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Protein
Submitted name:

Insulin-like growth factor-binding protein 3

Gene

Igfbp3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

  1. protein tyrosine phosphatase activator activity Source: Ensembl

GO - Biological processi

  1. negative regulation of protein phosphorylation Source: Ensembl
  2. negative regulation of smooth muscle cell migration Source: Ensembl
  3. negative regulation of smooth muscle cell proliferation Source: Ensembl
  4. osteoblast differentiation Source: Ensembl
  5. positive regulation of apoptotic process Source: Ensembl
  6. positive regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
  7. positive regulation of MAPK cascade Source: Ensembl
  8. positive regulation of myoblast differentiation Source: Ensembl
  9. protein phosphorylation Source: Ensembl
  10. regulation of cell growth Source: Ensembl
  11. regulation of glucose metabolic process Source: Ensembl
  12. type B pancreatic cell proliferation Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_250882. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Names & Taxonomyi

Protein namesi
Submitted name:
Insulin-like growth factor-binding protein 3Imported
Gene namesi
Name:Igfbp3Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi2874. Igfbp3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: Ensembl
Complete GO annotation...

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation

Family & Domainsi

Sequence similaritiesi

Contains IGFBP N-terminal domain.SAAS annotation

Phylogenomic databases

GeneTreeiENSGT00550000074457.
OMAiRALEQCK.
OrthoDBiEOG74N5HG.
TreeFamiTF331211.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR012211. IGFBP-3.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF3. PTHR11551:SF3. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01979. IGFBPFAMILY3.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

F1LRU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PGAPAVTGLV REPGCGCCLT CALREGDACG VYTERCGTGL RCQPRPAEQY
60 70 80 90 100
PLKALLNGRG FCANASAASS LSAYLPSQPS PGNTTESEED HNAGSVESQV
110 120 130 140 150
VPSTHRVTDS KFHPLHSKME VIIKGQARDS QRYKVDYESQ STDTQNFSSE
160 170 180 190 200
SKRETEYGPC RREMEDTLNH LKFLNVLSPR GVHIPNCDKK GFYKKKQCRP
210 220 230
SKGRKRGFCW CVDKYGQPLP GYDTKGKDDV HCLSVQSQ
Length:238
Mass (Da):26,209
Last modified:April 3, 2013 - v2
Checksum:i2A00147E16AA2506
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06080135 Genomic DNA. No translation available.
AABR06080136 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000011678; ENSRNOP00000011678; ENSRNOG00000008645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06080135 Genomic DNA. No translation available.
AABR06080136 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011678; ENSRNOP00000011678; ENSRNOG00000008645.

Organism-specific databases

RGDi2874. Igfbp3.

Phylogenomic databases

GeneTreeiENSGT00550000074457.
OMAiRALEQCK.
OrthoDBiEOG74N5HG.
TreeFamiTF331211.

Enzyme and pathway databases

ReactomeiREACT_250882. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

NextBioi35576869.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR012211. IGFBP-3.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF3. PTHR11551:SF3. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01979. IGFBPFAMILY3.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiF1LRU0_RAT
AccessioniPrimary (citable) accession number: F1LRU0
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: April 3, 2013
Last modified: March 4, 2015
This is version 28 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.