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IGF1B_XENLA
ID   IGF1B_XENLA             Reviewed;          44 AA.
AC   P84775;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Insulin-like growth factor I-B;
DE            Short=IGF-I'';
DE            Short=IGF-IB;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor; Fragment;
GN   Name=igf1-b;
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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).
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 IGF1R. Binds to the
CC       alpha subunit of IGF1R, leading to the activation of the intrinsic
CC       tyrosine kinase activity which autophosphorylates tyrosine residues in
CC       the beta subunit thus initiatiating a cascade of down-stream signaling
CC       events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK
CC       pathways. Binds to integrins. Its binding to integrins and subsequent
CC       ternary complex formation with integrins and IGFR1 are essential for
CC       IGF1 signaling. {ECO:0000250|UniProtKB:P05019}.
CC   -!- TISSUE SPECIFICITY: Expressed in adult liver.
CC       {ECO:0000269|PubMed:2302204}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000255}.
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DR   AlphaFoldDB; P84775; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0060323; P:head morphogenesis; ISS: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; ISS: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   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02002; INSLNLIKEGF.
DR   PRINTS; PR02005; INSLNLIKEGF1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Growth factor; Reference proteome.
FT   CHAIN           <1..37
FT                   /note="Insulin-like growth factor I-B"
FT                   /id="PRO_0000224646"
FT   PROPEP          38..>44
FT                   /note="E peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000224647"
FT   REGION          <1..8
FT                   /note="C"
FT                   /evidence="ECO:0000255"
FT   REGION          9..29
FT                   /note="A"
FT                   /evidence="ECO:0000255"
FT   REGION          30..37
FT                   /note="D"
FT                   /evidence="ECO:0000255"
FT   DISULFID        14..19
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   NON_TER         1
FT                   /evidence="ECO:0000255"
FT   NON_TER         44
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   44 AA;  5136 MW;  AA4EE1A5990809E8 CRC64;
     NNRRAHHRGI VDECCFQSCD FRRLEMYCAP AKPAKSARSV RAQR
 
 
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