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Protein

Follistatin-related protein 1

Gene

Fstl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. response to starvation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_220505. Signaling by BMP.

Protein family/group databases

MEROPSiI01.967.

Names & Taxonomyi

Protein namesi
Recommended name:
Follistatin-related protein 1
Alternative name(s):
Follistatin-like protein 1
TGF-beta-inducible protein TSC-36
Gene namesi
Name:Fstl1
Synonyms:Frp, Fstl, Tsc36
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:102793. Fstl1.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 306288Follistatin-related protein 1PRO_0000010113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 82PROSITE-ProRule annotation
Disulfide bondi56 ↔ 75PROSITE-ProRule annotation
Disulfide bondi64 ↔ 96PROSITE-ProRule annotation
Glycosylationi142 – 1421N-linked (GlcNAc...)1 Publication
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ62356.
PaxDbiQ62356.
PRIDEiQ62356.

PTM databases

PhosphoSiteiQ62356.

Expressioni

Gene expression databases

BgeeiQ62356.
CleanExiMM_FSTL1.
GenevestigatoriQ62356.

Interactioni

Subunit structurei

Interacts with SCN10A.

Binary interactionsi

WithEntry#Exp.IntActNotes
DIP2AQ146893EBI-2564326,EBI-2564275From a different organism.

Protein-protein interaction databases

DIPiDIP-56414N.
IntActiQ62356. 1 interaction.
STRINGi10090.ENSMUSP00000110411.

Structurei

3D structure databases

ProteinModelPortaliQ62356.
SMRiQ62356. Positions 27-97, 147-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 5124Follistatin-likeAdd
BLAST
Domaini46 – 9853Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini142 – 17635EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 22636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini231 – 28555VWFCAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 follistatin-like domain.Curated
Contains 1 Kazal-like domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG148907.
GeneTreeiENSGT00530000063333.
HOGENOMiHOG000007780.
HOVERGENiHBG051665.
InParanoidiQ62356.
OMAiWVHAEEE.
OrthoDBiEOG7WT427.
TreeFamiTF106409.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
SM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51465. KAZAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWKRWLALSL VTIALVHGEE EPRSKSKICA NVFCGAGREC AVTEKGEPTC
60 70 80 90 100
LCIEQCKPHK RPVCGSNGKT YLNHCELHRD ACLTGSKIQV DYDGHCKEKK
110 120 130 140 150
SASPSASPVV CYQANRDELR RRLIQWLEAE IIPDGWFSKG SNYSEILDKY
160 170 180 190 200
FKSFDNGDSH LDSSEFLKFV EQNETAINIT TYADQENNKL LRSLCVDALI
210 220 230 240 250
ELSDENADWK LSFQEFLKCL NPSFNPPEKK CALEDETYAD GAETEVDCNR
260 270 280 290 300
CVCSCGHWVC TAMTCDGKNQ KGVQTHTEEE KTGYVQELQK HQGTAEKTKK

VNTKEI
Length:306
Mass (Da):34,554
Last modified:July 27, 2011 - v2
Checksum:i0AEB11C6321E8FDC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351D → V in AAC37633 (PubMed:7901004).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37339.1.
PIRiS38251.
RefSeqiNP_032073.2. NM_008047.5.
UniGeneiMm.182434.

Genome annotation databases

EnsembliENSMUST00000114763; ENSMUSP00000110411; ENSMUSG00000022816.
GeneIDi14314.
KEGGimmu:14314.
UCSCiuc007zej.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37339.1.
PIRiS38251.
RefSeqiNP_032073.2. NM_008047.5.
UniGeneiMm.182434.

3D structure databases

ProteinModelPortaliQ62356.
SMRiQ62356. Positions 27-97, 147-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-56414N.
IntActiQ62356. 1 interaction.
STRINGi10090.ENSMUSP00000110411.

Protein family/group databases

MEROPSiI01.967.

PTM databases

PhosphoSiteiQ62356.

Proteomic databases

MaxQBiQ62356.
PaxDbiQ62356.
PRIDEiQ62356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114763; ENSMUSP00000110411; ENSMUSG00000022816.
GeneIDi14314.
KEGGimmu:14314.
UCSCiuc007zej.1. mouse.

Organism-specific databases

CTDi11167.
MGIiMGI:102793. Fstl1.

Phylogenomic databases

eggNOGiNOG148907.
GeneTreeiENSGT00530000063333.
HOGENOMiHOG000007780.
HOVERGENiHBG051665.
InParanoidiQ62356.
OMAiWVHAEEE.
OrthoDBiEOG7WT427.
TreeFamiTF106409.

Enzyme and pathway databases

ReactomeiREACT_220505. Signaling by BMP.

Miscellaneous databases

ChiTaRSiFstl1. mouse.
NextBioi285749.
PROiQ62356.
SOURCEiSearch...

Gene expression databases

BgeeiQ62356.
CleanExiMM_FSTL1.
GenevestigatoriQ62356.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
SM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFSTL1_MOUSE
AccessioniPrimary (citable) accession number: Q62356
Secondary accession number(s): Q6GTX2, Q99JI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.