IBP2B_DANRE
ID IBP2B_DANRE Reviewed; 265 AA.
AC B3F211;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Insulin-like growth factor-binding protein 2-B;
DE Short=IGF-binding protein 2-B;
DE Short=IGFBP-2-B;
DE Short=IGFBP-2b;
DE Flags: Precursor;
GN Name=igfbp2b {ECO:0000312|ZFIN:ZDB-GENE-090107-3};
GN Synonyms=igfbp2a {ECO:0000312|ZFIN:ZDB-GENE-090107-3};
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] {ECO:0000305, ECO:0000312|EMBL:ABS30427.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IGF1, TISSUE
RP 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:19081843}.
CC -!- SUBUNIT: Interacts with igf2 (By similarity). Interacts with igf1.
CC {ECO:0000250|UniProtKB:Q9PTH3, ECO:0000269|PubMed:19081843}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In early embryos, expressed at a low level in most
CC tissues with expression becoming abundant in the liver by 96 hours
CC post-fertilization (hpf). The expression pattern in adults exhibits
CC sexual dimorphism; in adult males expression is limited exclusively to
CC the liver whereas in adult females expression is observed in the liver
CC and other tissues including the gut, kidney, ovary and muscle.
CC {ECO:0000269|PubMed:19081843}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
CC {ECO:0000269|PubMed:19081843}.
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DR EMBL; EF507265; ABS30427.1; -; mRNA.
DR AlphaFoldDB; B3F211; -.
DR SMR; B3F211; -.
DR PaxDb; B3F211; -.
DR ZFIN; ZDB-GENE-090107-3; igfbp2b.
DR InParanoid; B3F211; -.
DR PhylomeDB; B3F211; -.
DR PRO; PR:B3F211; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005520; F:insulin-like growth factor binding; IDA:ZFIN.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
DR GO; GO:0031995; F:insulin-like growth factor II binding; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048640; P:negative regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISS: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; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..265
FT /note="Insulin-like growth factor-binding protein 2-B"
FT /evidence="ECO:0000250|UniProtKB:Q9PTH3, ECO:0000305"
FT /id="PRO_0000381735"
FT DOMAIN 19..99
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 166..248
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 243..245
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 169..203
FT /evidence="ECO:0000250|UniProtKB:P18065,
FT ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 214..225
FT /evidence="ECO:0000250|UniProtKB:P18065,
FT ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 227..248
FT /evidence="ECO:0000250|UniProtKB:P18065,
FT ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 265 AA; 29439 MW; 1E1A785AB69D92DE CRC64;
MSLALLCSLL LVHGSLGEIV FRCPSCTAER QAACPKLTTS CEIVREPGCG CCPVCARQKG
ELCGVYTTRC GSGLRCYPSA NSELPLEQLI QGLGRCENKV DLEPTMTNQE SAAHSGEVNG
TRSPPMKKPG KDYQYIKEIA VNKHHNNKRT RMYNTQDDPK TPHPKQSQCQ QELDKVLENI
SRMAFHDNKG PLENLYDLKF PNCDKTGQYN LKQCHMSTHG QRGECWCVNP YTGVQIPSSD
KVRGDPNCSQ YYGGPELEPP TAQQK
