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IGF2_CHICK
ID   IGF2_CHICK              Reviewed;         187 AA.
AC   P33717; P79890; Q7ZZT6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Insulin-like growth factor II;
DE            Short=IGF-II;
DE   Flags: Precursor;
GN   Name=IGF2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8804558; DOI=10.1006/gcen.1996.0071;
RA   Darling D.C., Brickell P.M.;
RT   "Nucleotide sequence and genomic structure of the chicken insulin-like
RT   growth factor-II (IGF-II) coding region.";
RL   Gen. Comp. Endocrinol. 102:283-287(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=14601723; DOI=10.1093/ps/82.10.1485;
RA   Amills M., Jimenez N., Villalba D., Tor M., Molina E., Cubilo D.,
RA   Marcos C., Francesch A., Sanchez A., Estany J.;
RT   "Identification of three single nucleotide polymorphisms in the chicken
RT   insulin-like growth factor 1 and 2 genes and their associations with growth
RT   and feeding traits.";
RL   Poult. Sci. 82:1485-1493(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-91.
RX   PubMed=1688912; DOI=10.1677/joe.0.1240089;
RA   Kallincos N.C., Wallace J.C., Francis G.L., Ballard F.J.;
RT   "Chemical and biological characterization of chicken insulin-like growth
RT   factor-II.";
RL   J. Endocrinol. 124:89-97(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-60.
RX   PubMed=3379351; DOI=10.1677/joe.0.1170173;
RA   Dawe S.R., Francis G.L., McNamara P.J., Wallace J.C., Ballard F.J.;
RT   "Purification, partial sequences and properties of chicken insulin-like
RT   growth factors.";
RL   J. Endocrinol. 117:173-181(1988).
CC   -!- FUNCTION: The insulin-like growth factors, isolated from plasma, are
CC       structurally and functionally related to insulin but have a much higher
CC       growth-promoting activity. Acts as a ligand for integrin which is
CC       required for IGF2 signaling. {ECO:0000250|UniProtKB:P01344}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; S82962; AAB46818.1; -; Genomic_DNA.
DR   EMBL; S82960; AAB46818.1; JOINED; Genomic_DNA.
DR   EMBL; AY267181; AAP22173.1; -; mRNA.
DR   PIR; A60740; A60740.
DR   PIR; T10897; T10897.
DR   RefSeq; NP_001025513.1; NM_001030342.2.
DR   AlphaFoldDB; P33717; -.
DR   SMR; P33717; -.
DR   STRING; 9031.ENSGALP00000010570; -.
DR   PaxDb; P33717; -.
DR   Ensembl; ENSGALT00000053800; ENSGALP00000048743; ENSGALG00000035282.
DR   GeneID; 395097; -.
DR   KEGG; gga:395097; -.
DR   CTD; 3481; -.
DR   VEuPathDB; HostDB:geneid_395097; -.
DR   eggNOG; ENOG502S0I0; Eukaryota.
DR   GeneTree; ENSGT00940000160745; -.
DR   HOGENOM; CLU_092464_1_0_1; -.
DR   InParanoid; P33717; -.
DR   OMA; PSHAKYS; -.
DR   OrthoDB; 1644517at2759; -.
DR   PhylomeDB; P33717; -.
DR   TreeFam; TF332820; -.
DR   PRO; PR:P33717; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000035282; Expressed in liver and 13 other tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0051148; P:negative regulation of muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IBA:GO_Central.
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:2000467; P:positive regulation of glycogen (starch) synthase activity; IBA:GO_Central.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IBA:GO_Central.
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:0051147; P:regulation of muscle cell differentiation; IBA:GO_Central.
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   Direct protein sequencing; Disulfide bond; Growth factor; Mitogen;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..91
FT                   /note="Insulin-like growth factor II"
FT                   /id="PRO_0000221092"
FT   PROPEP          92..187
FT                   /note="E peptide"
FT                   /id="PRO_0000370382"
FT   REGION          25..51
FT                   /note="B"
FT   REGION          52..64
FT                   /note="C"
FT   REGION          64..85
FT                   /note="A"
FT   REGION          86..91
FT                   /note="D"
FT   REGION          162..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            47
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            57
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            60
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   DISULFID        32..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..75
FT                   /evidence="ECO:0000250"
FT   CONFLICT        64
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   187 AA;  20837 MW;  B301581CD4878EEC CRC64;
     MCAARQILLL LLAFLAYALD SAAAYGTAET LCGGELVDTL QFVCGDRGFY FSRPVGRNNR
     RINRGIVEEC CFRSCDLALL ETYCAKSVKS ERDLSATSLA GLPALNKESF QKPSHAKYSK
     YNVWQKKSSQ RLQREVPGIL RARRYRWQAE GLQAAEEARA MHRPLISLPS QRPPAPRASP
     EATGPQE
 
 
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