[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT PANCREATIC CARCINOMA HIS-493. TISSUE=Fetal brain; DOI=10.1126/science.271.5247.350; PubMed=8553070 [NCBI, ExPASy, EBI, Israel, Japan] Hahn S.A., Schutte M., Shamsul Hoque A.T.M., Moskaluk C.A., da Costa L.T., Rozenblum E., Weinstein C.L., Fischer A., Yeo C.J., Hruban R.H., Kern S.E.; "DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1."; Science 271:350-353(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Placenta; DOI=10.1038/383168a0; PubMed=8774881 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.; "Receptor-associated Mad homologues synergize as effectors of the TGF-beta response."; Nature 383:168-172(1996).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1097/00019606-199704000-00003; PubMed=9098646 [NCBI, ExPASy, EBI, Israel, Japan] Moskaluk C.A., Hruban R.H., Schutte M., Lietman A.S., Smyrk T., Fusaro L., Fusaro R., Lynch J., Yeo C.J., Jackson C.E., Lynch H.T., Kern S.E.; "Genomic sequencing of DPC4 in the analysis of familial pancreatic carcinoma."; Diagn. Mol. Pathol. 6:85-90(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Muscle; 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).
[5]	FUNCTION. PubMed=9389648 [NCBI, ExPASy, EBI, Israel, Japan] Liu F., Pouponnot C., Massague J.; "Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes."; Genes Dev. 11:3157-3167(1997).
[6]	INTERACTION WITH ZNF423. DOI=10.1016/S0092-8674(00)81561-5; PubMed=10660046 [NCBI, ExPASy, EBI, Israel, Japan] Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A., Massague J.; "OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-Smad and Olf signaling pathways."; Cell 100:229-240(2000).
[7]	CHARACTERIZATION OF SAD DOMAIN. DOI=10.1074/jbc.275.3.2115; PubMed=10636916 [NCBI, ExPASy, EBI, Israel, Japan] de Caestecker M.P., Yahata T., Wang D., Parks W.T., Huang S., Hill C.S., Shioda T., Roberts A.B., Lechleider R.J.; "The Smad4 activation domain (SAD) is a proline-rich, p300-dependent transcriptional activation domain."; J. Biol. Chem. 275:2115-2122(2000).
[8]	IDENTIFICATION IN A TERNARY COMPLEX COMPOSED OF STK11 AND STK11IP, AND INTERACTS WITH STK11 AND STK11IP. DOI=10.1093/hmg/10.25.2869; PubMed=11741830 [NCBI, ExPASy, EBI, Israel, Japan] Smith D.P., Rayter S.I., Niederlander C., Spicer J., Jones C.M., Ashworth A.; "LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1."; Hum. Mol. Genet. 10:2869-2877(2001).
[9]	INTERACTION WITH COPS5. DOI=10.1093/embo-reports/kvf024; PubMed=11818334 [NCBI, ExPASy, EBI, Israel, Japan] Wan M., Cao X., Wu Y., Bai S., Wu L., Shi X., Wang N., Cao X.; "Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation."; EMBO Rep. 3:171-176(2002).
[10]	INTERACTION WITH DACH1. DOI=10.1074/jbc.M310021200; PubMed=14525983 [NCBI, ExPASy, EBI, Israel, Japan] Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K., Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.; "DACH1 inhibits transforming growth factor-beta signaling through binding Smad4."; J. Biol. Chem. 278:51673-51684(2003).
[11]	INTERACTION WITH ZNF521. DOI=10.1182/blood-2003-07-2388; PubMed=14630787 [NCBI, ExPASy, EBI, Israel, Japan] Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N., De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M., Morrone G., Venuta S.; "Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse Evi3, is highly expressed in primitive human hematopoietic cells."; Blood 103:2062-2070(2004).
[12]	INTERACTION WITH TRIM33. DOI=10.1016/j.cell.2005.01.033; PubMed=15820681 [NCBI, ExPASy, EBI, Israel, Japan] Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M., Rugge M., Piccolo S.; "Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase."; Cell 121:87-99(2005).
[13]	INTERACTION WITH USP9X, UBIQUITINATION, AND MUTAGENESIS OF LYS-519. DOI=10.1016/j.cell.2008.10.051; PubMed=19135894 [NCBI, ExPASy, EBI, Israel, Japan] Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L., Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L., Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.; "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination."; Cell 136:123-135(2009).
[14]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 319-543. DOI=10.1038/40431; PubMed=9214508 [NCBI, ExPASy, EBI, Israel, Japan] Shi Y., Hata A., Lo R.S., Massague J., Pavletich N.P.; "A structural basis for mutational inactivation of the tumour suppressor Smad4."; Nature 388:87-93(1997).
[15]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 285-552. DOI=10.1016/S0969-2126(00)88340-9; PubMed=10647180 [NCBI, ExPASy, EBI, Israel, Japan] Qin B., Lam S.S., Lin K.; "Crystal structure of a transcriptionally active Smad4 fragment."; Structure 7:1493-1503(1999).
[16]	X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) OF 273-552. DOI=10.1038/84995; PubMed=11224571 [NCBI, ExPASy, EBI, Israel, Japan] Chacko B.M., Qin B., Correia J.J., Lam S.S., de Caestecker M.P., Lin K.; "The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization."; Nat. Struct. Biol. 8:248-253(2001).
[17]	REVIEW. DOI=10.1146/annurev.biochem.67.1.753; PubMed=9759503 [NCBI, ExPASy, EBI, Israel, Japan] Massague J.; "TGF-beta signal transduction."; Annu. Rev. Biochem. 67:753-791(1998).
[18]	REVIEW. DOI=10.1016/S1359-6101(99)00012-X; PubMed=10647776 [NCBI, ExPASy, EBI, Israel, Japan] Verschueren K., Huylebroeck D.; "Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells."; Cytokine Growth Factor Rev. 10:187-199(1999).
[19]	REVIEW. DOI=10.1016/S1359-6101(99)00024-6; PubMed=10708948 [NCBI, ExPASy, EBI, Israel, Japan] Wrana J.L., Attisano L.; "The Smad pathway."; Cytokine Growth Factor Rev. 11:5-13(2000).
[20]	REVIEW. DOI=10.1016/S1359-6101(99)00025-8; PubMed=10708949 [NCBI, ExPASy, EBI, Israel, Japan] Miyazono K.; "TGF-beta signaling by Smad proteins."; Cytokine Growth Factor Rev. 11:15-22(2000).
[21]	VARIANT JPS CYS-361. DOI=10.1093/hmg/7.12.1907; PubMed=9811934 [NCBI, ExPASy, EBI, Israel, Japan] Houlston R., Bevan S., Williams A., Young J., Dunlop M., Rozen P., Eng C., Markie D., Woodford-Richens K., Rodriguez-Bigas M.A., Leggett B., Neale K., Phillips R., Sheridan E., Hodgson S., Iwama T., Eccles D., Bodmer W., Tomlinson I.; "Mutations in DPC4 (SMAD4) cause juvenile polyposis syndrome, but only account for a minority of cases."; Hum. Mol. Genet. 7:1907-1912(1998).
[22]	VARIANTS JPS GLY-330 AND ARG-352. PubMed=12417513 [NCBI, ExPASy, EBI, Israel, Japan] Sayed M.G., Ahmed A.F., Ringold J.R., Anderson M.E., Bair J.L., Mitros F.A., Lynch H.T., Tinley S.T., Petersen G.M., Giardiello F.M., Vogelstein B., Howe J.R.; "Germline SMAD4 or BMPR1A mutations and phenotype of juvenile polyposis."; Ann. Surg. Oncol. 9:901-906(2002).
[23]	VARIANTS JP/HHT ARG-352 AND ASP-386. DOI=10.1016/S0140-6736(04)15732-2; PubMed=15031030 [NCBI, ExPASy, EBI, Israel, Japan] Gallione C.J., Repetto G.M., Legius E., Rustgi A.K., Schelley S.L., Tejpar S., Mitchell G., Drouin E., Westermann C.J.J., Marchuk D.A.; "A combined syndrome of juvenile polyposis and hereditary haemorrhagic telangiectasia associated with mutations in MADH4 (SMAD4)."; Lancet 363:852-859(2004).
[24]	VARIANTS [LARGE SCALE ANALYSIS] SER-130; ASN-351 AND HIS-361. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Common mediator of signal transduction by TGF-beta (transforming growth factor) superfamily; SMAD4 is the common SMAD (co-SMAD). Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. May act as a tumor suppressor.
SUBUNIT: May form trimers with receptor-regulated SMAD (R-SMAD). Found in a ternary complex composed of SMAD4, STK11 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11, STK11IP and TRIM33. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with USP9X.
INTERACTION:
P17676:CEBPB; NbExp=1; IntAct=EBI-347263, EBI-969696;
Q9UI36:DACH1; NbExp=3; IntAct=EBI-347263, EBI-347111;
P12755:SKI; NbExp=2; IntAct=EBI-347263, EBI-347281;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with R-SMAD.
PTM: Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade.
DISEASE: Defects in SMAD4 are a cause of pancreatic carcinoma [MIM:260350].
DISEASE: Defects in SMAD4 are a cause of juvenile polyposis syndrome (JPS) [MIM:174900]; also known as juvenile intestinal polyposis (JIP). JPS is an autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.
DISEASE: Defects in SMAD4 are a cause of juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome (JP/HHT) [MIM:175050]. JP/HHT syndrome phenotype consists of the coexistence of juvenile polyposis (JIP) and hereditary hemorrhagic telangiectasia (HHT) [MIM:187300] in a single individual. JIP and HHT are autosomal dominant disorders with distinct and non-overlapping clinical features. The former, an inherited gastrointestinal malignancy predisposition, is caused by mutations in SMAD4 or BMPR1A, and the latter is a vascular malformation disorder caused by mutations in ENG or ACVRL1. All four genes encode proteins involved in the transforming-growth-factor-signaling pathway. Although there are reports of patients and families with phenotypes of both disorders combined, the genetic aetiology of this association is unknown.
DISEASE: Defects in SMAD4 may be a cause of colorectal cancer (CRC) [MIM:114500].
SIMILARITY: Belongs to the dwarfin/SMAD family.
SIMILARITY: Contains 1 MH1 (MAD homology 1) domain.
SIMILARITY: Contains 1 MH2 (MAD homology 2) domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/SMAD4ID371.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SMAD4";.

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

AF045447; AAC03051.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045438; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045439; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045440; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045441; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045442; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045443; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045444; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045445; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045446; AAC03051.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U44378; AAA91041.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002379; AAH02379.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00013404; -.

S71811; S71811.

NP_005350.1; -.

3D structure databases

PDB

1DD1; X-ray; 2.62 A; A/B/C=285-552.	[ExPASy / RCSB / EBI]
1G88; X-ray; 3.00 A; A/B/C=285-552.	[ExPASy / RCSB / EBI]
1MR1; X-ray; 2.85 A; A/B=319-552.	[ExPASy / RCSB / EBI]
1U7F; X-ray; 2.60 A; B=314-552.	[ExPASy / RCSB / EBI]
1U7V; X-ray; 2.70 A; B=314-549.	[ExPASy / RCSB / EBI]
1YGS; X-ray; 2.10 A; A=319-552.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DD1; -.
1G88; -.
1MR1; -.
1U7F; -.
1U7V; -.
1YGS; -.

DisProt

DP00464; -.

ModBase

Q13485.

Protein-protein interaction databases

IntAct

Q13485; 8.

PTM databases

PhosphoSite

Q13485; -.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway; BMP receptor signaling.
wnt_canonical_pathway; Canonical Wnt signaling pathway.
hif1_tfpathway; HIF-1-alpha transcription factor network.
smad2_3pathway; Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
tgfbrpathway; TGF-beta receptor signaling.

Reactome

REACT_12034; Signaling by BMP.
REACT_6844; Signaling by TGF beta.

Organism-specific databases

GC18P046810; -.

HIX0014453; -.

HGNC:6770; SMAD4.

CAB002312; -.

114500; phenotype. [NCBI / EBI]
174900; phenotype. [NCBI / EBI]
175050; phenotype. [NCBI / EBI]
260350; phenotype. [NCBI / EBI]
600993; gene. [NCBI / EBI]

Orphanet

2929; Juvenile gastrointestinal polyposis.
1333; Pancreatic carcinoma, familial.

PharmGKB

PA30527; -.

Gene expression databases

Q13485; -.

Q13485; -.

HS_SMAD4; -.

ENSG00000141646; Homo sapiens.

Ontologies

GO:0032444;	Cellular component: activin responsive factor complex (inferred from direct assay from UniProtKB).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0010843;	Molecular function: promoter binding (inferred from direct assay from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0070412;	Molecular function: R-SMAD binding (inferred from physical interaction from UniProtKB).
GO:0003700;	Molecular function: transcription factor activity (inferred from electronic annotation from InterPro).
GO:0030616;	Molecular function: transforming growth factor beta receptor, common-partner cytoplasmic mediator activity (inferred from direct assay from UniProtKB).
GO:0030509;	Biological process: BMP signaling pathway (inferred from direct assay from UniProtKB).
GO:0030308;	Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0045892;	Biological process: negative regulation of transcription, DNA-dependent (inferred from direct assay from UniProtKB).
GO:0060021;	Biological process: palate development (inferred from sequence or structural similarity from UniProtKB).
GO:0010718;	Biological process: positive regulation of epithelial to mesenchymal transition (inferred from sequence or structural similarity from UniProtKB).
GO:0010862;	Biological process: positive regulation of pathway-restricted SMAD protein phosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0060391;	Biological process: positive regulation of SMAD protein nuclear translocation (inferred from sequence or structural similarity from UniProtKB).
GO:0032909;	Biological process: regulation of transforming growth factor-beta2 production (inferred from mutant phenotype from UniProtKB).
GO:0001666;	Biological process: response to hypoxia (inferred from mutant phenotype from UniProtKB).
GO:0007183;	Biological process: SMAD protein complex assembly (inferred from direct assay from UniProtKB).
GO:0060395;	Biological process: SMAD protein signal transduction (inferred from direct assay from UniProtKB).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013790; Dwarfin.
IPR003619; MAD_homology1_Dwarfin-type.
IPR013019; MAD_homology_MH1.
IPR017855; SMAD_dom-like.
IPR001132; SMAD_dom_Dwarfin-type.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.520.10; MAD_MH1; 1.
G3DSA:2.60.200.10; MH2_Dwarfin-type; 1.

PANTHER

PTHR13703; Dwarfin; 1.

Pfam

PF03165; MH1; 1.
PF03166; MH2; 1.
Pfam graphical view of domain structure.

SMART

SM00523; DWA; 1.
SM00524; DWB; 1.
SMART graphical view of domain structure.

PROSITE

PS51075; MH1; 1.
PS51076; MH2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q13485; -.

PRIDE

Q13485; -.

Genome annotation databases

Ensembl

ENSG00000141646; Homo sapiens. [Contig view]

GeneID

4089; -.

KEGG

hsa:4089; -.

Phylogenomic databases

HOGENOM

Q13485; -.

HOVERGEN

Q13485; -.

OMA

Q13485; AQPATYH.

Other

16030; -.

SMAD4; Homo sapiens.

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

Keywords

3D-structure; Cytoplasm; Disease mutation; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Transcription; Transcription regulation; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 552`	`552`	`Mothers against decapentaplegic homolog 4.`	`PRO_0000090861`
`DOMAIN`	`18 142`	`125`	`MH1.`
`DOMAIN`	`323 552`	`230`	`MH2.`
`REGION`	`275 320`	`46`	`SAD.`
`COMPBIAS`	`451 466`	`16`	`Poly-Ala.`
`CROSSLNK`	`519 519`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`VARIANT`	`101 101`	`1`	`W -> G (in dbSNP:rs2229083 [NCBI]).`	`VAR_052022`
`VARIANT`	`130 130`	`1`	`P -> S (in a colorectal cancer sample; somatic mutation).`	`VAR_036475`
`VARIANT`	`330 330`	`1`	`E -> G (in JPS).`	`VAR_022833 [3D]`
`VARIANT`	`351 351`	`1`	`D -> N (in a colorectal cancer sample; somatic mutation).`	`VAR_036476 [3D]`
`VARIANT`	`352 352`	`1`	`G -> R (in JP/HHT and JPS).`	`VAR_019571 [3D]`
`VARIANT`	`361 361`	`1`	`R -> C (in JPS).`	`VAR_019572 [3D]`
`VARIANT`	`361 361`	`1`	`R -> H (in a colorectal cancer sample; somatic mutation).`	`VAR_036477 [3D]`
`VARIANT`	`386 386`	`1`	`G -> D (in JP/HHT).`	`VAR_019573 [3D]`
`VARIANT`	`493 493`	`1`	`D -> H (in pancreatic carcinoma).`	`VAR_011380 [3D]`
`MUTAGEN`	`519 519`		`K->R: Abolishes ubiquitination.`
`STRAND`	`288 291`	`4`
`STRAND`	`321 330`	`10`
`STRAND`	`333 342`	`10`
`STRAND`	`346 353`	`8`
`STRAND`	`359 363`	`5`
`HELIX`	`374 380`	`7`
`TURN`	`381 385`	`5`
`STRAND`	`387 392`	`6`
`TURN`	`393 395`	`3`
`STRAND`	`396 401`	`6`
`STRAND`	`403 405`	`3`
`STRAND`	`407 410`	`4`
`HELIX`	`412 416`	`5`
`TURN`	`417 419`	`3`
`STRAND`	`427 429`	`3`
`STRAND`	`434 438`	`5`
`HELIX`	`440 454`	`15`
`HELIX`	`493 497`	`5`
`STRAND`	`500 506`	`7`
`HELIX`	`518 520`	`3`
`STRAND`	`521 529`	`9`
`HELIX`	`530 541`	`12`

Sequence information

Length: 552 AA [This is the length of the unprocessed precursor]

Molecular weight: 60439 Da [This is the MW of the unprocessed precursor]

CRC64: 7EE3C4647712DA90 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK KDELDSLITA 

        70         80         90        100        110        120 
ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR WPDLHKNELK HVKYCQYAFD 

       130        140        150        160        170        180 
LKCDSVCVNP YHYERVVSPG IDLSGLTLQS NAPSSMMVKD EYVHDFEGQP SLSTEGHSIQ 

       190        200        210        220        230        240 
TIQHPPSNRA STETYSTPAL LAPSESNATS TANFPNIPVA STSQPASILG GSHSEGLLQI 

       250        260        270        280        290        300 
ASGPQPGQQQ NGFTGQPATY HHNSTTTWTG SRTAPYTPNL PHHQNGHLQH HPPMPPHPGH 

       310        320        330        340        350        360 
YWPVHNELAF QPPISNHPAP EYWCSIAYFE MDVQVGETFK VPSSCPIVTV DGYVDPSGGD 

       370        380        390        400        410        420 
RFCLGQLSNV HRTEAIERAR LHIGKGVQLE CKGEGDVWVR CLSDHAVFVQ SYYLDREAGR 

       430        440        450        460        470        480 
APGDAVHKIY PSAYIKVFDL RQCHRQMQQQ AATAQAAAAA QAAAVAGNIP GPGSVGGIAP 

       490        500        510        520        530        540 
AISLSAAAGI GVDDLRRLCI LRMSFVKGWG PDYPRQSIKE TPCWIEIHLH RALQLLDEVL 

       550 
HTMPIADPQP LD

Q13485 in FASTA format

View entry in raw text format (no links)
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	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