Q62356 (FSTL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Repeat Signal
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DIP2A	Q14689	3	EBI-2564326,EBI-2564275	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 306	288	Follistatin-related protein 1		PRO_0000010113
Regions
	Domain	28 – 51	24	Follistatin-like
	Domain	46 – 98	53	Kazal-like
	Domain	142 – 176	35	EF-hand 1
	Domain	191 – 226	36	EF-hand 2
	Domain	231 – 285	55	VWFC
Amino acid modifications
	Glycosylation	142	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Disulfide bond	52 ↔ 82		By similarity
	Disulfide bond	56 ↔ 75		By similarity
	Disulfide bond	64 ↔ 96		By similarity
Experimental info
	Sequence conflict	235	1	D → V in AAC37633. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q62356 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 0AEB11C6321E8FDC	FASTA	306	34,554
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00124707.
PIR	S38251.
RefSeq	NP_032073.2. NM_008047.5.
UniGene	Mm.182434.
3D structure databases
ProteinModelPortal	Q62356.
SMR	Q62356. Positions 27-97, 144-221.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62356. 1 interaction.
STRING	10090.ENSMUSP00000110411.
Protein family/group databases
MEROPS	I01.967.
PTM databases
PhosphoSite	Q62356.
Proteomic databases
PaxDb	Q62356.
PRIDE	Q62356.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114763; ENSMUSP00000110411; ENSMUSG00000022816.
GeneID	14314.
KEGG	mmu:14314.
Organism-specific databases
CTD	11167.
MGI	MGI:102793. Fstl1.
Phylogenomic databases
eggNOG	NOG148907.
GeneTree	ENSGT00530000063333.
HOGENOM	HOG000007780.
HOVERGEN	HBG051665.
InParanoid	Q6GTX2.
OMA	GFNPPEK.
OrthoDB	EOG4J3WHG.
Gene expression databases
Bgee	Q62356.
CleanEx	MM_FSTL1.
Genevestigator	Q62356.
GermOnline	ENSMUSG00000022816. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR002048. EF_hand_dom. IPR003645. Fol_N. IPR015369. Follistatin/Osteonectin_EGF. IPR002350. Kazal_dom. [Graphical view]
Pfam	PF09289. FOLN. 1 hit. PF07648. Kazal_2. 1 hit. [Graphical view]
SMART	SM00054. EFh. 2 hits. SM00274. FOLN. 1 hit. SM00280. KAZAL. 1 hit. [Graphical view]
PROSITE	PS50222. EF_HAND_2. 2 hits. PS00282. KAZAL_1. False negative. PS51465. KAZAL_2. 1 hit. PS01208. VWFC_1. False negative. PS50184. VWFC_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	285749.
SOURCE	Search...

Entry information

Entry name

FSTL1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program