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P47879 (IBP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor-binding protein 4
Short name=IBP-4
Short name=IGF-binding protein 4
Short name=IGFBP-4
Gene names
Name:Igfbp4
Synonyms:Igfbp-4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.

Subunit structure

Binds IGF2 more than IGF1.

Subcellular location

Secreted.

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Chain22 – 254233Insulin-like growth factor-binding protein 4
PRO_0000014383

Regions

Domain23 – 10381IGFBP N-terminal
Domain167 – 24579Thyroglobulin type-1

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 53 By similarity
Disulfide bond30 ↔ 55 By similarity
Disulfide bond38 ↔ 59 By similarity
Disulfide bond44 ↔ 56 By similarity
Disulfide bond67 ↔ 80 By similarity
Disulfide bond74 ↔ 100 By similarity
Disulfide bond131 ↔ 138 By similarity
Disulfide bond170 ↔ 200 By similarity
Disulfide bond211 ↔ 222 By similarity
Disulfide bond224 ↔ 245 By similarity

Experimental info

Sequence conflict4 – 52FG → CS in CAA57272. Ref.1
Sequence conflict131A → T in CAA57272. Ref.1
Sequence conflict561C → S in CAA57272. Ref.1
Sequence conflict671C → G in CAA57272. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47879 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 58EF89CB514AEE17

FASTA25427,807
        10         20         30         40         50         60 
MLPFGLVAAL LLAAGPRPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA 

        70         80         90        100        110        120 
LGLGMPCGVY TPRCGSGMRC YPPRGVEKPL RTLMHGQGVC TELSEIEAIQ ESLQTSDKDE 

       130        140        150        160        170        180 
SEHPNNSFNP CSAHDHRCLQ KHMAKIRDRS KMKIVGTPRE EPRPVPQGSC QSELHRALER 

       190        200        210        220        230        240 
LAASQSRTHE DLFIIPIPNC DRNGNFHPKQ CHPALDGQRG KCWCVDRKTG VKLPGGLEPK 

       250 
GELDCHQLAD SFQE

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and mRNA expression of the six mouse insulin-like growth factor binding proteins."
Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C., Drop S.L.S.
Mol. Cell. Endocrinol. 104:57-66(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning of mouse insulin-like growth factor binding protein 4 (IGFBP4) cDNA and expression of a fusion protein with IGF-binding activity."
Bethel C.R., Vitullo J.C., Miller R.E., Aron D.C.
Biochem. Mol. Biol. Int. 34:385-392(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6J.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[5]"Characterization of the mouse insulin-like growth factor binding protein 4 gene regulatory region and expression studies."
Glantschnig H., Varga F., Luegmayr E., Klaushofer K.
DNA Cell Biol. 17:51-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
Strain: BALB/c.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X81582 mRNA. Translation: CAA57272.1.
X76066 Genomic DNA. Translation: CAA53667.1.
AK150229 mRNA. Translation: BAE29395.1.
AK165688 mRNA. Translation: BAE38340.1.
BC019836 mRNA. Translation: AAH19836.1.
Z95492 Genomic DNA. Translation: CAB08859.1.
IPIIPI00112487.
PIRI48599.
I48603.
RefSeqNP_034647.1. NM_010517.3.
UniGeneMm.233799.

3D structure databases

ProteinModelPortalP47879.
SMRP47879. Positions 24-103, 168-246.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000017637.

PTM databases

PhosphoSiteP47879.

Proteomic databases

PaxDbP47879.
PRIDEP47879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017637; ENSMUSP00000017637; ENSMUSG00000017493.
GeneID16010.
KEGGmmu:16010.
UCSCuc007lie.1. mouse.

Organism-specific databases

CTD3487.
MGIMGI:96439. Igfbp4.

Phylogenomic databases

eggNOGNOG46496.
GeneTreeENSGT00550000074457.
HOGENOMHOG000253012.
HOVERGENHBG002631.
InParanoidP47879.
OMAKGMPCGV.
OrthoDBEOG4FR0SF.

Gene expression databases

ArrayExpressP47879.
BgeeP47879.
CleanExMM_IGFBP4.
GenevestigatorP47879.
GermOnlineENSMUSG00000017493. Mus musculus.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. Growth_fac_rcpt_N_dom.
IPR022327. IGFBP-4.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERPTHR11551. PTHR11551. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01980. IGFBPFAMILY4.
SMARTSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMSSF57184. Grow_fac_recept. 1 hit.
SSF57610. Thyroglobulin_1. 1 hit.
PROSITEPS00222. 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]
ProtoNetSearch...

Other

ChiTaRSIGFBP4. mouse.
NextBio288822.
PMAP-CutDBP47879.
SOURCESearch...

Entry information

Entry nameIBP4_MOUSE
AccessionPrimary (citable) accession number: P47879
Secondary accession number(s): O35666, Q3TMV0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 15, 1998
Last modified: May 29, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents