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IGF2A_XENLA
ID   IGF2A_XENLA             Reviewed;         217 AA.
AC   Q90WW4; Q6NS08;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Insulin-like growth factor II-A;
DE            Short=IGF-II-A;
DE   AltName: Full=Insulin-like growth factor 2-A;
DE            Short=xIGF-2;
DE   Flags: Precursor;
GN   Name=igf2-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] {ECO:0000305, ECO:0000312|EMBL:AAL11445.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   [2] {ECO:0000312|EMBL:AAH70545.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:AAH70545.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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 anterior neural development
CC       (PubMed:11709186). Acts as a ligand for integrin which is required for
CC       IGF2 signaling (By similarity). {ECO:0000250|UniProtKB:P01344,
CC       ECO:0000269|PubMed:11709186}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed in the dorsal midline during gastrulation and neurulation.
CC       {ECO:0000269|PubMed:11709186}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH70545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY050645; AAL11445.1; -; mRNA.
DR   EMBL; BC070545; AAH70545.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001082128.1; NM_001088659.1.
DR   RefSeq; XP_018114956.1; XM_018259467.1.
DR   AlphaFoldDB; Q90WW4; -.
DR   DNASU; 398240; -.
DR   GeneID; 398240; -.
DR   KEGG; xla:398240; -.
DR   CTD; 398240; -.
DR   Xenbase; XB-GENE-6251806; igf2.S.
DR   OMA; YFSRPYR; -.
DR   OrthoDB; 1644517at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 398240; Expressed in internal ear and 16 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:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0060323; P:head morphogenesis; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   InterPro; IPR022334; IGF2.
DR   InterPro; IPR013576; IGF2_C.
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; PF08365; IGF2_C; 1.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR02002; INSLNLIKEGF.
DR   PRINTS; PR02006; INSLNLIKEGF2.
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; Differentiation; Disulfide bond; Growth factor;
KW   Neurogenesis; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..56
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..123
FT                   /note="Insulin-like growth factor II-A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000224639"
FT   PROPEP          124..217
FT                   /note="E peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000224640"
FT   REGION          57..83
FT                   /note="B"
FT                   /evidence="ECO:0000255"
FT   REGION          84..96
FT                   /note="C"
FT                   /evidence="ECO:0000255"
FT   REGION          97..117
FT                   /note="A"
FT                   /evidence="ECO:0000255"
FT   REGION          118..123
FT                   /note="D"
FT                   /evidence="ECO:0000255"
FT   SITE            79
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            89
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            92
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   SITE            93
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   DISULFID        64..103
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   DISULFID        76..116
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
FT   DISULFID        102..107
FT                   /evidence="ECO:0000250|UniProtKB:P01344"
SQ   SEQUENCE   217 AA;  24874 MW;  E1D290F8458BBA7A CRC64;
     MEQLSCKHRS SSVEAEAQLC RQTESRSTQL PRMSVMRHLF LLSITFLVYT LDSAKAYRAT
     ETLCGGELVD TLQFVCGDRG FYFSTNNGRS NRRPNRGIVD VCCFKSCDLE LLETYCAKPT
     KNERDVSTAP ATAIPPLSKQ DLYHKHHHTK SSKYDIWQRK SIHRLRRGVP AIVRARQYRL
     LMEKAEEAEQ ALSHRPLTTL PITRPLRLQQ ASEPSHN
 
 
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