[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 28383 / FL100 / VTT C-80102; DOI=10.1016/0378-1119(89)90092-9; PubMed=2570735 [NCBI, ExPASy, EBI, Israel, Japan] Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S.; "Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex."; Gene 79:59-70(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan] Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; EMBO J. 15:2031-2049(1996).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-510. STRAIN=ATCC 28383 / FL100 / VTT C-80102; DOI=10.1007/BF00331595; PubMed=3039294 [NCBI, ExPASy, EBI, Israel, Japan] Souciet J.-L., Potier S., Hubert J.-C., Lacroute F.; "Nucleotide sequence of the pyrimidine specific carbamoyl phosphate synthetase, a part of the yeast multifunctional protein encoded by the URA2 gene."; Mol. Gen. Genet. 207:314-319(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/(SICI)1097-0061(199611)12:14<1471::AID-YEA30>3.3.CO;2-W; PubMed=8948101 [NCBI, ExPASy, EBI, Israel, Japan] Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.; "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta elements and a Ty4 transposon."; Yeast 12:1471-1474(1996).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-117. STRAIN=ATCC 201390 / BY4743; DOI=10.1073/pnas.0610354104; PubMed=17244705 [NCBI, ExPASy, EBI, Israel, Japan] Juneau K., Palm C., Miranda M., Davis R.W.; "High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing."; Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 14-119. STRAIN=ATCC 201390 / BY4743; DOI=10.1101/gr.6049107; PubMed=17351133 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Hesselberth J.R., Fields S.; "Genome-wide identification of spliced introns using a tiling microarray."; Genome Res. 17:503-509(2007).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-2214. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/(SICI)1097-0061(19960630)12:8<787::AID-YEA954>3.3.CO;2-W; PubMed=8813765 [NCBI, ExPASy, EBI, Israel, Japan] Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.; "Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."; Yeast 12:787-797(1996).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 838-877. DOI=10.1007/s004380050415; PubMed=9150260 [NCBI, ExPASy, EBI, Israel, Japan] Akada R., Yamamoto J., Yamashita I.; "Screening and identification of yeast sequences that cause growth inhibition when overexpressed."; Mol. Gen. Genet. 254:267-274(1997).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1268-2214. PubMed=2498313 [NCBI, ExPASy, EBI, Israel, Japan] Nagy M., le Gouar M., Potier S., Souciet J.-L., Herve G.; "The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activity and nuclear localization."; J. Biol. Chem. 264:8366-8374(1989).
[10]	PROTEIN SEQUENCE OF 1855-1874, AND PHOSPHORYLATION AT SER-1857. PubMed=1977585 [NCBI, ExPASy, EBI, Israel, Japan] Denis-Duphil M., Lecaer J.-P., Hardie D.G., Carrey E.A.; "Yeast carbamoyl-phosphate-synthetase--aspartate-transcarbamylase multidomain protein is phosphorylated in vitro by cAMP-dependent protein kinase."; Eur. J. Biochem. 193:581-587(1990).
[11]	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).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, 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).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND MASS SPECTROMETRY. DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.; "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."; J. Proteome Res. 6:1190-1197(2007).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, 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).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1859, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan] Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1452; TYR-1453; SER-1553; SER-1857; THR-1859; SER-1986 AND SER-2142, 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).

Comments

FUNCTION: This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6 .
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6 .
INTERACTION:
Q04264:PDS5; NbExp=1; IntAct=EBI-14372, EBI-13077;
DOMAIN: The DHOase domain is defective.
MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
MISCELLANEOUS: Present with 11000 molecules/cell in log phase SD medium.
SIMILARITY: In the central section; belongs to the DHOase family.
SIMILARITY: Contains 2 ATP-grasp domains.
SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.

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

M27174; AAA68280.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49405; CAA89425.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05553; CAA29068.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF123133; ABM97477.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ881452; ABI95879.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X87371; CAA60825.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D28139; BAA05680.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04711; AAA35198.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56911; QZBYU2.

RefSeq

NP_012405.1; -.

3D structure databases

HSSP

P77918; 1ML4. [HSSP ENTRY / PDB]

ModBase

P07259.

Protein-protein interaction databases

IntAct

P07259; -.

Organism-specific databases

YJL130c; -.

S000003666; URA2.

Gene expression databases

ArrayExpress

P07259; -.

GermOnline

YJL130C; Saccharomyces cerevisiae.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from direct assay from SGD).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from direct assay from SGD).
GO:0004088;	Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from mutant phenotype from SGD).
GO:0006541;	Biological process: glutamine metabolic process (inferred from direct assay from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR006220; Anth_synthII.
IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR001317; CarbamoylP_synth_GATase.
IPR005483; CarbamoylP_synth_lsu.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR006275; CarbamoylP_synth_lsu_Gln-dep.
IPR005481; CarbamoylP_synth_lsu_N.
IPR005480; CarbamoylP_synth_lsu_oligo.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
IPR011607; MGS.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
G3DSA:3.40.50.20; Pre-ATP_grasp; 2.

Pfam

PF00289; CPSase_L_chain; 2.
PF02786; CPSase_L_D2; 2.
PF02787; CPSase_L_D3; 1.
PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
PF02142; MGS; 1.
PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00097; ANTSNTHASEII.
PR00100; AOTCASE.
PR00101; ATCASE.
PR00098; CPSASE.
PR00099; CPSGATASE.
PR00096; GATASE.

TIGRFAMs

TIGR00670; asp_carb_tr; 1.
TIGR01369; CPSaseII_lrg; 1.
TIGR01368; CPSaseIIsmall; 1.

PROSITE

PS50975; ATP_GRASP; 2.
PS00097; CARBAMOYLTRANSFERASE; 1.
PS00866; CPSASE_1; 2.
PS00867; CPSASE_2; 2.
PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P07259.

Proteomic databases

PeptideAtlas

P07259; -.

Genome annotation databases

Ensembl

YJL130C; Saccharomyces cerevisiae. [Contig view]

853311; -.

Y13136_GR; YJL130C.

sce:YJL130C; -.

fig|4932.3.peg.3372; -.

Phylogenomic databases

HOGENOM

P07259; -.

Other

P07259; -.

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

Keywords

Complete proteome; Direct protein sequencing; Ligase; Multifunctional enzyme; Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2214`	`2214`	`Protein URA1.`	`PRO_0000199511`
`DOMAIN`	`228 413`	`186`	`Glutamine amidotransferase type-1.`
`DOMAIN`	`562 754`	`193`	`ATP-grasp 1.`
`DOMAIN`	`1099 1290`	`192`	`ATP-grasp 2.`
`REGION`	`1 400`	`400`	`GATase (Glutamine amidotransferase).`
`REGION`	`401 440`	`40`	`Linker.`
`REGION`	`441 1482`	`1042`	`CPSase (Carbamoyl-phosphate synthase).`
`REGION`	`1483 1492`	`10`	`Linker.`
`REGION`	`1493 1821`	`329`	`Defective DHOase domain.`
`REGION`	`1822 1909`	`88`	`Linker.`
`REGION`	`1910 2214`	`305`	`ATCase (Aspartate transcarbamylase).`
`ACT_SITE`	`302 302`		`For GATase activity (By similarity).`
`ACT_SITE`	`386 386`		`For GATase activity (By similarity).`
`ACT_SITE`	`388 388`		`For GATase activity (By similarity).`
`MOD_RES`	`1452 1452`		`Phosphoserine.`
`MOD_RES`	`1453 1453`		`Phosphotyrosine.`
`MOD_RES`	`1553 1553`		`Phosphoserine.`
`MOD_RES`	`1857 1857`		`Phosphoserine; by PKA.`
`MOD_RES`	`1859 1859`		`Phosphothreonine.`
`MOD_RES`	`1986 1986`		`Phosphoserine.`
`MOD_RES`	`2142 2142`		`Phosphoserine.`
`CONFLICT`	`86 86`		`H -> D (in Ref. 3; CAA29068).`
`CONFLICT`	`123 123`		`R -> A (in Ref. 1; AAA68280 and 3; CAA29068).`
`CONFLICT`	`250 257`		`ELKVVPWN -> RIESCSMD (in Ref. 3; CAA29068).`
`CONFLICT`	`270 270`		`I -> Y (in Ref. 3; CAA29068).`
`CONFLICT`	`313 314`		`GA -> VQ (in Ref. 3; CAA29068).`
`CONFLICT`	`372 373`		`GI -> RF (in Ref. 3; CAA29068).`
`CONFLICT`	`394 402`		`RDTEFLFDV -> EIQNSCLT (in Ref. 3; CAA29068).`
`CONFLICT`	`431 433`		`KAH -> QGT (in Ref. 3; CAA29068).`
`CONFLICT`	`482 482`		`I -> T (in Ref. 3; CAA29068).`
`CONFLICT`	`485 485`		`I -> N (in Ref. 3; CAA29068).`
`CONFLICT`	`492 492`		`A -> G (in Ref. 3; CAA29068).`
`CONFLICT`	`501 510`		`TAEFVRKVIL -> NAAKQRDVDR (in Ref. 3; CAA29068).`
`CONFLICT`	`1411 1412`		`EV -> S (in Ref. 9; AAA35198).`
`CONFLICT`	`1582 1582`		`I -> M (in Ref. 9; AAA35198).`
`CONFLICT`	`1588 1588`		`N -> K (in Ref. 9; AAA35198).`
`CONFLICT`	`1592 1592`		`V -> G (in Ref. 9; AAA35198).`
`CONFLICT`	`1595 1595`		`S -> A (in Ref. 9; AAA35198).`
`CONFLICT`	`1872 1872`		`Missing (in Ref. 10; AA sequence).`
`CONFLICT`	`1937 1937`		`A -> R (in Ref. 1; AAA68280 and 9; AAA35198).`
`CONFLICT`	`1997 1997`		`T -> I (in Ref. 9; AAA35198).`
`CONFLICT`	`2039 2039`		`H -> L (in Ref. 9; AAA35198).`
`CONFLICT`	`2158 2165`		`KILAHAKE -> VRSWHTQQK (in Ref. 9; AAA35198).`

Sequence information

Length: 2214 AA [This is the length of the unprocessed precursor]

Molecular weight: 245126 Da [This is the MW of the unprocessed precursor]

CRC64: 4CA58304DAECAD21 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATIAPTAPI TPPMESTGDR LVTLELKDGT VLQGYSFGAE KSVAGELVFQ TGMVGYPESV 

        70         80         90        100        110        120 
TDPSYEGQIL VITYPLVGNY GVPDMHLRDE LVEELPRYFE SNRIHIAGLV ISHYTDEYSH 

       130        140        150        160        170        180 
YLRKSSLGKW LQNEGIPAVY GVDTRSLTKH LRDAGSMLGR LSLEKSGSDR TISRSSSWRS 

       190        200        210        220        230        240 
AFDVPEWVDP NVQNLVSKVS INEPKLYVPP ADNKHIELQT GPDGKVLRIL AIDVGMKYNQ 

       250        260        270        280        290        300 
IRCFIKRGVE LKVVPWNYDF TKEDYDGLFI SNGPGDPSVL DDLSQRLSNV LEAKKTPVFG 

       310        320        330        340        350        360 
ICLGHQLIAR AAGASTLKLK FGNRGHNIPC TSTISGRCYI TSQNHGFAVD VDTLTSGWKP 

       370        380        390        400        410        420 
LFVNANDDSN EGIYHSELPY FSVQFHPEST PGPRDTEFLF DVFIQAVKEF KYTQVLKPIA 

       430        440        450        460        470        480 
FPGGLLEDNV KAHPRIEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP 

       490        500        510        520        530        540 
NIATIQTSKG LADKVYFVPV TAEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFEAL 

       550        560        570        580        590        600 
GVKVLGTPID TIITTEDREL FSNAIDEINE KCAKSQAANS VDEALAAVKE IGFPVIVRAA 

       610        620        630        640        650        660 
YALGGLGSGF ANNEKELVDL CNVAFSSSPQ VLVEKSMKGW KEVEYEVVRD AFDNCITVCN 

       670        680        690        700        710        720 
MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPVSKD 

       730        740        750        760        770        780 
YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VKNSVTKSTC ACFEPSLDYC 

       790        800        810        820        830        840 
VVKMPRWDLK KFTRVSTELS SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDLD 

       850        860        870        880        890        900 
IDIDYELNNP TDMRVFAIAN AFAKKGYSVD KVWEMTRIDK WFLNKLHDLV QFAEKISSFG 

       910        920        930        940        950        960 
TKEELPSLVL RQAKQLGFDD RQIARFLDSN EVAIRRLRKE YGITPFVKQI DTVAAEFPAY 

       970        980        990       1000       1010       1020 
TNYLYMTYNA DSHDLSFDDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR ANNIKTIMVN 

      1030       1040       1050       1060       1070       1080 
YNPETVSTDY DEADRLYFET INLERVLDIY EIENSSGVVV SMGGQTSNNI AMTLHRENVK 

      1090       1100       1110       1120       1130       1140 
ILGTSPDMID SAENRYKFSR MLDQIGVDQP AWKELTSMDE AESFAEKVGY PVLVRPSYVL 

      1150       1160       1170       1180       1190       1200 
SGAAMNTVYS KNDLESYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVARN GELVMHVVSE 

      1210       1220       1230       1240       1250       1260 
HVENAGVHSG DATLIVPPQD LAPETVDRIV VATAKIGKAL KITGPYNIQF IAKDNEIKVI 

      1270       1280       1290       1300       1310       1320 
ECNVRASRSF PFISKVVGVN LIELATKAIM GLPLTPYPVE KLPDDYVAVK VPQFSFPRLA 

      1330       1340       1350       1360       1370       1380 
GADPVLGVEM ASTGEVATFG HSKYEAYLKS LLATGFKLPK KNILLSIGSY KEKQELLSSV 

      1390       1400       1410       1420       1430       1440 
QKLYNMGYKL FATSGTADFL SEHGIAVQYL EVLNKDDDDQ KSEYSLTQHL ANNEIDLYIN 

      1450       1460       1470       1480       1490       1500 
LPSANRFRRP ASYVSKGYKT RRLAVDYSVP LVTNVKCAKL LIEAISRNIT LDVSERDAQT 

      1510       1520       1530       1540       1550       1560 
SHRTITLPGL INIATYVPNA SHVIKGPAEL KETTRLFLES GFTYCQLMPR SISGPVITDV 

      1570       1580       1590       1600       1610       1620 
ASLKAANSVS QDSSYTDFSF TIAGTAHNAH SVTQSASKVT ALFLPLRELK NKITAVAELL 

      1630       1640       1650       1660       1670       1680 
NQWPTEKQVI AEAKTADLAS VLLLTSLQNR SIHITGVSNK EDLALIMTVK AKDPRVTCDV 

      1690       1700       1710       1720       1730       1740 
NIYSLFIAQD DYPEAVFLPT KEDQEFFWNN LDSIDAFSVG ALPVALANVT GNKVDVGMGI 

      1750       1760       1770       1780       1790       1800 
KDSLPLLLAA VEEGKLTIDD IVLRLHDNPA KIFNIPTQDS VVEIDLDYSF RRNKRWSPFN 

      1810       1820       1830       1840       1850       1860 
KDMNGGIERV VYNGETLVLS GELVSPGAKG KCIVNPSPAS ITASAELQST SAKRRFSITE 

      1870       1880       1890       1900       1910       1920 
EAIADNLDAA EDAIPEQPLE QKLMSSRPPR ELVAPGAIQN LIRSNNPFRG RHILSIKQFK 

      1930       1940       1950       1960       1970       1980 
RSDFHVLFAV AQELRAAVAR EGVLDLMKGH VITTIFFEPS TRTCSSFIAA MERLGGRIVN 

      1990       2000       2010       2020       2030       2040 
VNPLVSSVKK GETLQDTIRT LACYSDAIVM RHSEEMSVHI AAKYSPVPII NGGNGSREHP 

      2050       2060       2070       2080       2090       2100 
TQAFLDLFTI REEIGTVNGI TVTFMGDLKH GRTVHSLCRL LMHYQVRINL VSPPELRLPE 

      2110       2120       2130       2140       2150       2160 
GLREELRKAG LLGVESIELT PHIISKTDVL YCTRVQEERF NSPEEYARLK DTYIVDNKIL 

      2170       2180       2190       2200       2210 
AHAKENMAIM HPLPRVNEIK EEVDYDHRAA YFRQMKYGLF VRMALLAMVM GVDM

P07259 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