ID A3E108_MONDO Unreviewed; 186 AA. AC A3E108; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Insulin-like growth factor II {ECO:0000256|ARBA:ARBA00018566}; GN Name=IGF2 {ECO:0000313|EMBL:ABG22162.1}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|EMBL:ABG22162.1}; RN [1] {ECO:0000313|EMBL:ABG22162.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17268191; DOI=10.1159/000097431; RA Lawton B.R., Obergfell C., O'Neill R.J., O'Neill M.J.; RT "Physical mapping of the IGF2 locus in the South American opossum RT Monodelphis domestica."; RL Cytogenet. Genome Res. 116:130-131(2007). CC -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin, CC and acts as a 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:0000256|ARBA:ARBA00043916}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU000406}. CC -!- SIMILARITY: Belongs to the insulin family. CC {ECO:0000256|ARBA:ARBA00009034, ECO:0000256|RuleBase:RU000406}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ519591; ABG22162.1; -; Genomic_DNA. DR AlphaFoldDB; A3E108; -. DR GO; GO:0005615; C:extracellular space; IEA:InterPro. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0005179; F:hormone activity; IEA:InterPro. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR CDD; cd04368; IlGF; 1. DR Gene3D; 1.10.100.10; Insulin-like; 1. 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 PANTHER; PTHR46886; INSULIN-LIKE GROWTH FACTOR II; 1. DR PANTHER; PTHR46886:SF1; INSULIN-LIKE GROWTH FACTOR II; 1. DR Pfam; PF08365; IGF2_C; 1. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR02002; INSLNLIKEGF. DR PRINTS; PR02006; INSLNLIKEGF2. DR PRINTS; PR00276; INSULINFAMLY. DR SMART; SM00078; IlGF; 1. DR SUPFAM; SSF56994; Insulin-like; 1. DR PROSITE; PS00262; INSULIN; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR622350-50}; KW Growth factor {ECO:0000256|ARBA:ARBA00023030}; KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU000406}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..186 FT /note="Insulin-like growth factor II" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002652424" FT DOMAIN 30..88 FT /note="Insulin-like" FT /evidence="ECO:0000259|SMART:SM00078" FT DISULFID 33..75 FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50" FT DISULFID 45..88 FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50" FT DISULFID 74..79 FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50" SQ SEQUENCE 186 AA; 20909 MW; 56BD00C6553CE511 CRC64; MGFPTKKMLL LSLTFLAFAS CCDAAYRPSE TLCGGELVDT LQFVCGDRGF YFSLPGRPLS RVSRRLNRGI VEECCFRSCD LALLETYCAT PAKSERDLSA SMMVLPDNFP RFPVGRFFKL DTWQKSAHRL RRGLPALLRA RRDRLRAQAL DAIREAKRHR PLISLPSGDP LRAELAAASE KAARQK //