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Q62356 (FSTL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Follistatin-related protein 1
Alternative name(s):
Follistatin-like protein 1
TGF-beta-inducible protein TSC-36
Gene names
Name:Fstl1
Synonyms:Frp, Fstl, Tsc36
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin By similarity.

Subunit structure

Interacts with SCN10A.

Subcellular location

Secreted Potential.

Sequence similarities

Contains 2 EF-hand domains.

Contains 1 follistatin-like domain.

Contains 1 Kazal-like domain.

Contains 1 VWFC domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to starvation

Inferred from direct assay PubMed 20054002. Source: UniProt

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20054002. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DIP2AQ146893EBI-2564326,EBI-2564275From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 306288Follistatin-related protein 1
PRO_0000010113

Regions

Domain28 – 5124Follistatin-like
Domain46 – 9853Kazal-like
Domain142 – 17635EF-hand 1
Domain191 – 22636EF-hand 2
Domain231 – 28555VWFC

Amino acid modifications

Glycosylation1421N-linked (GlcNAc...) Ref.5
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Disulfide bond52 ↔ 82 By similarity
Disulfide bond56 ↔ 75 By similarity
Disulfide bond64 ↔ 96 By similarity

Experimental info

Sequence conflict2351D → V in AAC37633. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62356 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0AEB11C6321E8FDC

FASTA30634,554
        10         20         30         40         50         60 
MWKRWLALSL VTIALVHGEE EPRSKSKICA NVFCGAGREC AVTEKGEPTC LCIEQCKPHK 

        70         80         90        100        110        120 
RPVCGSNGKT YLNHCELHRD ACLTGSKIQV DYDGHCKEKK SASPSASPVV CYQANRDELR 

       130        140        150        160        170        180 
RRLIQWLEAE IIPDGWFSKG SNYSEILDKY FKSFDNGDSH LDSSEFLKFV EQNETAINIT 

       190        200        210        220        230        240 
TYADQENNKL LRSLCVDALI ELSDENADWK LSFQEFLKCL NPSFNPPEKK CALEDETYAD 

       250        260        270        280        290        300 
GAETEVDCNR CVCSCGHWVC TAMTCDGKNQ KGVQTHTEEE KTGYVQELQK HQGTAEKTKK 


VNTKEI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning from a mouse osteoblastic cell line of a set of transforming-growth-factor-beta 1-regulated genes, one of which seems to encode a follistatin-related polypeptide."
Shibanuma M., Mashimo J., Mita A., Kuroki T., Nose K.
Eur. J. Biochem. 217:13-19(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Strain: C57BL/6J.
Tissue: Heart.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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.
[5]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-142.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M91380 mRNA. Translation: AAC37633.1.
AK049440 mRNA. Translation: BAC33751.1.
AK147117 mRNA. Translation: BAE27689.1.
CH466521 Genomic DNA. Translation: EDK97964.1.
BC028921 mRNA. Translation: AAH28921.1.
BC006185 mRNA. No translation available.
CCDSCCDS37339.1.
PIRS38251.
RefSeqNP_032073.2. NM_008047.5.
UniGeneMm.182434.

3D structure databases

ProteinModelPortalQ62356.
SMRQ62356. Positions 27-97, 145-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-56414N.
IntActQ62356. 1 interaction.
STRING10090.ENSMUSP00000110411.

Protein family/group databases

MEROPSI01.967.

PTM databases

PhosphoSiteQ62356.

Proteomic databases

MaxQBQ62356.
PaxDbQ62356.
PRIDEQ62356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114763; ENSMUSP00000110411; ENSMUSG00000022816.
GeneID14314.
KEGGmmu:14314.
UCSCuc007zej.1. mouse.

Organism-specific databases

CTD11167.
MGIMGI:102793. Fstl1.

Phylogenomic databases

eggNOGNOG148907.
GeneTreeENSGT00530000063333.
HOGENOMHOG000007780.
HOVERGENHBG051665.
InParanoidQ6GTX2.
OMARGLCIDA.
OrthoDBEOG7WT427.
TreeFamTF106409.

Gene expression databases

BgeeQ62356.
CleanExMM_FSTL1.
GenevestigatorQ62356.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
[Graphical view]
PfamPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
SM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 2 hits.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285749.
PROQ62356.
SOURCESearch...

Entry information

Entry nameFSTL1_MOUSE
AccessionPrimary (citable) accession number: Q62356
Secondary accession number(s): Q6GTX2, Q99JI9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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