Q12841 (FSTL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Follistatin-related protein 1

Alternative name(s):
Follistatin-like protein 1

Gene names

Name:	FSTL1
Synonyms:	FRP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	308 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.
Tissue specificity	Overexpressed in synovial tissues from rheumatoid arthritis. Ref.3
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Traceable author statement. Source: Reactome
Cellular_component	extracellular space Traceable author statement Ref.2. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Ref.7
	Chain	21 – 308	288	Follistatin-related protein 1		PRO_0000010111
Regions
	Domain	30 – 53	24	Follistatin-like
	Domain	48 – 100	53	Kazal-like
	Domain	144 – 178	35	EF-hand 1
	Domain	193 – 228	36	EF-hand 2
	Domain	233 – 287	55	VWFC
Amino acid modifications
	Glycosylation	144	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	180	1	N-linked (GlcNAc...) Ref.8
	Disulfide bond	54 ↔ 84		By similarity
	Disulfide bond	58 ↔ 77		By similarity
	Disulfide bond	66 ↔ 98		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12841 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BD4C651FAFF24800	FASTA	308	34,986
	10 20 30 40 50 60 MWKRWLALAL ALVAVAWVRA EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP 70 80 90 100 110 120 HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE 130 140 150 160 170 180 LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN 190 200 210 220 230 240 ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY 250 260 270 280 290 300 ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a rat C6 glioma-secreted follistatin-related protein (FRP). Cloning and sequence of the human homologue." Zwijsen A., Blockx H., van Arnhem W., Willems J., Fransen L., Devos K., Raymackers J., van de Voorde A., Slegers H. Eur. J. Biochem. 225:937-946(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning of follistatin-related protein as a novel autoantigen in systemic rheumatic diseases." Tanaka M., Ozaki S., Osakada F., Mori K., Okubo M., Nakao K. Int. Immunol. 10:1305-1314(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Synovium.
[3]	"Follistatin-related protein gene (FRP) is expressed in the synovial tissues of rheumatoid arthritis, but its polymorphisms are not associated with genetic susceptibility." Ehara Y., Sakurai D., Tsuchiya N., Nakano K., Tanaka Y., Yamaguchi A., Tokunaga K. Clin. Exp. Rheumatol. 22:707-712(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Kidney.
[7]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-35.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175 AND ASN-180, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U06863 mRNA. Translation: AAA66062.1. D89937 mRNA. Translation: BAA28707.1. AB119283 Genomic DNA. Translation: BAD12167.1. AK289388 mRNA. Translation: BAF82077.1. AK312261 mRNA. Translation: BAG35192.1. CH471052 Genomic DNA. Translation: EAW79526.1. CH471052 Genomic DNA. Translation: EAW79527.1. BC000055 mRNA. Translation: AAH00055.1.
IPI	IPI00029723.
PIR	S51362.
RefSeq	NP_009016.1. NM_007085.4.
UniGene	Hs.269512.
3D structure databases
ProteinModelPortal	Q12841.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12841. 3 interactions.
STRING	9606.ENSP00000295633.
Protein family/group databases
MEROPS	I01.967.
PTM databases
PhosphoSite	Q12841.
Polymorphism databases
DMDM	2498390.
Proteomic databases
PaxDb	Q12841.
PeptideAtlas	Q12841.
PRIDE	Q12841.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295633; ENSP00000295633; ENSG00000163430.
GeneID	11167.
KEGG	hsa:11167.
UCSC	uc003eds.3. human.
Organism-specific databases
CTD	11167.
GeneCards	GC03M120111.
HGNC	HGNC:3972. FSTL1.
HPA	HPA035251.
MIM	605547. gene.
neXtProt	NX_Q12841.
PharmGKB	PA28389.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148907.
HOGENOM	HOG000007780.
HOVERGEN	HBG051665.
InParanoid	Q12841.
OMA	GFNPPEK.
OrthoDB	EOG4J3WHG.
PhylomeDB	Q12841.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q12841.
Bgee	Q12841.
CleanEx	HS_FSTL1.
Genevestigator	Q12841.
GermOnline	ENSG00000163430. Homo sapiens.
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
ChiTaRS	FSTL1. human.
GenomeRNAi	11167.
NextBio	42487.
PMAP-CutDB	Q12841.
SOURCE	Search...

Entry information

Entry name

FSTL1_HUMAN

Accession

Primary (citable) accession number: Q12841
Secondary accession number(s): D3DN90, Q549Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.