ID   IGF1A_XENLA             Reviewed;         153 AA.
AC   P16501;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Insulin-like growth factor I-A;
DE            Short=IGF-I';
DE            Short=IGF-IA;
DE            Short=xIGF-1;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor;
GN   Name=igf1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=2330002; DOI=10.1210/mend-4-2-217;
RA   Kajimoto Y., Rotwein P.;
RT   "Evolution of insulin-like growth factor I (IGF-I): structure and
RT   expression of an IGF-I precursor from Xenopus laevis.";
RL   Mol. Endocrinol. 4:217-226(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-125, AND TISSUE SPECIFICITY.
RX   PubMed=2302204; DOI=10.1016/0006-291x(90)91934-k;
RA   Shuldiner A.R., Nirula A., Scott L.A., Roth J.;
RT   "Evidence that Xenopus laevis contains two different nonallelic insulin-
RT   like growth factor-I genes.";
RL   Biochem. Biophys. Res. Commun. 166:223-230(1990).
RN   [3]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11709186; DOI=10.1016/s1534-5807(01)00069-7;
RA   Pera E.M., Wessely O., Li S.-Y., De Robertis E.M.;
RT   "Neural and head induction by insulin-like growth factor signals.";
RL   Dev. Cell 1:655-665(2001).
RN   [4]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11944947; DOI=10.1006/dbio.2002.0605;
RA   Richard-Parpaillon L., Heligon C., Chesnel F., Boujard D., Philpott A.;
RT   "The IGF pathway regulates head formation by inhibiting Wnt signaling in
RT   Xenopus.";
RL   Dev. Biol. 244:407-417(2002).
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. Promotes head development by inhibiting Wnt
CC       signaling during embryogenesis (PubMed:11709186, PubMed:11944947). Acts
CC       as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to
CC       the activation of the intrinsic tyrosine kinase activity which
CC       autophosphorylates tyrosine residues in the beta subunit thus
CC       initiatiating a cascade of down-stream signaling events leading to
CC       activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to
CC       integrins. Its binding to integrins and subsequent ternary complex
CC       formation with integrins and IGFR1 are essential for IGF1 signaling (By
CC       similarity). {ECO:0000250|UniProtKB:P05019,
CC       ECO:0000269|PubMed:11709186, ECO:0000269|PubMed:11944947}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in adult liver, lung, heart, kidney and
CC       peritoneal fat. {ECO:0000269|PubMed:2302204,
CC       ECO:0000269|PubMed:2330002}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically after
CC       the midblastula transition. Present both dorsally and ventrally at the
CC       beginning of neurulation. Expression is restricted to the developing
CC       heart at the tailbud stage. {ECO:0000269|PubMed:11709186,
CC       ECO:0000269|PubMed:11944947}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; M29857; AAA70330.1; -; mRNA.
DR   PIR; A34049; A34049.
DR   PIR; A36079; A36079.
DR   RefSeq; NP_001156865.1; NM_001163393.1.
DR   RefSeq; XP_018110181.1; XM_018254692.1.
DR   AlphaFoldDB; P16501; -.
DR   SMR; P16501; -.
DR   GeneID; 108712492; -.
DR   GeneID; 378699; -.
DR   KEGG; xla:108712492; -.
DR   AGR; Xenbase:XB-GENE-17330790; -.
DR   CTD; 378699; -.
DR   OMA; DLWHLEM; -.
DR   OrthoDB; 5402912at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 108712492; Expressed in liver and 4 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0060323; P:head morphogenesis; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   CDD; cd04368; IlGF; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR022341; IGF-I.
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; PTHR46845; INSULIN-LIKE GROWTH FACTOR I; 1.
DR   PANTHER; PTHR46845:SF1; INSULIN-LIKE GROWTH FACTOR I; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02002; INSLNLIKEGF.
DR   PRINTS; PR02005; INSLNLIKEGF1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Growth factor; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..?
FT   PROPEP          ?..48
FT                   /id="PRO_0000015708"
FT   CHAIN           49..118
FT                   /note="Insulin-like growth factor I-A"
FT                   /id="PRO_0000015709"
FT   PROPEP          119..153
FT                   /note="E peptide"
FT                   /id="PRO_0000015710"
FT   REGION          49..77
FT                   /note="B"
FT   REGION          78..89
FT                   /note="C"
FT   REGION          90..110
FT                   /note="A"
FT   REGION          111..118
FT                   /note="D"
FT   REGION          119..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        54..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250"
FT   CONFLICT        114
FT                   /note="Q -> P (in Ref. 1; AAA70330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="T -> A (in Ref. 1; AAA70330)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   153 AA;  17410 MW;  F83BC8AA17AFDBEE CRC64;
     METNNNLSTQ LFKCYFCDIL KLKMHKMSCI HLLYLVLCFL TLTHSAAAGP ETLCGAELVD
     TLQFVCGDRG FYFSKPTGYG SNNRRSHHRG IVDECCFQSC DFRRLEMYCA PAKQAKSARS
     VRTQRHTDMP KAQKEVHPKN TSRGNTGSRG FRM
//