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UniProtKB/Swiss-Prot entry P05990


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYR1_DROME
Primary accession number P05990
Secondary accession numbers O97163 Q26376 Q7KUX4 Q8SXM0 Q9VXD5
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on October 25, 2005 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 107)
Name and origin of the protein
Protein name CAD protein
Synonym Protein rudimentary
Includes Glutamine-dependent carbamoyl-phosphate synthase
     (EC 6.3.5.5)
Aspartate carbamoyltransferase
     (EC 2.1.3.2)
Dihydroorotase
     (EC 3.5.2.3)
Gene name
Name: r
ORFNames: CG18572
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(87)90621-8; PubMed=2884325 [NCBI, ExPASy, EBI, Israel, Japan]
Freund J.-N., Jarry B.P.;
"The rudimentary gene of Drosophila melanogaster encodes four enzymic functions.";
J. Mol. Biol. 193:1-13(1987).
[2]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(86)90378-5; PubMed=3023623 [NCBI, ExPASy, EBI, Israel, Japan]
Freund J.-N., Zerges W., Schedl P., Jarry B.P.;
"Molecular organization of the rudimentary gene of Drosophila melanogaster.";
J. Mol. Biol. 189:25-36(1986).
[3]
ERRATUM.
Freund J.-N., Zerges W., Schedl P., Jarry B.P.;
J. Mol. Biol. 191:727-727(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
DOI=10.1093/nar/20.17.4639; PubMed=1329025 [NCBI, ExPASy, EBI, Israel, Japan]
Zerges W., Udvardy A., Schedl P.;
"Molecular characterization of the 5' end of the rudimentary gene in Drosophila and analysis of three P element insertions.";
Nucleic Acids Res. 20:4639-4647(1992).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-2224 (ISOFORM B).
STRAIN=Berkeley;
TISSUE=Larva, and Pupae;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 898-1649 (ISOFORM A), CPSASE ACTIVITY, AND MUTAGENESIS OF GLU-1167.
DOI=10.1006/jmbi.1999.2618; PubMed=10080891 [NCBI, ExPASy, EBI, Israel, Japan]
Simmons A.J., Rawls J.M., Piskur J., Davidson J.N.;
"A mutation that uncouples allosteric regulation of carbamyl phosphate synthetase in Drosophila.";
J. Mol. Biol. 287:277-285(1999).
[9]
SEQUENCE REVISION TO 2066-2146.
DOI=10.1006/jmbi.1994.1663; PubMed=7932764 [NCBI, ExPASy, EBI, Israel, Japan]
Davidson J.N., Kern C.B.;
"Revision in sequence of CAD aspartate transcarbamylase domain of Drosophila.";
J. Mol. Biol. 243:364-366(1994).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1883; SER-1885; SER-1892 AND SER-1894, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
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
X04813; CAA28502.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03875; CAA27509.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03876; CAA27510.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03877; CAA27511.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03878; CAA27512.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03879; CAA27513.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF48639.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAS65389.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M37783; AAA28873.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089560; AAL90298.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF129814; AAD18071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S74010; AAB32204.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29106; QZFF.
RefSeq NP_523377.1; -.
NP_996488.1; -.
UniGene Dm.4956
3D structure databases
HSSP P00479; 3CSU. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P05990.
Protein-protein interaction databases
IntAct P05990; -.
Organism-specific databases
FlyBase FBgn0003189; r.
Gene expression databases
ArrayExpress P05990; -.
GermOnline CG18572; Drosophila melanogaster.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR006680; Amidohydro_1.
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.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
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; 1.
Pfam PF01979; Amidohydro_1; 1.
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.
ProDom PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00670; asp_carb_tr; 1.
TIGR01369; CPSaseII_lrg; 1.
TIGR01368; CPSaseIIsmall; 1.
TIGR00857; pyrC_multi; 1.
PROSITE PS50975; ATP_GRASP; 2.
PS00097; CARBAMOYLTRANSFERASE; 1.
PS00866; CPSASE_1; 1.
PS00867; CPSASE_2; 2.
PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05990.
Genome annotation databases
Ensembl CG18572; Drosophila melanogaster. [Contig view]
GeneID 32640; -.
KEGG dme:Dmel_CG18572; -.
NMPDR fig|7227.3.peg.18220; -.
Phylogenomic databases
HOGENOM P05990; -.
Other
ProtoNet P05990.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2224  2224     CAD protein. PRO_0000199505
DOMAIN   195    380  186     Glutamine amidotransferase type-1. 
DOMAIN   529    721  193     ATP-grasp 1. 
DOMAIN   1066   1257  192     ATP-grasp 2. 
NP_BIND   555    610  56     ATP (By similarity). 
NP_BIND   1092   1149  58     ATP (By similarity). 
REGION   1    369  369     GATase (Glutamine amidotransferase). 
REGION   370    415  46     Linker. 
REGION   416   1470  1055     CPSase (Carbamoyl-phosphate synthase). 
REGION   1471   1484  14     Linker. 
REGION   1485   1800  316     DHOase (dihydroorotase). 
REGION   1801   1912  112     Linker. 
REGION   1913   2224  312     ATCase (Aspartate transcarbamylase). 
ACT_SITE   269    269        For GATase activity (By similarity). 
ACT_SITE   353    353        For GATase activity (By similarity). 
ACT_SITE   355    355        For GATase activity (By similarity). 
METAL   678    678        Manganese 1 (By similarity). 
METAL   692    692        Manganese 1 (By similarity). 
METAL   692    692        Manganese 2 (By similarity). 
METAL   694    694        Manganese 2 (By similarity). 
METAL   1216   1216        Manganese 3 (By similarity). 
METAL   1228   1228        Manganese 3 (By similarity). 
METAL   1228   1228        Manganese 4 (By similarity). 
METAL   1230   1230        Manganese 4 (By similarity). 
METAL   1486   1486        Zinc (Potential). 
METAL   1488   1488        Zinc (Potential). 
MOD_RES   1883   1883        Phosphoserine. 
MOD_RES   1885   1885        Phosphoserine. 
MOD_RES   1892   1892        Phosphoserine. 
MOD_RES   1894   1894        Phosphoserine. 
VAR_SEQ   1374   1386        ESVQWTFDKTTPD -> SIFMSVCLLYIMQ (in isoform B). VSP_016004
VAR_SEQ   1387   2224        Missing (in isoform B). VSP_016005
MUTAGEN   1167   1167        E->K: Severely diminishes UTP inhibition of CPSase; in Su(b). 
CONFLICT   34     34        F -> V (in Ref. 2; CAA27509). 
CONFLICT   58     58        G -> A (in Ref. 2; CAA27509). 
CONFLICT   172    173        RN -> QD (in Ref. 2; CAA27509). 
CONFLICT   220    221        LL -> FV (in Ref. 2; CAA27509). 
CONFLICT   288    288        Y -> I (in Ref. 2; CAA27509). 
CONFLICT   394    394        P -> L (in Ref. 2; CAA27509). 
CONFLICT   2192   2192        S -> L (in Ref. 2; CAA27513). 
CONFLICT   2222   2224        TAL -> RRS (in Ref. 2; CAA27513). 
Sequence information
Length: 2224 AA [This is the length of the unprocessed precursor] Molecular weight: 246672 Da [This is the MW of the unprocessed precursor] CRC64: F89DEAD44FEFAEC6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA LTDRSYSGQI 

        70         80         90        100        110        120 
LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV VGEVAEEAFH WRKWKTLPDW 

       130        140        150        160        170        180 
LKQHKVPGIQ DIDTRALTKK LREQGSMLGK IVYEKPPVEG LPKSSFVDPN VRNLAKECSV 

       190        200        210        220        230        240 
KERQVYGNPN GKGPRIAILD CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG 

       250        260        270        280        290        300 
PGNPESCDQI VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR 

       310        320        330        340        350        360 
ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV QFHPEHHAGP 

       370        380        390        400        410        420 
QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP VMPRKVLILG SGGLSIGQAG 

       430        440        450        460        470        480 
EFDYSGSQAI KAMRESNIQT VLINPNIATV QTSKGMADKC YFLPLTPHYV EQVIKSERPN 

       490        500        510        520        530        540 
GVLLTFGGQT ALNCGVQLER AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA 

       550        560        570        580        590        600 
PSEAVYSVAQ ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV 

       610        620        630        640        650        660 
DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL SDREYQMLRS 

       670        680        690        700        710        720 
TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA 

       730        740        750        760        770        780 
LGLPLPDIKN SVTGNTTACF EPSLDYCVVK IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG 

       790        800        810        820        830        840 
RNFEEAFQKA LRMVDSDVLG FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE 

       850        860        870        880        890        900 
LHQLTNIDYW FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA 

       910        920        930        940        950        960 
VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI VVGSGVYRIG 

       970        980        990       1000       1010       1020 
SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC DRLYFEEISF EVVMDIYEME 

      1030       1040       1050       1060       1070       1080 
NSEGIILSMG GQLPNNIAMD LHRQQAKVLG TSPESIDCAE NRFKFSRMLD RKGILQPRWK 

      1090       1100       1110       1120       1130       1140 
ELTNLQSAIE FCEEVGYPCL VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS 

      1150       1160       1170       1180       1190       1200 
KFLTEAKEID VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT 

      1210       1220       1230       1240       1250       1260 
CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA TATRAIVGLD 

      1270       1280       1290       1300       1310       1320 
VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG EVACFGDNRY EAYLKAMMST 

      1330       1340       1350       1360       1370       1380 
GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA KMGYKLYASM GTGDFYAEHG VNVESVQWTF 

      1390       1400       1410       1420       1430       1440 
DKTTPDDING ELRHLAEFLA NKQFDLVINL PMSGGGARRV SSFMTHGYRT RRLAVDYSIP 

      1450       1460       1470       1480       1490       1500 
LVTDVKCTKL LVESMRMNGG KPPMKTHTDC MTSRRIVKLP GFIDVHVHLR EPGATHKEDF 

      1510       1520       1530       1540       1550       1560 
ASGTAAALAG GVTLVCAMPN TNPSIVDRET FTQFQELAKA GARCDYALYV GASDDNWAQV 

      1570       1580       1590       1600       1610       1620 
NELASHACGL KMYLNDTFGT LKLSDMTSWQ RHLSHWPKRS PIVCHAERQS TAAVIMLAHL 

      1630       1640       1650       1660       1670       1680 
LDRSVHICHV ARKEEIQLIR SAKEKGVKVT CEVCPHHLFL STKDVERLGH GMSEVRPLLC 

      1690       1700       1710       1720       1730       1740 
SPEDQEALWE NIDYIDVFAT DHAPHTLAEK RSERPPPGFP GVETILPLLL QAVHEGRLTM 

      1750       1760       1770       1780       1790       1800 
EDIKRKFHRN PKIIFNLPDQ AQTYVEVDLD EEWTITGNEM KSKSGWTPFE GTKVKGRVHR 

      1810       1820       1830       1840       1850       1860 
VVLRGEVAFV DGQVLVQPGF GQNVRPKQSP LASEASQDLL PSDNDANDTF TRLLTSEGPG 

      1870       1880       1890       1900       1910       1920 
GGVHGISTKV HFVDGANFLR PNSPSPRIRL DSASNTTLRE YLQRTTNSNP VAHSLMGKHI 

      1930       1940       1950       1960       1970       1980 
LAVDMFNKDH LNDIFNLAQL LKLRGTKDRP VDELLPGKIM ASVFYEVSTR TQCSFAAAML 

      1990       2000       2010       2020       2030       2040 
RLGGRVISMD NITSSVKKGE SLEDSIKVVS SYADVVVLRH PSPGAVARAA TFSRKPLINA 

      2050       2060       2070       2080       2090       2100 
GDGVGEHPTQ ALLDIFTIRE EFGTVNGLTI TMVGDLKNGR TVHSLARLLT LYNVNLQYVA 

      2110       2120       2130       2140       2150       2160 
PNSLQMPDEV VQFVHQRGVK QLFARDLKNV LPDTDVLYMT RIQRERFDNV EDYEKCCGHL 

      2170       2180       2190       2200       2210       2220 
VLTPEHMMRA KKRSIVLHPL PRLNEISREI DSDPRAAYFR QAEYGMYIRM ALLAMVVGGR 


NTAL 

P05990 in FASTA format

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