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IGF1B_CYPCA
ID   IGF1B_CYPCA             Reviewed;         161 AA.
AC   Q90326;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Insulin-like growth factor I, juvenile form;
DE   Flags: Precursor;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9137817; DOI=10.1080/15216549700201921;
RA   Hashimoto H., Mikawa S., Takayama E., Yokoyama Y., Toyohara H.,
RA   Sakaguchi M.;
RT   "Molecular cloning and growth hormone-regulated gene expression of carp
RT   insulin-like growth factor-I.";
RL   Biochem. Mol. Biol. Int. 41:877-886(1997).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; D83272; BAA11879.1; -; mRNA.
DR   AlphaFoldDB; Q90326; -.
DR   SMR; Q90326; -.
DR   Ensembl; ENSCCRT00015098137; ENSCCRP00015095059; ENSCCRG00015038324.
DR   Ensembl; ENSCCRT00020005421; ENSCCRP00020004765; ENSCCRG00020002702.
DR   Proteomes; UP000694384; Unplaced.
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   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; 2.
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          ?..44
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015699"
FT   CHAIN           45..114
FT                   /note="Insulin-like growth factor I, juvenile form"
FT                   /id="PRO_0000015700"
FT   PROPEP          115..161
FT                   /note="E peptide"
FT                   /id="PRO_0000015701"
FT   REGION          45..73
FT                   /note="B"
FT   REGION          74..85
FT                   /note="C"
FT   REGION          86..106
FT                   /note="A"
FT   REGION          107..114
FT                   /note="D"
FT   REGION          111..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        50..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..96
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   161 AA;  17918 MW;  A48BB63F5BBCDC2A CRC64;
     MSSGHFFQGH WCDVFKCTMR CLSCTHTLSL VLCVLALTPA TLEAGPETLC GAELVDTLQF
     VCGDRGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKP GKTPRSVRAQ
     RHTDSPRTAK KPLPGQSHSS YKEVHQKNSS RGNTGGRNYR I
 
 
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