SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P22700

- ATC1_DROME

UniProt

P22700 - ATC1_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
Gene
Ca-P60A, CG3725
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi304 – 3041Calcium 2; via carbonyl oxygen By similarity
Metal bindingi305 – 3051Calcium 2; via carbonyl oxygen By similarity
Metal bindingi307 – 3071Calcium 2; via carbonyl oxygen By similarity
Metal bindingi309 – 3091Calcium 2 By similarity
Active sitei351 – 35114-aspartylphosphate intermediate By similarity
Metal bindingi703 – 7031Magnesium By similarity
Metal bindingi707 – 7071Magnesium By similarity
Metal bindingi768 – 7681Calcium 1 By similarity
Metal bindingi771 – 7711Calcium 1 By similarity
Metal bindingi796 – 7961Calcium 2 By similarity
Metal bindingi799 – 7991Calcium 1 By similarity
Metal bindingi800 – 8001Calcium 1 By similarity
Metal bindingi800 – 8001Calcium 2 By similarity
Metal bindingi908 – 9081Calcium 1 By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-transporting ATPase activity Source: FlyBase
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: FlyBase

GO - Biological processi

  1. calcium ion transmembrane transport Source: GOC
  2. cellular calcium ion homeostasis Source: FlyBase
  3. flight behavior Source: FlyBase
  4. heart contraction Source: FlyBase
  5. intestinal stem cell homeostasis Source: FlyBase
  6. neuromuscular synaptic transmission Source: FlyBase
  7. positive regulation of calcium-transporting ATPase activity Source: FlyBase
  8. regulation of sequestering of calcium ion Source: FlyBase
  9. stabilization of membrane potential Source: FlyBase
  10. stem cell differentiation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type (EC:3.6.3.8)
Alternative name(s):
Calcium ATPase at 60A
Calcium pump
Gene namesi
Name:Ca-P60A
ORF Names:CG3725
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0263006. Ca-P60A.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein
Note: Colocalizes with SclA and SclB at the sarcoplasmic reticulum (SR) and the dyad, a structure in which the SR membrane lies closest to both the plasma membrane and the sarcomeres.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848Cytoplasmic By similarity
Add
BLAST
Transmembranei49 – 6921Helical; Name=1; By similarity
Add
BLAST
Topological domaini70 – 8920Lumenal By similarity
Add
BLAST
Transmembranei90 – 11021Helical; Name=2; By similarity
Add
BLAST
Topological domaini111 – 253143Cytoplasmic By similarity
Add
BLAST
Transmembranei254 – 27320Helical; Name=3; By similarity
Add
BLAST
Topological domaini274 – 29522Lumenal By similarity
Add
BLAST
Transmembranei296 – 31318Helical; Name=4; By similarity
Add
BLAST
Topological domaini314 – 757444Cytoplasmic By similarity
Add
BLAST
Transmembranei758 – 77720Helical; Name=5; By similarity
Add
BLAST
Topological domaini778 – 78710Lumenal By similarity
Transmembranei788 – 80821Helical; Name=6; By similarity
Add
BLAST
Topological domaini809 – 82820Cytoplasmic By similarity
Add
BLAST
Transmembranei829 – 85123Helical; Name=7; By similarity
Add
BLAST
Topological domaini852 – 89746Lumenal By similarity
Add
BLAST
Transmembranei898 – 91720Helical; Name=8; By similarity
Add
BLAST
Topological domaini918 – 93013Cytoplasmic By similarity
Add
BLAST
Transmembranei931 – 94919Helical; Name=9; By similarity
Add
BLAST
Topological domaini950 – 96415Lumenal By similarity
Add
BLAST
Transmembranei965 – 98521Helical; Name=10; By similarity
Add
BLAST
Topological domaini986 – 102035Cytoplasmic By similarity
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. lipid particle Source: FlyBase
  4. nuclear envelope Source: FlyBase
  5. sarcoplasmic reticulum Source: UniProtKB
  6. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10201020Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
PRO_0000046208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP22700.
PRIDEiP22700.

Expressioni

Gene expression databases

BgeeiP22700.

Interactioni

Subunit structurei

Interacts with SclA and SclB.1 Publication

Protein-protein interaction databases

BioGridi72161. 103 interactions.
DIPiDIP-20129N.
IntActiP22700. 2 interactions.
MINTiMINT-1567799.

Structurei

3D structure databases

ProteinModelPortaliP22700.
SMRiP22700. Positions 1-989.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00560000076887.
InParanoidiP22700.
OMAiPKMEDMI.
OrthoDBiEOG73Z2SF.
PhylomeDBiP22700.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR005782. ATPase_P-typ_Ca-transp_IIA.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: P22700-1) [UniParc]FASTAAdd to Basket

Also known as: C, D, E, F, G, H

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW     50
QLVLEQFDDL LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA 100
NAVVGVWQER NAESAIEALK EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL 150
VEVSVGDKIP ADIRITHIYS TTLRIDQSIL TGESVSVIKH TDAIPDPRAV 200
NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS ETEEIKTPLQ 250
QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV 300
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
DKTGTLTTNQ MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ 400
RIKAADYDTL QELSTICIMC NDSAIDYNEF KQAFEKVGEA TETALIVLAE 450
KLNSFSVNKS GLDRRSAAIA CRGEIETKWK KEFTLEFSRD RKSMSSYCTP 500
LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA LKAKILALTG 550
QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML 600
DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG 650
KSYSGREFDD LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM 700
TGDGVNDAPA LKKAEIGIAM GSGTAVAKSA AEMVLADDNF SSIVSAVEEG 750
RAIYNNMKQF IRYLISSNIG EVVSIFLTAA LGLPEALIPV QLLWVNLVTD 800
GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI GFYVGAATVG 850
AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA 900
LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV 950
DVLSTVFQVT PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK 1000
MHGIVLMWAV FFGLLYAMML 1020

Note: No experimental confirmation available.

Length:1,020
Mass (Da):111,701
Last modified:December 1, 2000 - v2
Checksum:i6A62D350BF316984
GO
Isoform A (identifier: P22700-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     994-1020: GESPIYKMHGIVLMWAVFFGLLYAMML → VPDVVVDRM

Show »
Length:1,002
Mass (Da):109,611
Checksum:i463400C1967BD7D7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei994 – 102027GESPI…YAMML → VPDVVVDRM in isoform A.
VSP_010297Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581K → R in AAL13694. 1 Publication
Sequence conflicti302 – 3021L → V in AAB00735. 1 Publication
Sequence conflicti357 – 3571T → L in CAA35505. 1 Publication
Sequence conflicti495 – 4951S → P in AAL13694. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62892 mRNA. Translation: AAB00735.1.
AE013599 Genomic DNA. Translation: AAF47101.1.
AE013599 Genomic DNA. Translation: AAF47102.1.
AE013599 Genomic DNA. Translation: AAF47103.1.
AE013599 Genomic DNA. Translation: AAM68278.1.
AE013599 Genomic DNA. Translation: AAM68279.1.
AE013599 Genomic DNA. Translation: AAM68280.1.
AE013599 Genomic DNA. Translation: AAM68281.1.
AY058465 mRNA. Translation: AAL13694.1.
X17472 mRNA. Translation: CAA35505.1.
PIRiA36691.
RefSeqiNP_476832.1. NM_057484.2. [P22700-2]
NP_726381.1. NM_166633.1. [P22700-1]
NP_726382.1. NM_166634.1. [P22700-1]
NP_726383.1. NM_166635.1. [P22700-1]
NP_726384.1. NM_166636.1. [P22700-1]
NP_726385.1. NM_166637.1. [P22700-1]
NP_726386.1. NM_166638.1. [P22700-1]
NP_726387.1. NM_166639.1. [P22700-1]
UniGeneiDm.3812.

Genome annotation databases

EnsemblMetazoaiFBtr0072211; FBpp0072120; FBgn0263006. [P22700-1]
FBtr0072212; FBpp0072121; FBgn0263006. [P22700-1]
FBtr0072213; FBpp0072122; FBgn0263006. [P22700-1]
FBtr0072214; FBpp0072123; FBgn0263006. [P22700-1]
FBtr0072216; FBpp0072125; FBgn0263006. [P22700-1]
FBtr0072217; FBpp0072126; FBgn0263006. [P22700-1]
FBtr0072218; FBpp0072127; FBgn0263006. [P22700-1]
GeneIDi49297.
KEGGidme:Dmel_CG3725.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M62892 mRNA. Translation: AAB00735.1 .
AE013599 Genomic DNA. Translation: AAF47101.1 .
AE013599 Genomic DNA. Translation: AAF47102.1 .
AE013599 Genomic DNA. Translation: AAF47103.1 .
AE013599 Genomic DNA. Translation: AAM68278.1 .
AE013599 Genomic DNA. Translation: AAM68279.1 .
AE013599 Genomic DNA. Translation: AAM68280.1 .
AE013599 Genomic DNA. Translation: AAM68281.1 .
AY058465 mRNA. Translation: AAL13694.1 .
X17472 mRNA. Translation: CAA35505.1 .
PIRi A36691.
RefSeqi NP_476832.1. NM_057484.2. [P22700-2 ]
NP_726381.1. NM_166633.1. [P22700-1 ]
NP_726382.1. NM_166634.1. [P22700-1 ]
NP_726383.1. NM_166635.1. [P22700-1 ]
NP_726384.1. NM_166636.1. [P22700-1 ]
NP_726385.1. NM_166637.1. [P22700-1 ]
NP_726386.1. NM_166638.1. [P22700-1 ]
NP_726387.1. NM_166639.1. [P22700-1 ]
UniGenei Dm.3812.

3D structure databases

ProteinModelPortali P22700.
SMRi P22700. Positions 1-989.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 72161. 103 interactions.
DIPi DIP-20129N.
IntActi P22700. 2 interactions.
MINTi MINT-1567799.

Proteomic databases

PaxDbi P22700.
PRIDEi P22700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0072211 ; FBpp0072120 ; FBgn0263006 . [P22700-1 ]
FBtr0072212 ; FBpp0072121 ; FBgn0263006 . [P22700-1 ]
FBtr0072213 ; FBpp0072122 ; FBgn0263006 . [P22700-1 ]
FBtr0072214 ; FBpp0072123 ; FBgn0263006 . [P22700-1 ]
FBtr0072216 ; FBpp0072125 ; FBgn0263006 . [P22700-1 ]
FBtr0072217 ; FBpp0072126 ; FBgn0263006 . [P22700-1 ]
FBtr0072218 ; FBpp0072127 ; FBgn0263006 . [P22700-1 ]
GeneIDi 49297.
KEGGi dme:Dmel_CG3725.

Organism-specific databases

CTDi 49297.
FlyBasei FBgn0263006. Ca-P60A.

Phylogenomic databases

eggNOGi COG0474.
GeneTreei ENSGT00560000076887.
InParanoidi P22700.
OMAi PKMEDMI.
OrthoDBi EOG73Z2SF.
PhylomeDBi P22700.

Miscellaneous databases

GenomeRNAii 49297.
NextBioi 839728.
PROi P22700.

Gene expression databases

Bgeei P22700.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi IPR005782. ATPase_P-typ_Ca-transp_IIA.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view ]
Pfami PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and chromosomal localization of a sarco/endoplasmic reticulum-type Ca2(+)-ATPase of Drosophila melanogaster."
    Magyar A., Varadi A.
    Biochem. Biophys. Res. Commun. 173:872-877(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  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.
    , 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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Head.
  5. "Amplification of the phosphorylation site-ATP-binding site cDNA fragment of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by polymerase chain reaction."
    Varadi A., Gilmore-Heber M., Benz E.J. Jr.
    FEBS Lett. 258:203-207(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 357-513.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames."
    Magny E.G., Pueyo J.I., Pearl F.M., Cespedes M.A., Niven J.E., Bishop S.A., Couso J.P.
    Science 341:1116-1120(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCLA AND SCLB, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiATC1_DROME
AccessioniPrimary (citable) accession number: P22700
Secondary accession number(s): A4UZU0
, Q2MGN2, Q95TX1, Q9W1G2, Q9W1G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi