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Q9VNR2 (Q9VNR2_DROME) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesSubmitted name:
Secretory pathway calcium atpase, isoform A EMBL AAF51860.1
EC=3.6.3.35 EMBL AAF51860.1
EC=3.6.3.8 EMBL AAF51860.1
Gene names
Name:SPoCk EMBL AAF51860.1
ORF Names:Dmel_CG32451 EMBL AAF51860.1
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length901 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. RuleBase RU000653

Sequences

Sequence LengthMass (Da)Tools
Q9VNR2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DBB417DC2CA110DA

FASTA90199,546
        10         20         30         40         50         60 
MLLSTSESST HSASEVAGRL QVDVRTGLKW TEAKYRAKII GHNELLLVAE DPTWKKYIEQ 

        70         80         90        100        110        120 
FRNPLILLLL GSALVSVIMK QFDDAVSITI AILIVVTVAF IQEYRSEKSL EELKKLVPPE 

       130        140        150        160        170        180 
CHCLREGRLD TFLARELVPG DIVHLNVGDR VPADVRLFEA VDLSIDESSF TGETEPARKI 

       190        200        210        220        230        240 
TDVLLNNTNV KDHSNMKNIA FMGTLVRCGN GKGIVVSTGE RSEFGEVFKM MQAEEAPKTP 

       250        260        270        280        290        300 
LQKSMDILGA QLSFYSFLII GVIMLLGWLQ GKPLSEMFNI SVSLAVAAIP EGLPIVVTVT 

       310        320        330        340        350        360 
LALGVMRMAK RNSIVKKLPT VETLGCVNVI CSDKTGTLTK NEMTATIIIT SDGYMADVTG 

       370        380        390        400        410        420 
AGYNDQGEIH IRHCNNVEMA KTNITNLLEI GAVCNNAYIQ NGTLLGQPTE GALVAVAMKN 

       430        440        450        460        470        480 
GMYATAENYV RIQEYPFSSE QKMMAVKCIH KYNNNKEEIF FAKGALETLL PQCTKYQFGT 

       490        500        510        520        530        540 
QTVPLTKQNE AEFLAEAYEI GRKGLRVLAL AKGRSMQDLI YCGLVGITDP PRPLVRESIE 

       550        560        570        580        590        600 
MLMQSGVRVK MVTGDAQETA LAIANLIGID TIHHQTLSGQ EMDQMNEHQL DKVANNVSVF 

       610        620        630        640        650        660 
YRVSPRHKLE IVKSLQRSGN IVGMTGDGVN DGVALKKADI GIAMGKNGTD VCKEAADMIL 

       670        680        690        700        710        720 
VNDDFHTIIA AIEEGKGIFY NIRNFVRFQL STSIAALALI ALATLMDIAN PLNAMQILWI 

       730        740        750        760        770        780 
NIIMDGPPAQ SLGVEPVDHD VLKQKPRNVK QPMITKSVVV NVLLSASIIV LGTLWVFQRE 

       790        800        810        820        830        840 
MADGTLGKTK RDTTMTFTCF VFFDMFNALS CRSQTKSVFT IGLTTNRMFL LAVAFSIIGQ 

       850        860        870        880        890        900 
MLVVYFPPLQ MVFQTEALTP YDIFFLVSLT SSVLVVSEIK KWFERTMERK MYSTRSELDF 


V

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References

« Hide 'large scale' references
[1]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Berkeley.
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., 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., WoodageT, 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., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014296 Genomic DNA. Translation: AAF51860.1.
RefSeqNP_730745.1. NM_168963.2.
UniGeneDm.31157.

3D structure databases

HSSPHSSP built from PDB template 1SU4 based on UniProtKB P04191.
ProteinModelPortalQ9VNR2.
SMRQ9VNR2. Positions 5-889.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VNR2. 2 interactions.
MINTMINT-321839.
STRINGQ9VNR2.

Proteomic databases

PRIDEQ9VNR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078531; FBpp0078183; FBgn0052451.
GeneID40495.
KEGGdme:Dmel_CG32451.
UCSCCG32451-RA. d. melanogaster.

Organism-specific databases

CTD40495.
FlyBaseFBgn0052451. SPoCk.

Phylogenomic databases

GeneTreeEMGT00050000001937.
InParanoidQ9VNR2.
PhylomeDBQ9VNR2.

Gene expression databases

ArrayExpressQ9VNR2.
BgeeQ9VNR2.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006413. ATPase_P-typ_Ca-transp_PMR1.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KOK01537.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio819046.

Entry information

Entry nameQ9VNR2_DROME
AccessionPrimary (citable) accession number: Q9VNR2
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info