IGF1A_XENLA
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 03-AUG-2022, entry version 114.
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 GeneID; 108712492; -.
DR GeneID; 378699; -.
DR KEGG; xla:108712492; -.
DR CTD; 378699; -.
DR Xenbase; XB-GENE-17330790; igf1.S.
DR OMA; CAPAKTN; -.
DR OrthoDB; 1644517at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 108712492; Expressed in liver and 4 other 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 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 Pfam; PF00049; Insulin; 1.
DR PRINTS; PR02002; INSLNLIKEGF.
DR PRINTS; PR02005; INSLNLIKEGF1.
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 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
