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IGF1_CAPHI
ID   IGF1_CAPHI              Reviewed;         154 AA.
AC   P51457;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Insulin-like growth factor I;
DE            Short=IGF-I;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor;
GN   Name=IGF1;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7765981; DOI=10.1271/bbb.59.87;
RA   Mikawa S., Yoshikawa G., Aoki H., Yamano Y., Sakai H., Komano T.;
RT   "Dynamic aspects in the expression of the goat insulin-like growth factor-I
RT   (IGF-I) gene: diversity in transcription and post-transcription.";
RL   Biosci. Biotechnol. Biochem. 59:87-92(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Shiba; TISSUE=Liver;
RX   PubMed=7772848; DOI=10.1271/bbb.59.759;
RA   Mikawa S., Yoshikawa G., Yamano Y., Sakai H., Komano T., Hosoi Y.,
RA   Utsumi K.;
RT   "Tissue- and development-specific expression of goat insulin-like growth
RT   factor-I (IGF-I) mRNAs.";
RL   Biosci. Biotechnol. Biochem. 59:759-761(1995).
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. May be a physiological regulator of [1-14C]-
CC       2-deoxy-D-glucose (2DG) transport and glycogen synthesis in
CC       osteoblasts. Stimulates glucose transport in bone-derived osteoblastic
CC       (PyMS) cells and is effective at much lower concentrations than
CC       insulin, not only regarding glycogen and DNA synthesis but also with
CC       regard to enhancing glucose uptake. May play a role in synapse
CC       maturation. Ca(2+)-dependent exocytosis of IGF1 is required for sensory
CC       perception of smell in the olfactory bulb. Acts as a ligand for IGF1R.
CC       Binds to the alpha subunit of IGF1R, leading to the activation of the
CC       intrinsic tyrosine kinase activity which autophosphorylates tyrosine
CC       residues in the beta subunit thus initiatiating a cascade of down-
CC       stream signaling events leading to activation of the PI3K-AKT/PKB and
CC       the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4.
CC       Its binding to integrins and subsequent ternary complex formation with
CC       integrins and IGFR1 are essential for IGF1 signaling. Induces the
CC       phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and
CC       AKT1 (By similarity). {ECO:0000250|UniProtKB:P05017,
CC       ECO:0000250|UniProtKB:P05019}.
CC   -!- SUBUNIT: Forms a ternary complex with IGFR1 and ITGAV:ITGB3. Forms a
CC       ternary complex with IGFR1 and ITGA6:ITGB4.
CC       {ECO:0000250|UniProtKB:P05019}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined: brain, lung,
CC       liver, spleen, uterus, ovary, testis, heart and skeletal muscle.
CC       {ECO:0000269|PubMed:7772848}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; D26119; BAB77524.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; D11378; BAA01976.1; -; mRNA.
DR   PIR; JC2483; JC2483.
DR   RefSeq; NP_001272626.1; NM_001285697.1.
DR   AlphaFoldDB; P51457; -.
DR   SMR; P51457; -.
DR   STRING; 9925.ENSCHIP00000020185; -.
DR   Ensembl; ENSCHIT00000027999; ENSCHIP00000020169; ENSCHIG00000018863.
DR   GeneID; 100860838; -.
DR   KEGG; chx:100860838; -.
DR   CTD; 3479; -.
DR   GeneTree; ENSGT00940000159081; -.
DR   OMA; FFYLALC; -.
DR   OrthoDB; 1644517at2759; -.
DR   Proteomes; UP000291000; Chromosome 5.
DR   Bgee; ENSCHIG00000018863; Expressed in fallopian tube and 17 other tissues.
DR   GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISS:UniProtKB.
DR   GO; GO:0070382; C:exocytic vesicle; ISS:UniProtKB.
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:InterPro.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; 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:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; 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   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   Disulfide bond; Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..49
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015652"
FT   CHAIN           50..119
FT                   /note="Insulin-like growth factor I"
FT                   /id="PRO_0000015653"
FT   PROPEP          120..154
FT                   /note="E peptide"
FT                   /id="PRO_0000015654"
FT   REGION          50..78
FT                   /note="B"
FT   REGION          79..90
FT                   /note="C"
FT   REGION          91..111
FT                   /note="A"
FT   REGION          112..119
FT                   /note="D"
FT   REGION          120..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        55..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..101
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  17082 MW;  07238B6AF3068422 CRC64;
     MGKISSLPTQ LFKCCFCDFL KQVKMPVTSS SHLFYLALCL LAFTSSATAG PETLCGAELV
     DALQFVCGDR GFYFNKPTGY GSSSRRAPQT GIVDECCFRS CDLRRLEMYC APLKPTKSAR
     SVRAQRHTDM PKAQKEVHLK NTSRGSAGNK NYRM
 
 
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