IBP2A_DANRE
ID IBP2A_DANRE Reviewed; 276 AA.
AC Q9PTH3; A8E5I5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Insulin-like growth factor-binding protein 2-A;
DE Short=IGF-binding protein 2-A;
DE Short=IGFBP-2-A;
DE Short=IGFBP-2a;
DE Flags: Precursor;
GN Name=igfbp2a; Synonyms=igfbp2, igfbp2b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IGF1 AND IGF2,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10611375; DOI=10.1073/pnas.96.26.15274;
RA Duan C., Ding J., Li Q., Tsai W., Pozios K.;
RT "Insulin-like growth factor binding protein 2 is a growth inhibitory
RT protein conserved in zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15274-15279(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19081843; DOI=10.1371/journal.pone.0003926;
RA Zhou J., Li W., Kamei H., Duan C.;
RT "Duplication of the IGFBP-2 gene in teleost fish: protein structure and
RT functionality conservation and gene expression divergence.";
RL PLoS ONE 3:E3926-E3926(2008).
CC -!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and
CC have been shown to either inhibit or stimulate the growth promoting
CC effects of the IGFs on cell culture. They alter the interaction of IGFs
CC with their cell surface receptors. {ECO:0000269|PubMed:10611375,
CC ECO:0000269|PubMed:19081843}.
CC -!- SUBUNIT: Interacts equally well with igf1 and igf2.
CC {ECO:0000269|PubMed:10611375}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In embryos at 24 hpf, initially expressed in the
CC lens and cranial region, and at 48 and 72 hpf in the brain boundary
CC vasculature. Expression in these regions persists throughout the
CC hatching period and by 96 hpf expression is most abundant in the liver.
CC In both male and female adults, highest expression is in the liver with
CC modest expression in the brain. In male but not females adults,
CC expressed at a low level in muscle and gonad. Also expressed in the
CC adult intestine. {ECO:0000269|PubMed:10611375,
CC ECO:0000269|PubMed:19081843}.
CC -!- DEVELOPMENTAL STAGE: Not expressed until 10 hpf. Expression gradually
CC increases from 10 to 36 hpf and is maintained at high levels
CC thereafter. {ECO:0000269|PubMed:19081843}.
CC -!- INDUCTION: Expression increases in response to prolonged fasting but
CC decreases in response to growth hormone (GH).
CC {ECO:0000269|PubMed:10611375}.
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DR EMBL; AF198033; AAF23123.1; -; mRNA.
DR EMBL; BC056331; AAH56331.1; -; mRNA.
DR EMBL; BC153606; AAI53607.1; -; mRNA.
DR RefSeq; NP_571533.1; NM_131458.2.
DR AlphaFoldDB; Q9PTH3; -.
DR SMR; Q9PTH3; -.
DR STRING; 7955.ENSDARP00000068816; -.
DR MEROPS; I31.953; -.
DR PaxDb; Q9PTH3; -.
DR Ensembl; ENSDART00000074327; ENSDARP00000068816; ENSDARG00000052470.
DR Ensembl; ENSDART00000182607; ENSDARP00000150294; ENSDARG00000111105.
DR GeneID; 794176; -.
DR KEGG; dre:794176; -.
DR CTD; 794176; -.
DR ZFIN; ZDB-GENE-000125-12; igfbp2a.
DR eggNOG; ENOG502QRWQ; Eukaryota.
DR GeneTree; ENSGT00940000158542; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; Q9PTH3; -.
DR OMA; AEPCAEM; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; Q9PTH3; -.
DR TreeFam; TF331211; -.
DR Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR PRO; PR:Q9PTH3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000052470; Expressed in liver and 20 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0048640; P:negative regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR012210; IGFBP-2.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR022321; IGFBP_1-6_chordata.
DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01978; IGFBPFAMILY2.
DR SMART; SM00121; IB; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS00222; IGFBP_N_1; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Growth factor binding;
KW Growth regulation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..276
FT /note="Insulin-like growth factor-binding protein 2-A"
FT /id="PRO_0000014376"
FT DOMAIN 24..105
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 177..259
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT MOTIF 254..256
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT DISULFID 180..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 225..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 238..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 276 AA; 30764 MW; 37AB561B7C9947D7 CRC64;
MLSYVSCGLL LALVTFHGTA RSEMVFRCPS CTAERQAACP MLTETCGEIV REPGCGCCPV
CARQEGEQCG VYTPRCSSGL RCYPKPDSEL PLELLVQGLG RCGRKVDTEP TGSAEPREVS
GEVQDPLDIG LTEVPPIRKP TKDSPWKESA VLQHRQQLKS KMKYHKVEDP KAPHAKQSQC
QQELDQVLER ISKITFKDNR TPLEDLYSLH IPNCDKRGQY NLKQCKMSVN GYRGECWCVN
PHTGRPMPTS PLIRGDPNCN QYLDGQEMDP SVDPPN
