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IGF2_CAVPO
ID   IGF2_CAVPO              Reviewed;         128 AA.
AC   Q08279;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Insulin-like growth factor II;
DE            Short=IGF-II;
DE   AltName: Full=Somatomedin-A;
DE   Contains:
DE     RecName: Full=Insulin-like growth factor II;
DE   Contains:
DE     RecName: Full=Preptin;
DE   Flags: Precursor; Fragment;
GN   Name=IGF2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Liver;
RX   PubMed=1301379; DOI=10.1016/0303-7207(92)90216-s;
RA   Levinovitz A., Norstedt G., van den Berg S., Robinson I.C.A.F.,
RA   Ekstroem T.J.;
RT   "Isolation of an insulin-like growth factor II cDNA from guinea pig liver:
RT   expression and developmental regulation.";
RL   Mol. Cell. Endocrinol. 89:105-110(1992).
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. Acts as a ligand for integrin which is required for
CC       IGF2 signaling. Positively regulates myogenic transcription factor
CC       MYOD1 function by facilitating the recruitment of transcriptional
CC       coactivators, thereby controlling muscle terminal differentiation (By
CC       similarity). Inhibits myoblast differentiation and metabolism via
CC       increasing the mitochondrial respiration rate (By similarity).
CC       {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
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:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
CC   -!- SUBUNIT: Interacts with MYORG; this interaction is required for IGF2
CC       secretion. Interacts with integrins ITGAV:ITGB3 and ITGA6:ITGB4;
CC       integrin-binding is required for IGF2 signaling.
CC       {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344,
CC       ECO:0000250|UniProtKB:P09535}.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in fetal tissues and at
CC       lower levels in adult.
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:0000250|UniProtKB:P01344}.
CC   -!- MISCELLANEOUS: The IGF2 locus is imprinted. Paternal inherited gene is
CC       expressed, while the maternal inherited gene is imprinted, hence
CC       silenced. {ECO:0000250|UniProtKB:P09535}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; S59899; AAB26479.1; -; mRNA.
DR   PIR; I57671; I57671.
DR   AlphaFoldDB; Q08279; -.
DR   BMRB; Q08279; -.
DR   SMR; Q08279; -.
DR   STRING; 10141.ENSCPOP00000020235; -.
DR   eggNOG; ENOG502S0I0; Eukaryota.
DR   HOGENOM; CLU_161062_0_0_1; -.
DR   InParanoid; Q08279; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
DR   GO; GO:0060669; P:embryonic placenta morphogenesis; ISS:UniProtKB.
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: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:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
DR   GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Growth factor; Hormone; Mitogen;
KW   Osteogenesis; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..91
FT                   /note="Insulin-like growth factor II"
FT                   /id="PRO_0000015713"
FT   PROPEP          92..>128
FT                   /note="E peptide"
FT                   /id="PRO_0000015714"
FT   PEPTIDE         93..126
FT                   /note="Preptin"
FT                   /id="PRO_0000370374"
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   SITE            48
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            58
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            61
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            62
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   DISULFID        33..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..75
FT                   /evidence="ECO:0000250"
FT   NON_TER         128
SQ   SEQUENCE   128 AA;  14420 MW;  BC65A1D81A4CE056 CRC64;
     MGISMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFSRPASRVS
     RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSASLAV LPDNFPRYPV GKFFQYDTWR
     QSTQRLRR
 
 
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