 pathway causes fetal
RT growth restriction.";
RL Genet. Med. 20:250-258(2018).
CC -!- FUNCTION: The insulin-like growth factors possess growth-promoting
CC activity (By similarity). Major fetal growth hormone in mammals. Plays
CC a key role in regulating fetoplacental development. IGF2 is influenced
CC by placental lactogen. Also involved in tissue differentiation. In
CC adults, involved in glucose metabolism in adipose tissue, skeletal
CC muscle and liver (Probable). Acts as a ligand for integrin which is
CC required for IGF2 signaling (PubMed:28873464). Positively regulates
CC myogenic transcription factor MYOD1 function by facilitating the
CC recruitment of transcriptional coactivators, thereby controlling muscle
CC terminal differentiation (By similarity). Inhibits myoblast
CC differentiation and modulates metabolism via increasing the
CC mitochondrial respiration rate (By similarity).
CC {ECO:0000250|UniProtKB:P09535, ECO:0000269|PubMed:28873464,
CC ECO:0000305|PubMed:24593700}.
CC -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin,
CC and acts as physiological amplifier of glucose-mediated insulin
CC secretion. Exhibits osteogenic properties by increasing osteoblast
CC mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
CC {ECO:0000269|PubMed:16912056}.
CC -!- SUBUNIT: Interacts with MYORG; this interaction is required for IGF2
CC secretion (By similarity). Interacts with integrins ITGAV:ITGB3 and
CC ITGA6:ITGB4; integrin-binding is required for IGF2 signaling
CC (PubMed:28873464). {ECO:0000250|UniProtKB:P09535,
CC ECO:0000269|PubMed:28873464}.
CC -!- INTERACTION:
CC P01344; P11717: IGF2R; NbExp=17; IntAct=EBI-7178764, EBI-1048580;
CC P01344; Q93062: RBPMS; NbExp=3; IntAct=EBI-7178764, EBI-740322;
CC P01344-1; P11717: IGF2R; NbExp=2; IntAct=EBI-15658078, EBI-1048580;
CC P01344-3; A0A024R644: CLN5; NbExp=3; IntAct=EBI-13334485, EBI-12838990;
CC P01344-3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-13334485, EBI-13345167;
CC P01344-3; P22692: IGFBP4; NbExp=4; IntAct=EBI-13334485, EBI-2831948;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16040806}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P01344-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01344-2; Sequence=VSP_002708;
CC Name=3;
CC IsoId=P01344-3; Sequence=VSP_045624;
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, muscle,
CC kidney, tongue, limb, eye and pancreas. {ECO:0000269|PubMed:16531418}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, detected in liver, lung,
CC skeletal muscle and placenta. {ECO:0000269|PubMed:16531418}.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 is a
CC minor glycosylation site compared to Thr-99.
CC {ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:19838169,
CC ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360}.
CC -!- PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128
CC and Arg-92 to generate big-IGF2 and mature IGF2.
CC {ECO:0000269|PubMed:16040806}.
CC -!- MASS SPECTROMETRY: [Insulin-like growth factor II]: Mass=7469.4;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:12586351,
CC ECO:0000269|PubMed:15359740};
CC -!- MASS SPECTROMETRY: [Insulin-like growth factor II Ala-25 Del]:
CC Mass=7398.3; Method=MALDI; Evidence={ECO:0000269|PubMed:12586351,
CC ECO:0000269|PubMed:15359740};
CC -!- POLYMORPHISM: Genetic variations in IGF2 are associated with body mass
CC index (BMI). The BMI is a statistical measurement which compares a
CC person's weight and height. {ECO:0000269|PubMed:11448941}.
CC -!- DISEASE: Silver-Russell syndrome 1 (SRS1) [MIM:180860]: A form of
CC Silver-Russell syndrome, a clinically heterogeneous condition
CC characterized by severe intrauterine growth retardation, poor postnatal
CC growth, craniofacial features such as a triangular shaped face and a
CC broad forehead, body asymmetry, and a variety of minor malformations.
CC The phenotypic expression changes during childhood and adolescence,
CC with the facial features and asymmetry usually becoming more subtle
CC with age. SRS1 is caused by epigenetic changes of DNA hypomethylation
CC at the telomeric imprinting control region (ICR1) on chromosome 11p15,
CC involving the H19 and IGF2 genes. {ECO:0000269|PubMed:19066168}.
CC Note=The gene represented in this entry is involved in disease
CC pathogenesis.
CC -!- DISEASE: Silver-Russell syndrome 3 (SRS3) [MIM:616489]: A form of
CC Silver-Russell syndrome, a clinically heterogeneous condition
CC characterized by severe intrauterine growth retardation, poor postnatal
CC growth, craniofacial features such as a triangular shaped face and a
CC broad forehead, body asymmetry, and a variety of minor malformations.
CC The phenotypic expression changes during childhood and adolescence,
CC with the facial features and asymmetry usually becoming more subtle
CC with age. SRS3 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:26154720, ECO:0000269|PubMed:28796236}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The IGF2 locus is imprinted. Paternal inherited gene is
CC expressed, while the maternal inherited gene is imprinted, hence
CC silenced. Transcripts from 5 promoters P0, P1, P2, P3 and P4 code for
CC the same protein but are differentially regulated in a developmental
CC stage and tissue specificity. {ECO:0000305|PubMed:16531418}.
CC -!- MISCELLANEOUS: [Isoform 1]: Product of 5 different transcripts
CC regulated by 5 different promoters, denominated P0, P1, P2, P3 and P4.
CC {ECO:0000305|PubMed:16531418}.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Insulin-like growth factor 2 entry;
CC URL="https://en.wikipedia.org/wiki/Insulin-like_growth_factor_2";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/igf2/";
CC ---------------------------------------------------------------------------
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DR EMBL; X03562; CAA27249.1; -; Genomic_DNA.
DR EMBL; X00910; CAA25426.1; -; mRNA.
DR EMBL; J03242; AAA52545.1; -; mRNA.
DR EMBL; X03425; CAA27155.1; -; Genomic_DNA.
DR EMBL; X03426; CAA27156.1; -; Genomic_DNA.
DR EMBL; X03427; CAA27157.1; -; Genomic_DNA.
DR EMBL; M17426; AAA60088.1; -; mRNA.
DR EMBL; M29645; AAA52544.1; -; mRNA.
DR EMBL; M17863; AAA52443.1; ALT_SEQ; mRNA.
DR EMBL; S77035; AAB34155.1; -; mRNA.
DR EMBL; DQ104203; ABD93451.1; -; mRNA.
DR EMBL; HM481219; ADO21454.1; -; mRNA.
DR EMBL; AF217977; AAG17220.1; -; mRNA.
DR EMBL; BT007013; AAP35659.1; -; mRNA.
DR EMBL; AF517226; AAM51825.1; -; Genomic_DNA.
DR EMBL; AC132217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK126688; BAG54360.1; -; mRNA.
DR EMBL; CH471158; EAX02485.1; -; Genomic_DNA.
DR EMBL; BC000531; AAH00531.1; -; mRNA.
DR EMBL; X07868; CAA30717.1; -; Genomic_DNA.
DR EMBL; X06159; CAA29516.1; -; mRNA.
DR EMBL; X06160; CAA29517.1; -; Transcribed_RNA.
DR EMBL; X06161; CAA29518.1; -; mRNA.
DR EMBL; M22373; AAA52536.1; -; Genomic_DNA.
DR CCDS; CCDS44517.1; -. [P01344-3]
DR CCDS; CCDS7728.1; -. [P01344-1]
DR PIR; B23614; IGHU2.
DR PIR; I67610; I67610.
DR PIR; S02423; S02423.
DR RefSeq; NP_000603.1; NM_000612.5. [P01344-1]
DR RefSeq; NP_001007140.2; NM_001007139.5. [P01344-1]
DR RefSeq; NP_001121070.1; NM_001127598.2. [P01344-3]
DR RefSeq; NP_001278790.1; NM_001291861.2. [P01344-1]
DR RefSeq; NP_001278791.1; NM_001291862.2. [P01344-1]
DR PDB; 1IGL; NMR; -; A=25-91.
DR PDB; 2L29; NMR; -; B=25-91.
DR PDB; 2V5P; X-ray; 4.10 A; C/D=25-91.
DR PDB; 3E4Z; X-ray; 2.28 A; C/D=25-91.
DR PDB; 3KR3; X-ray; 2.20 A; D=25-91.
DR PDB; 5L3L; NMR; -; A=25-91.
DR PDB; 5L3M; NMR; -; A=25-91.
DR PDB; 5L3N; NMR; -; A=25-91.
DR PDB; 6UM2; EM; 4.32 A; B=25-91.
DR PDB; 6VWG; EM; 3.21 A; I=25-91.
DR PDB; 6VWI; EM; 3.70 A; I=25-91.
DR PDBsum; 1IGL; -.
DR PDBsum; 2L29; -.
DR PDBsum; 2V5P; -.
DR PDBsum; 3E4Z; -.
DR PDBsum; 3KR3; -.
DR PDBsum; 5L3L; -.
DR PDBsum; 5L3M; -.
DR PDBsum; 5L3N; -.
DR PDBsum; 6UM2; -.
DR PDBsum; 6VWG; -.
DR PDBsum; 6VWI; -.
DR AlphaFoldDB; P01344; -.
DR BMRB; P01344; -.
DR SMR; P01344; -.
DR BioGRID; 109702; 35.
DR CORUM; P01344; -.
DR DIP; DIP-29508N; -.
DR IntAct; P01344; 11.
DR MINT; P01344; -.
DR STRING; 9606.ENSP00000391826; -.
DR ChEMBL; CHEMBL3712957; -.
DR GlyConnect; 760; 9 O-Linked glycans (4 sites).
DR GlyGen; P01344; 4 sites, 9 O-linked glycans (4 sites).
DR iPTMnet; P01344; -.
DR PhosphoSitePlus; P01344; -.
DR BioMuta; IGF2; -.
DR DMDM; 124255; -.
DR jPOST; P01344; -.
DR MassIVE; P01344; -.
DR MaxQB; P01344; -.
DR PaxDb; P01344; -.
DR PeptideAtlas; P01344; -.
DR PRIDE; P01344; -.
DR ProteomicsDB; 51375; -. [P01344-1]
DR ProteomicsDB; 51376; -. [P01344-2]
DR ProteomicsDB; 9318; -.
DR ABCD; P01344; 7 sequenced antibodies.
DR Antibodypedia; 1027; 606 antibodies from 40 providers.
DR DNASU; 3481; -.
DR Ensembl; ENST00000381389.5; ENSP00000370796.1; ENSG00000167244.21. [P01344-1]
DR Ensembl; ENST00000381392.5; ENSP00000370799.1; ENSG00000167244.21. [P01344-2]
DR Ensembl; ENST00000381395.5; ENSP00000370802.1; ENSG00000167244.21. [P01344-1]
DR Ensembl; ENST00000381406.8; ENSP00000370813.4; ENSG00000167244.21. [P01344-2]
DR Ensembl; ENST00000416167.7; ENSP00000414497.2; ENSG00000167244.21. [P01344-1]
DR Ensembl; ENST00000418738.2; ENSP00000402047.2; ENSG00000167244.21. [P01344-1]
DR Ensembl; ENST00000434045.6; ENSP00000391826.2; ENSG00000167244.21. [P01344-3]
DR GeneID; 3481; -.
DR KEGG; hsa:3481; -.
DR MANE-Select; ENST00000416167.7; ENSP00000414497.2; NM_000612.6; NP_000603.1.
DR UCSC; uc001lvf.4; human. [P01344-1]
DR CTD; 3481; -.
DR DisGeNET; 3481; -.
DR GeneCards; IGF2; -.
DR GeneReviews; IGF2; -.
DR HGNC; HGNC:5466; IGF2.
DR HPA; ENSG00000167244; Tissue enriched (placenta).
DR MalaCards; IGF2; -.
DR MIM; 147470; gene.
DR MIM; 180860; phenotype.
DR MIM; 616489; phenotype.
DR neXtProt; NX_P01344; -.
DR OpenTargets; ENSG00000167244; -.
DR Orphanet; 231117; Beckwith-Wiedemann syndrome due to imprinting defect of 11p15.
DR Orphanet; 2128; Isolated hemihyperplasia.
DR Orphanet; 231144; Silver-Russell syndrome due to 11p15 microduplication.
DR Orphanet; 397590; Silver-Russell syndrome due to a point mutation.
DR Orphanet; 231140; Silver-Russell syndrome due to an imprinting defect of 11p15.
DR PharmGKB; PA29699; -.
DR VEuPathDB; HostDB:ENSG00000167244; -.
DR eggNOG; ENOG502S0I0; Eukaryota.
DR GeneTree; ENSGT00940000160745; -.
DR HOGENOM; CLU_092464_1_0_1; -.
DR InParanoid; P01344; -.
DR OMA; PSHAKYS; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P01344; -.
DR TreeFam; TF332820; -.
DR PathwayCommons; P01344; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
DR Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R.
DR Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR SignaLink; P01344; -.
DR SIGNOR; P01344; -.
DR BioGRID-ORCS; 3481; 10 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; P01344; -.
DR GeneWiki; Insulin-like_growth_factor_2; -.
DR GenomeRNAi; 3481; -.
DR Pharos; P01344; Tbio.
DR PRO; PR:P01344; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P01344; protein.
DR Bgee; ENSG00000167244; Expressed in adrenal tissue and 96 other tissues.
DR Genevisible; P01344; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; IPI:BHF-UCL.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IMP:AgBase.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; ISS:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; ISS:UniProtKB.
DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:BHF-UCL.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:BHF-UCL.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:BHF-UCL.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:BHF-UCL.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046622; P:positive regulation of organ growth; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:BHF-UCL.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IBA:GO_Central.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; TAS:ProtInc.
DR GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
DR GO; GO:0060720; P:spongiotrophoblast cell proliferation; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR InterPro; IPR022334; IGF2.
DR InterPro; IPR013576; IGF2_C.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR022350; Insulin-like_growth_factor.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR Pfam; PF08365; IGF2_C; 1.
DR Pfam; PF00049; Insulin; 2.
DR PRINTS; PR02002; INSLNLIKEGF.
DR PRINTS; PR02006; INSLNLIKEGF2.
DR PRINTS; PR00276; INSULINFAMLY.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; Disulfide bond; Dwarfism; Glucose metabolism;
KW Glycoprotein; Growth factor; Hormone; Mitogen; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:658418,
FT ECO:0000269|PubMed:7633596"
FT CHAIN 25..91
FT /note="Insulin-like growth factor II"
FT /id="PRO_0000015717"
FT CHAIN 26..91
FT /note="Insulin-like growth factor II Ala-25 Del"
FT /id="PRO_0000015718"
FT PROPEP 92..180
FT /note="E peptide"
FT /id="PRO_0000015719"
FT PEPTIDE 93..126
FT /note="Preptin"
FT /id="PRO_0000370376"
FT REGION 25..52
FT /note="B"
FT REGION 53..64
FT /note="C"
FT REGION 65..85
FT /note="A"
FT REGION 86..91
FT /note="D"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 48
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:28873464"
FT SITE 58
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:28873464"
FT SITE 61
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:28873464"
FT SITE 62
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:28873464"
FT CARBOHYD 96
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320,
FT ECO:0000269|PubMed:23234360"
FT CARBOHYD 99
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1569071,
FT ECO:0000269|PubMed:22171320"
FT CARBOHYD 163
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:22171320"
FT DISULFID 33..71
FT /evidence="ECO:0000269|PubMed:2722836"
FT DISULFID 45..84
FT /evidence="ECO:0000269|PubMed:2722836"
FT DISULFID 70..75
FT /evidence="ECO:0000269|PubMed:2722836"
FT VAR_SEQ 1
FT /note="M -> MVSPDPQIIVVAPETELASMQVQRTEDGVTIIQIFWVGRKGELLRRT
FT PVSSAMQTPM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:20842449"
FT /id="VSP_045624"
FT VAR_SEQ 53
FT /note="S -> RLPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3653397,
FT ECO:0000303|PubMed:3881277"
FT /id="VSP_002708"
FT VARIANT 26..180
FT /note="Missing (in SRS3)"
FT /evidence="ECO:0000269|PubMed:28796236"
FT /id="VAR_084336"
FT VARIANT 120
FT /note="K -> N (in dbSNP:rs14367)"
FT /id="VAR_011959"
FT VARIANT 173
FT /note="P -> Q (in dbSNP:rs1050342)"
FT /id="VAR_011960"
FT VARIANT 180
FT /note="K -> N (in dbSNP:rs12993)"
FT /id="VAR_011961"
FT MUTAGEN 48
FT /note="R->E: Does not affect integrin binding. Defective
FT integrin binding and IGF2 signaling; when associated with
FT E-58; E-61 and E-62."
FT /evidence="ECO:0000269|PubMed:28873464"
FT MUTAGEN 58
FT /note="R->E: Does not affect integrin binding. Defective
FT integrin binding and IGF2 signaling; when associated with
FT E-48; E-61 and E-62."
FT /evidence="ECO:0000269|PubMed:28873464"
FT MUTAGEN 61
FT /note="R->E: Does not affect integrin binding. Defective
FT integrin binding and IGF2 signaling; when associated with
FT E-48; E-58 and E-62."
FT /evidence="ECO:0000269|PubMed:28873464"
FT MUTAGEN 62
FT /note="R->E: Does not affect integrin binding. Defective
FT integrin binding and IGF2 signaling; when associated with
FT E-48; E-58 and E-61."
FT /evidence="ECO:0000269|PubMed:28873464"
FT MUTAGEN 64
FT /note="R->E: Slight but significant increase in integrin
FT binding."
FT /evidence="ECO:0000269|PubMed:28873464"
FT MUTAGEN 92
FT /note="R->A: Decreases mature IGF2 levels."
FT /evidence="ECO:0000269|PubMed:16040806"
FT MUTAGEN 112
FT /note="K->A: No effect in proteolytical processing."
FT /evidence="ECO:0000269|PubMed:16040806"
FT MUTAGEN 128
FT /note="R->A: Abolishes proteolytical processing."
FT /evidence="ECO:0000269|PubMed:16040806"
FT CONFLICT 3
FT /note="I -> M (in Ref. 6; AAA52544)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..110
FT /note="RYPV -> EIPL (in Ref. 1; CAA27249)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="E -> ELE (in Ref. 5; AAA60088)"
FT /evidence="ECO:0000305"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3KR3"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3KR3"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3KR3"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3KR3"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3KR3"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:3KR3"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1IGL"
SQ SEQUENCE 180 AA; 20140 MW; C1B0EB1E016BA37A CRC64;
MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFSRPASRVS
RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTPPTV LPDNFPRYPV GKFFQYDTWK
QSTQRLRRGL PALLRARRGH VLAKELEAFR EAKRHRPLIA LPTQDPAHGG APPEMASNRK
