[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain stem; PubMed=3523756 [NCBI, ExPASy, EBI, Israel, Japan] Jaye M., Howk R., Burgess W., Ricca G.A., Chiu I.-M., Ravera M.W., O'Brien S.J., Modi W.S., Maciag T., Drohan W.N.; "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization."; Science 233:541-545(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0006-291X(89)91785-3; PubMed=2590193 [NCBI, ExPASy, EBI, Israel, Japan] Mergia A., Tischer E., Graves D., Tumolo A., Miller J., Gospodarowicz D., Abraham J.A., Shipley G.D., Fiddes J.C.; "Structural analysis of the gene for human acidic fibroblast growth factor."; Biochem. Biophys. Res. Commun. 164:1121-1129(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Brain stem; PubMed=2474753 [NCBI, ExPASy, EBI, Israel, Japan] Wang W.P., Lehtoma K., Varban M.L., Krishnan I., Chiu I.M.; "Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues."; Mol. Cell. Biol. 9:2387-2395(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain stem; PubMed=1693186 [NCBI, ExPASy, EBI, Israel, Japan] Chiu I.M., Wang W.P., Lehtoma K.; "Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1."; Oncogene 5:755-762(1990).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1717925 [NCBI, ExPASy, EBI, Israel, Japan] Wang W.P., Quick D., Balcerzak S.P., Needleman S.W., Chiu I.M.; "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients."; Oncogene 6:1521-1529(1991).
[6]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1084/jem.175.4.1073; PubMed=1372643 [NCBI, ExPASy, EBI, Israel, Japan] Li Y.L., Kha H., Golden J.A., Migchielsen A.A.J., Goetzl E.J., Turck E.J.; "An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist."; J. Exp. Med. 175:1073-1080(1992).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-21. Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-154. PubMed=7504343 [NCBI, ExPASy, EBI, Israel, Japan] Zhao X.M., Yeoh T.K., Hiebert M., Frist W.H., Miller G.G.; "The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells."; Transplantation 56:1177-1182(1993).
[10]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-40. DOI=10.1016/0006-291X(90)91348-V; PubMed=2393407 [NCBI, ExPASy, EBI, Israel, Japan] Crumley G., Dionne C.A., Jaye M.; "The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon."; Biochem. Biophys. Res. Commun. 171:7-13(1990).
[11]	PROTEIN SEQUENCE OF 16-155. DOI=10.1021/bi00362a017; PubMed=2427112 [NCBI, ExPASy, EBI, Israel, Japan] Harper J.W., Strydom D.J., Lobb R.R.; "Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor."; Biochemistry 25:4097-4103(1986).
[12]	PROTEIN SEQUENCE OF 16-155. DOI=10.1016/S0006-291X(86)80540-X; PubMed=3527167 [NCBI, ExPASy, EBI, Israel, Japan] Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.; "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor."; Biochem. Biophys. Res. Commun. 138:611-617(1986).
[13]	PROTEIN SEQUENCE OF 16-155. DOI=10.1016/0006-291X(86)90716-3; PubMed=3778488 [NCBI, ExPASy, EBI, Israel, Japan] Gautschi-Sova P., Mueller T., Boehlen P.; "Amino acid sequence of human acidic fibroblast growth factor."; Biochem. Biophys. Res. Commun. 140:874-880(1986).
[14]	PROTEIN SEQUENCE OF 16-47. DOI=10.1016/0006-291X(86)90028-8; PubMed=3964259 [NCBI, ExPASy, EBI, Israel, Japan] Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.; "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities."; Biochem. Biophys. Res. Commun. 135:541-548(1986).
[15]	PROTEIN SEQUENCE OF 16-49. DOI=10.1016/0014-5793(86)80812-2; PubMed=3732516 [NCBI, ExPASy, EBI, Israel, Japan] Gautschi P., Frater-Schroeder M., Boehlen P.; "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors."; FEBS Lett. 204:203-207(1986).
[16]	IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF2, AND INTERACTION WITH FGFBP1. PubMed=1885605 [NCBI, ExPASy, EBI, Israel, Japan] Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.; "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."; J. Biol. Chem. 266:16778-16785(1991).
[17]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-155. PubMed=1702556 [NCBI, ExPASy, EBI, Israel, Japan] Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.; "Three-dimensional structures of acidic and basic fibroblast growth factors."; Science 251:90-93(1991).
[18]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-155. DOI=10.1021/bi9521755; PubMed=8652550 [NCBI, ExPASy, EBI, Israel, Japan] Blaber M., Disalvo J., Thomas K.A.; "X-ray crystal structure of human acidic fibroblast growth factor."; Biochemistry 35:2086-2094(1996).
[19]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-155 IN COMPLEX WITH HEPARIN. DOI=10.1038/31741; PubMed=9655399 [NCBI, ExPASy, EBI, Israel, Japan] DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A.; "Structure of a heparin-linked biologically active dimer of fibroblast growth factor."; Nature 393:812-817(1998).
[20]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-155 IN COMPLEX WITH FGFR1. DOI=10.1016/S0092-8674(00)80851-X; PubMed=10830168 [NCBI, ExPASy, EBI, Israel, Japan] Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.; "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."; Cell 101:413-424(2000).
[21]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-155 IN COMPLEX WITH FGFR2 AND HEPARIN. DOI=10.1038/35039551; PubMed=11069186 [NCBI, ExPASy, EBI, Israel, Japan] Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.; "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."; Nature 407:1029-1034(2000).
[22]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-155 IN COMPLEX WITH FGFR2. DOI=10.1073/pnas.97.1.49; PubMed=10618369 [NCBI, ExPASy, EBI, Israel, Japan] Stauber D.J., DiGabriele A.D., Hendrickson W.A.; "Structural interactions of fibroblast growth factor receptor with its ligands."; Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000).
[23]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-155. DOI=10.1110/ps.43802; PubMed=11847269 [NCBI, ExPASy, EBI, Israel, Japan] Kim J., Blaber S.I., Blaber M.; "Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor."; Protein Sci. 11:459-466(2002).
[24]	X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FGFR3. DOI=10.1073/pnas.0307287101; PubMed=14732692 [NCBI, ExPASy, EBI, Israel, Japan] Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V., Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M.; "Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity."; Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004).
[25]	STRUCTURE BY NMR OF 24-155 IN COMPLEX WITH INOSITOL HEXASULFATE, AND PROTEIN SEQUENCE OF 24-27. DOI=10.1006/jmbi.1994.1558; PubMed=7521397 [NCBI, ExPASy, EBI, Israel, Japan] Pineda-Lucena A., Jimenez M.A., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.; "1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate."; J. Mol. Biol. 242:81-98(1994).
[26]	STRUCTURE BY NMR OF 24-155. DOI=10.1006/jmbi.1996.0631; PubMed=8950275 [NCBI, ExPASy, EBI, Israel, Japan] Pineda-Lucena A., Jimenez M.A., Lozano R.M., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.; "Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog."; J. Mol. Biol. 264:162-178(1996).
[27]	STRUCTURE BY NMR OF 24-155. DOI=10.1006/jmbi.1998.1977; PubMed=9719643 [NCBI, ExPASy, EBI, Israel, Japan] Lozano R.M., Jimenez M., Santoro J., Rico M., Gimenez-Gallego G.; "Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas."; J. Mol. Biol. 281:899-915(1998).

Comments

FUNCTION: The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
SUBUNIT: Monomer. Binds FGFR2. Forms a ternary complex containing 2 molecules each of FGFR2 and FGF1 for 1 heparin molecule. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1.
INTERACTION:
P21802:FGFR2; NbExp=1; IntAct=EBI-698068, EBI-1028658;
P22607:FGFR3; NbExp=2; IntAct=EBI-698068, EBI-348399;
MISCELLANEOUS: This protein binds heparin, although less strongly than does bFGF.
SIMILARITY: Belongs to the heparin-binding growth factors family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13361; AAA79245.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30492; AAA52446.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30490; AAA52446.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30491; AAA52446.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23087; AAA52638.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23086; AAA52638.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X51943; CAA36206.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X65778; CAA46661.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY601819; AAS99352.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032697; AAH32697.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S67291; AAB29057.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60515; AAA51672.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60516; AAA51673.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A33665; A33665.

RefSeq

NP_000791.1; -.
NP_149127.1; -.
NP_149128.1; -.

UniGene

Hs.483635

3D structure databases

PDB

1AXM; X-ray; 3.00 A; A/B/C/D/E/F=21-155.	[ExPASy / RCSB / EBI]
1DJS; X-ray; 2.40 A; B=21-155.	[ExPASy / RCSB / EBI]
1DZC; NMR; -; A=28-155.	[ExPASy / RCSB / EBI]
1DZD; NMR; -; A=29-155.	[ExPASy / RCSB / EBI]
1E0O; X-ray; 2.80 A; A/C=16-155.	[ExPASy / RCSB / EBI]
1EVT; X-ray; 2.80 A; A/B=22-155.	[ExPASy / RCSB / EBI]
1HKN; X-ray; 2.00 A; A/B/C/D/E/F=17-155.	[ExPASy / RCSB / EBI]
1JQZ; X-ray; 1.65 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1JT3; X-ray; 1.95 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1JT4; X-ray; 1.78 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1JT5; X-ray; 1.85 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1JT7; X-ray; 1.70 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
1JTC; X-ray; 1.70 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
1JY0; X-ray; 1.70 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1K5U; X-ray; 2.00 A; A/B/C=16-155.	[ExPASy / RCSB / EBI]
1K5V; X-ray; 2.10 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1M16; X-ray; 1.70 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1NZK; X-ray; 1.95 A; A/B/C/D=16-152.	[ExPASy / RCSB / EBI]
1P63; X-ray; 1.60 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1PZZ; X-ray; 2.00 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1Q03; X-ray; 2.05 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1Q04; X-ray; 1.80 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1QCT; Model; -; A/D=24-153.	[ExPASy / RCSB / EBI]
1RG8; X-ray; 1.10 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1RML; NMR; -; A=1-155.	[ExPASy / RCSB / EBI]
1RY7; X-ray; 3.20 A; A=1-155.	[ExPASy / RCSB / EBI]
1YTO; X-ray; 2.10 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
1Z2V; X-ray; 1.90 A; A/B=16-155.	[ExPASy / RCSB / EBI]
1Z4S; X-ray; 2.60 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
2AFG; X-ray; 2.00 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
2AQZ; X-ray; 1.85 A; A/B=16-155.	[ExPASy / RCSB / EBI]
2AXM; X-ray; 3.00 A; A/B=21-155.	[ExPASy / RCSB / EBI]
2ERM; NMR; -; B=17-155.	[ExPASy / RCSB / EBI]
2HW9; X-ray; 1.60 A; A/B=16-155.	[ExPASy / RCSB / EBI]
2HWA; X-ray; 1.65 A; A/B=16-155.	[ExPASy / RCSB / EBI]
2HWM; X-ray; 1.60 A; A/B=16-155.	[ExPASy / RCSB / EBI]
2HZ9; X-ray; 1.70 A; A/B=16-155.	[ExPASy / RCSB / EBI]
2NTD; X-ray; 2.52 A; A/B/C/D=16-155.	[ExPASy / RCSB / EBI]
3B9U; X-ray; 1.55 A; A=16-155.	[ExPASy / RCSB / EBI]
3BA4; X-ray; 1.80 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BA5; X-ray; 1.75 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BA7; X-ray; 1.60 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAD; X-ray; 2.00 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAG; X-ray; 1.75 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAH; X-ray; 1.65 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAO; X-ray; 1.55 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAQ; X-ray; 1.80 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAU; X-ray; 1.60 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BAV; X-ray; 1.62 A; A/B=16-155.	[ExPASy / RCSB / EBI]
3BB2; X-ray; 1.50 A; A/B=16-155.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AXM; -.
1DJS; -.
1DZC; -.
1DZD; -.
1E0O; -.
1EVT; -.
1HKN; -.
1JQZ; -.
1JT3; -.
1JT4; -.
1JT5; -.
1JT7; -.
1JTC; -.
1JY0; -.
1K5U; -.
1K5V; -.
1M16; -.
1NZK; -.
1P63; -.
1PZZ; -.
1Q03; -.
1Q04; -.
1QCT; -.
1RG8; -.
1RML; -.
1RY7; -.
1YTO; -.
1Z2V; -.
1Z4S; -.
2AFG; -.
2AQZ; -.
2AXM; -.
2ERM; -.
2HW9; -.
2HWA; -.
2HWM; -.
2HZ9; -.
2NTD; -.
3B9U; -.
3BA4; -.
3BA5; -.
3BA7; -.
3BAD; -.
3BAG; -.
3BAH; -.
3BAO; -.
3BAQ; -.
3BAU; -.
3BAV; -.
3BB2; -.

ModBase

P05230.

Protein-protein interaction databases

DIP

DIP:3787N; -.

IntAct

P05230; -.

Enzyme and pathway databases

Reactome

REACT_9470; Signaling by FGFR.

Polymorphism databases

NIEHS-SNPs

FGF1.

Organism-specific databases

HIX0005267; -.

HGNC:3665; FGF1.

FGF1; Homo sapiens.

CAB017519; -.

131220; gene. [NCBI / EBI]

PharmGKB

PA28105; -.

GeneCards

P05230.

Gene expression databases

ArrayExpress

P05230; -.

CleanEx

HS_FGF1; -.

GermOnline

ENSG00000113578; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0008083;	Molecular function: growth factor activity (traceable author statement from ProtInc).
GO:0009653;	Biological process: anatomical structure morphogenesis (traceable author statement from ProtInc).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
GO:0007275;	Biological process: multicellular organismal development (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.

PANTHER

PTHR11486; IL1_HBGF; 1.

Pfam

PF00167; FGF; 1.
Pfam graphical view of domain structure.

PRINTS

PR00263; HBGFFGF.
PR00262; IL1HBGF.

ProDom

PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00442; FGF; 1.
SMART graphical view of domain structure.

PROSITE

PS00247; HBGF_FGF; 1.

BLOCKS

P05230.

Genome annotation databases

Ensembl

ENSG00000113578; Homo sapiens. [Contig view]

GeneID

2246; -.

KEGG

hsa:2246; -.

Phylogenomic databases

HOGENOM

P05230; -.

HOVERGEN

P05230; -.

Other

DrugBank

DB00686; Pentosan Polysulfate.

P05230; -.

FGF1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Angiogenesis; Developmental protein; Differentiation; Direct protein sequencing; Growth factor; Heparin-binding; Mitogen; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 15`	`15`		`PRO_0000008907`
`CHAIN`	`16 155`	`140`	`Heparin-binding growth factor 1.`	`PRO_0000008908`
`REGION`	`127 143`	`17`	`Heparin-binding.`
`BINDING`	`33 33`		`Heparin.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`VARIANT`	`21 21`	`1`	`G -> E.`	`VAR_021357 [3D]`
`TURN`	`11 13`	`3`
`STRAND`	`23 25`	`3`
`STRAND`	`27 31`	`5`
`TURN`	`32 35`	`4`
`STRAND`	`36 40`	`5`
`STRAND`	`46 49`	`4`
`STRAND`	`59 65`	`7`
`STRAND`	`68 73`	`6`
`TURN`	`74 76`	`3`
`STRAND`	`79 82`	`4`
`STRAND`	`88 93`	`6`
`HELIX`	`96 98`	`3`
`STRAND`	`100 105`	`6`
`TURN`	`106 108`	`3`
`STRAND`	`109 115`	`7`
`HELIX`	`118 120`	`3`
`HELIX`	`135 137`	`3`
`STRAND`	`147 151`	`5`

Sequence information

Length: 155 AA [This is the length of the unprocessed precursor]

Molecular weight: 17460 Da [This is the MW of the unprocessed precursor]

CRC64: F586E8BFB09F1580 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR DRSDQHIQLQ 

        70         80         90        100        110        120 
LSAESVGEVY IKSTETGQYL AMDTDGLLYG SQTPNEECLF LERLEENHYN TYISKKHAEK 

       130        140        150 
NWFVGLKKNG SCKRGPRTHY GQKAILFLPL PVSSD

P05230 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools