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