[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 181-196; 815-820; 826-836; 862-879; 925-936 AND 1004-1013, AND SUBUNIT. STRAIN=ATCC 26786 / X2180-1A; PubMed=2139027 [NCBI, ExPASy, EBI, Israel, Japan] Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y.; "Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae."; J. Biol. Chem. 265:6726-6733(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/yea.320111007; PubMed=8533471 [NCBI, ExPASy, EBI, Israel, Japan] Verhasselt P., Voet M., Volckaert G.; "New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."; Yeast 11:961-966(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan] Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; Nature 387:75-78(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. STRAIN=ATCC 208353 / W303-1A; PubMed=1656215 [NCBI, ExPASy, EBI, Israel, Japan] Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.; "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."; Mol. Cell. Biol. 11:4876-4884(1991).
[5]	PROTEIN SEQUENCE OF 2-10; 52-63; 115-136; 173-178; 181-207; 220-239; 264-272; 770-784; 804-814; 826-842; 853-861; 918-937; 940-959; 1004-1014 AND 1058-1065, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. Bienvenut W.V., Peters C.; Submitted (OCT-2005) to UniProtKB.
[6]	PROTEIN SEQUENCE OF 2-6, CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF CYS-284; HIS-362; ASN-737 AND CYS-738, AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 274-747. DOI=10.1006/jmbi.2001.5357; PubMed=11884132 [NCBI, ExPASy, EBI, Israel, Japan] Mizutani R., Nogami S., Kawasaki M., Ohya Y., Anraku Y., Satow Y.; "Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides."; J. Mol. Biol. 316:919-929(2002).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-1071. PubMed=2905423 [NCBI, ExPASy, EBI, Israel, Japan] Shih C.K., Wagner R., Feinstein S., Kanik-Ennulat C., Neff N.; "A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth."; Mol. Cell. Biol. 8:3094-3103(1988).
[8]	PROTEIN SPLICING. DOI=10.1126/science.2146742; PubMed=2146742 [NCBI, ExPASy, EBI, Israel, Japan] Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H.; "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase."; Science 250:651-657(1990).
[9]	MUTAGENESIS OF CYS-284 AND CYS-738. DOI=10.1016/0006-291X(92)92347-Z; PubMed=1417861 [NCBI, ExPASy, EBI, Israel, Japan] Hirata R., Anraku Y.; "Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing."; Biochem. Biophys. Res. Commun. 188:40-47(1992).
[10]	SELF-SPLICING MECHANISM. PubMed=8508780 [NCBI, ExPASy, EBI, Israel, Japan] Cooper A.A., Chen Y.-J., Lindorfer M.A., Stevens T.H.; "Protein splicing of the yeast TFP1 intervening protein sequence: a model for self-excision."; EMBO J. 12:2575-2583(1993).
[11]	FUNCTION OF VDE. DOI=10.1038/357301a0; PubMed=1534148 [NCBI, ExPASy, EBI, Israel, Japan] Gimble F.S., Thorner J.; "Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae."; Nature 357:301-306(1992).
[12]	INTERACTION WITH RAV1 AND RAV2. DOI=10.1038/35070067; PubMed=11283612 [NCBI, ExPASy, EBI, Israel, Japan] Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.; "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."; Nat. Cell Biol. 3:384-391(2001).
[13]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[14]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[15]	REVIEW. DOI=10.1016/0960-9822(92)90336-9; PubMed=15335920 [NCBI, ExPASy, EBI, Israel, Japan] Grivell L.A.; "Homing in on an endosymbiotic endonuclease."; Curr. Biol. 2:450-452(1992).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan] Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.; "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."; Mol. Cell. Proteomics 4:310-327(2005).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-376, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan] Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-131; SER-448; THR-771; SER-777; SER-845; SER-858 AND SER-928, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[19]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PI-SCE I. DOI=10.1016/S0092-8674(00)80237-8; PubMed=9160747 [NCBI, ExPASy, EBI, Israel, Japan] Duan X., Gimble F.S., Quiocho F.A.; "Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity."; Cell 89:555-564(1997).
[20]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PI-SCE I. DOI=10.1074/jbc.275.4.2705; PubMed=10644733 [NCBI, ExPASy, EBI, Israel, Japan] Hu D., Crist M., Duan X., Quiocho F.A., Gimble F.S.; "Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking."; J. Biol. Chem. 275:2705-2712(2000).
[21]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-741, AND MUTAGENESIS OF CYS-284 AND ASN-737. DOI=10.1074/jbc.275.22.16408; PubMed=10828056 [NCBI, ExPASy, EBI, Israel, Japan] Poland B.W., Xu M.-Q., Quiocho F.A.; "Structural insights into the protein splicing mechanism of PI-SceI."; J. Biol. Chem. 275:16408-16413(2000).
[22]	X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 284-465. DOI=10.1093/nar/gkf523; PubMed=12235380 [NCBI, ExPASy, EBI, Israel, Japan] Werner E., Wende W., Pingoud A., Heinemann U.; "High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI."; Nucleic Acids Res. 30:3962-3971(2002).

Comments

FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.
FUNCTION: PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.
CATALYTIC ACTIVITY: ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out).
SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.
INTERACTION:
P13434:HAP3; NbExp=1; IntAct=EBI-20245, EBI-8157;
P47104:RAV1; NbExp=1; IntAct=EBI-20245, EBI-25471;
SUBCELLULAR LOCATION: Endomembrane system. Vacuole membrane (Probable). Note=Membranes of various intracellular acidic compartments.
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
MISCELLANEOUS: Present with 199895 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the ATPase alpha/beta chains family.
SIMILARITY: Contains 1 DOD-type homing endonuclease domain.
WEB RESOURCE: Name=Description of Sce VMA in Inbase; URL="http://tools.neb.com/inbase/intein.php?name=Sce+VMA";.

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

J05409; AAA34664.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X83276; CAA58261.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74233; CAA98760.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74233; CAA98761.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74233; CAA98762.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X58857; CAA41657.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21609; AAB63978.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35746; PXBYVA.

RefSeq

NP_010096.1; -.

3D structure databases

PDB

1DFA; X-ray; 2.00 A; A=284-737.	[ExPASy / RCSB / EBI]
1EF0; X-ray; 2.10 A; A/B=285-741.	[ExPASy / RCSB / EBI]
1GPP; X-ray; 1.35 A; A=284-736.	[ExPASy / RCSB / EBI]
1JVA; X-ray; 2.10 A; A/B=274-747.	[ExPASy / RCSB / EBI]
1LWS; X-ray; 3.50 A; A=284-737.	[ExPASy / RCSB / EBI]
1LWT; X-ray; 3.20 A; A=284-737.	[ExPASy / RCSB / EBI]
1UM2; X-ray; 2.90 A; A/B=285-737, C/D=274-747.	[ExPASy / RCSB / EBI]
1VDE; X-ray; 2.40 A; A/B=284-737.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DFA; -.
1EF0; -.
1GPP; -.
1JVA; -.
1LWS; -.
1LWT; -.
1UM2; -.
1VDE; -.

ModBase

P17255.

Protein-protein interaction databases

DIP

DIP:2293N; -.

IntAct

P17255; 79.

Protein family/group databases

REBASE

2615; PI-SceI.

TCDB

3.A.2.2.3; H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Enzyme and pathway databases

BRENDA

3.6.3.14; 250.

Organism-specific databases

YDL185w; -.

S000002344; TFP1.

Gene expression databases

ArrayExpress

P17255; -.

GermOnline

YDL185W; Saccharomyces cerevisiae.

Ontologies

GO:0012505;	Cellular component: endomembrane system (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000329;	Cellular component: fungal-type vacuole membrane (inferred from direct assay from UniProtKB).
GO:0000221;	Cellular component: vacuolar proton-transporting V-type ATPase, V1 domain (traceable author statement from SGD).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004520;	Molecular function: endodeoxyribonuclease activity (traceable author statement from SGD).
GO:0046933;	Molecular function: hydrogen ion transporting ATP synthase activity, rotational mechanism (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0046961;	Molecular function: proton-transporting ATPase activity, rotational mechanism (traceable author statement from SGD).
GO:0015986;	Biological process: ATP synthesis coupled proton transport (inferred from electronic annotation from InterPro).
GO:0016539;	Biological process: intein-mediated protein splicing (inferred from electronic annotation from InterPro).
GO:0006314;	Biological process: intron homing (traceable author statement from SGD).
GO:0007035;	Biological process: vacuolar acidification (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR020003; ATPase_F1/V1/A1_a/bsu_AS.
IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR003586; Hedgehog_hint_C.
IPR003587; Hedgehog_hint_N.
IPR007869; Hom_end.
IPR007868; Hom_end_hint.
IPR004042; Intein_endonuc.
IPR006141; Intein_splicing_site.
Graphical view of domain structure.

Pfam

PF00006; ATP-synt_ab; 1.
PF00306; ATP-synt_ab_C; 1.
PF02874; ATP-synt_ab_N; 1.
PF05204; Hom_end; 2.
PF05203; Hom_end_hint; 1.
Pfam graphical view of domain structure.

SMART

SM00305; HintC; 1.
SM00306; HintN; 1.
SMART graphical view of domain structure.

PROSITE

PS00152; ATPASE_ALPHA_BETA; 1.
PS50818; INTEIN_C_TER; 1.
PS50819; INTEIN_ENDONUCLEASE; 1.
PS50817; INTEIN_N_TER; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P17255; -.

PRIDE

P17255; -.

Genome annotation databases

Ensembl

YDL185W; Saccharomyces cerevisiae. [Contig view]

851342; -.

Z71256_GR; YDL185W.

sce:YDL185W; -.

fig|4932.3.peg.830; -.

Phylogenomic databases

HOGENOM

P17255; -.

OMA

P17255; HNCGERG.

Other

968420; -.

P17255; -.

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

Keywords

3D-structure; Acetylation; ATP-binding; Autocatalytic cleavage; Complete proteome; Direct protein sequencing; DNA-binding; Endonuclease; Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Membrane; Nuclease; Nucleotide-binding; Phosphoprotein; Protein splicing; Transport; Vacuole.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 283`	`282`	`V-type proton ATPase catalytic subunit A, 1st part.`	`PRO_0000002458`
`CHAIN`	`284 737`	`454`	`Endonuclease PI-SceI.`	`PRO_0000002459`
`CHAIN`	`738 1071`	`334`	`V-type proton ATPase catalytic subunit A, 2nd part.`	`PRO_0000002460`
`DOMAIN`	`494 642`	`149`	`DOD-type homing endonuclease.`
`NP_BIND`	`257 264`	`8`	`ATP (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`16 16`		`Phosphoserine.`
`MOD_RES`	`131 131`		`Phosphothreonine.`
`MOD_RES`	`166 166`		`Phosphoserine.`
`MOD_RES`	`376 376`		`Phosphoserine.`
`MOD_RES`	`448 448`		`Phosphoserine.`
`MOD_RES`	`771 771`		`Phosphothreonine.`
`MOD_RES`	`777 777`		`Phosphoserine.`
`MOD_RES`	`845 845`		`Phosphoserine.`
`MOD_RES`	`858 858`		`Phosphoserine.`
`MOD_RES`	`928 928`		`Phosphoserine.`
`MUTAGEN`	`284 284`		`C->S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE.`
`MUTAGEN`	`362 362`		`H->N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE.`
`MUTAGEN`	`737 737`		`N->S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE.`
`MUTAGEN`	`738 738`		`C->S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE.`
`CONFLICT`	`875 875`		`G -> D (in Ref. 7; AAB63978).`
`STRAND`	`290 293`	`4`
`STRAND`	`298 300`	`3`
`HELIX`	`301 303`	`3`
`STRAND`	`309 312`	`4`
`STRAND`	`315 322`	`8`
`STRAND`	`325 335`	`11`
`STRAND`	`355 359`	`5`
`STRAND`	`363 369`	`7`
`STRAND`	`372 379`	`8`
`STRAND`	`382 396`	`15`
`STRAND`	`402 414`	`13`
`HELIX`	`415 417`	`3`
`HELIX`	`420 431`	`12`
`STRAND`	`434 443`	`10`
`HELIX`	`444 449`	`6`
`HELIX`	`452 457`	`6`
`STRAND`	`459 462`	`4`
`HELIX`	`467 469`	`3`
`STRAND`	`474 476`	`3`
`STRAND`	`478 483`	`6`
`STRAND`	`485 487`	`3`
`HELIX`	`488 501`	`14`
`HELIX`	`516 528`	`13`
`HELIX`	`570 575`	`6`
`STRAND`	`579 584`	`6`
`HELIX`	`588 591`	`4`
`HELIX`	`595 609`	`15`
`STRAND`	`619 625`	`7`
`HELIX`	`627 639`	`13`
`STRAND`	`643 650`	`8`
`HELIX`	`654 656`	`3`
`STRAND`	`661 669`	`9`
`HELIX`	`672 678`	`7`
`TURN`	`684 686`	`3`
`STRAND`	`700 702`	`3`
`STRAND`	`704 714`	`11`
`STRAND`	`725 729`	`5`
`STRAND`	`733 736`	`4`

Sequence information

Length: 1071 AA [This is the length of the unprocessed precursor]

Molecular weight: 118637 Da [This is the MW of the unprocessed precursor]

CRC64: 2A4C65D2F59426FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE 

        70         80         90        100        110        120 
VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEES 

       130        140        150        160        170        180 
QSIYIPRGID TPALDRTIKW QFTPGKFQVG DHISGGDIYG SVFENSLISS HKILLPPRSR 

       190        200        210        220        230        240 
GTITWIAPAG EYTLDEKILE VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV 

       250        260        270        280        290        300 
LDALFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC 

       310        320        330        340        350        360 
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV PELLKFTCNA 

       370        380        390        400        410        420 
THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG RIVELVKEVS KSYPISEGPE 

       430        440        450        460        470        480 
RANELVESYR KASNKAYFEW TIEARDLSLL GSHVRKATYQ TYAPILYEND HFFDYMQKSK 

       490        500        510        520        530        540 
FHLTIEGPKV LAYLLGLWIG DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE 

       550        560        570        580        590        600 
PQVAKTVNLY SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET 

       610        620        630        640        650        660 
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP AKVDMNGTKH 

       670        680        690        700        710        720 
KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR GFYFELQELK EDDYYGITLS 

       730        740        750        760        770        780 
DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM EFPELYTEMS GTKEPIMKRT TLVANTSNMP 

       790        800        810        820        830        840 
VAAREASIYT GITLAEYFRD QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG 

       850        860        870        880        890        900 
AKLASFYERA GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL 

       910        920        930        940        950        960 
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL EQVVQLVGKS 

       970        980        990       1000       1010       1020 
ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD MMRAFISYHD EAQKAVANGA 

      1030       1040       1050       1060       1070 
NWSKLADSTG DVKHAVSSSK FFEPSRGEKE VHGEFEKLLS TMQERFAEST D

P17255 in FASTA format

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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