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Phospholipid-transporting ATPase 3 (AtALA3) (EC 3.6.3.1) (Aminophospholipid ATPase 3) (Aminophospholipid flippase 3) (Protein IRREGULAR TRICHOME BRANCH 2)

 ALA3_ARATH              Reviewed;        1213 AA.
Q9XIE6; Q8RWQ3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
28-FEB-2003, sequence version 2.
16-JAN-2019, entry version 146.
RecName: Full=Phospholipid-transporting ATPase 3 {ECO:0000303|PubMed:11402198};
Short=AtALA3 {ECO:0000303|PubMed:11402198};
EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
AltName: Full=Aminophospholipid ATPase 3 {ECO:0000303|PubMed:11402198};
AltName: Full=Aminophospholipid flippase 3 {ECO:0000303|PubMed:11402198};
AltName: Full=Protein IRREGULAR TRICHOME BRANCH 2 {ECO:0000303|PubMed:19566596};
Name=ALA3 {ECO:0000303|PubMed:11402198};
Synonyms=ITB2 {ECO:0000303|PubMed:19566596};
OrderedLocusNames=At1g59820 {ECO:0000312|Araport:AT1G59820};
ORFNames=F23H11.14 {ECO:0000312|EMBL:AAD39325.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11402198; DOI=10.1104/pp.126.2.696;
Axelsen K.B., Palmgren M.G.;
"Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
Plant Physiol. 126:696-706(2001).
[5]
FUNCTION, MUTAGENESIS OF ASP-413, DISRUPTION PHENOTYPE, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ALIS1; ALIS3 AND
ALIS5.
PubMed=18344284; DOI=10.1105/tpc.107.054767;
Poulsen L.R., Lopez-Marques R.L., McDowell S.C., Okkeri J., Licht D.,
Schulz A., Pomorski T., Harper J.F., Palmgren M.G.;
"The Arabidopsis P4-ATPase ALA3 localizes to the Golgi and requires a
beta-subunit to function in lipid translocation and secretory vesicle
formation.";
Plant Cell 20:658-676(2008).
[6]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19566596; DOI=10.1111/j.1365-313X.2009.03954.x;
Zhang X., Oppenheimer D.G.;
"IRREGULAR TRICHOME BRANCH 2 (ITB2) encodes a putative
aminophospholipid translocase that regulates trichome branch
elongation in Arabidopsis.";
Plant J. 60:195-206(2009).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALIS1; ALIS3 AND
ALIS5.
PubMed=20053675; DOI=10.1091/mbc.E09-08-0656;
Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K.,
Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.;
"Intracellular targeting signals and lipid specificity determinants of
the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-
subunit.";
Mol. Biol. Cell 21:791-801(2010).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23667493; DOI=10.1371/journal.pone.0062577;
McDowell S.C., Lopez-Marques R.L., Poulsen L.R., Palmgren M.G.,
Harper J.F.;
"Loss of the Arabidopsis thaliana P(4)-ATPase ALA3 reduces
adaptability to temperature stresses and impairs vegetative, pollen,
and ovule development.";
PLoS ONE 8:E62577-E62577(2013).
-!- FUNCTION: Involved in transport of phospholipids. Contributes to
transmembrane flipping of lipids. Required for secretory processes
during plant development. Requires an interaction with an ALIS
protein for activity. Has activity with phosphatidylserine,
phosphatidylcholine and phosphatidylethanolamine, but not with
lysolipid (PubMed:18344284, PubMed:19566596, PubMed:20053675).
Modifies endomembranes in multiple cell types, enabling structural
changes, or signaling functions that are critical for normal
development and adaptation to varied growth environments
(PubMed:23667493). {ECO:0000269|PubMed:18344284,
ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:20053675,
ECO:0000269|PubMed:23667493}.
-!- CATALYTIC ACTIVITY:
Reaction=a phospholipid derivative(in) + ATP + H2O = a
phospholipid derivative(out) + ADP + H(+) + phosphate;
Xref=Rhea:RHEA:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16247, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:456216; EC=7.6.2.1;
Evidence={ECO:0000305|PubMed:11402198};
-!- SUBUNIT: Associates with ALIS1 to form a stable and active
complex. Interacts with ALIS3 and ALIS5 in a heterologous system.
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}; Multi-
pass membrane protein {ECO:0000255}. Endoplasmic reticulum
membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane
protein {ECO:0000255}. Note=Requires the presence of an ALIS
protein to exit the endoplasmic reticulum to the Golgi.
{ECO:0000269|PubMed:20053675}.
-!- TISSUE SPECIFICITY: Expressed in petals and sepals, but not in
reproductive tissues. In siliques, detected in the upper part of
the seed pod and in the area between the seed pod and the stem,
but not in developing seeds. Strong expression in vascular shoot
tissues and in stomatal guard cells of young rosettes leaves. In
roots, expressed in cells surrounding the xylem and in central and
peripheral columella cells. Detected in developing and mature
trichomes, roots, pollen and growing pollen tubes.
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:19566596}.
-!- DISRUPTION PHENOTYPE: Impaired growth of roots and shoots
(PubMed:18344284, PubMed:23667493). Roots devoided of the
characteristic trans-Golgi proliferation of slime vesicles
containing polysaccharides and enzymes for secretion
(PubMed:18344284). Aberrant trichome expansion, reduced primary
root growth and longer root hairs (PubMed:19566596). Impaired
pollen growth (PubMed:19566596, PubMed:23667493). Impaired ovule
development (PubMed:23667493). Reduced adaptability to temperature
stresses (PubMed:23667493). {ECO:0000269|PubMed:18344284,
ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:23667493}.
-!- MISCELLANEOUS: The intracellular targeting signals and lipid
specificity determinants reside in the catalytic ALA subunit.
{ECO:0000269|PubMed:20053675}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC007258; AAD39325.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE33621.1; -; Genomic_DNA.
EMBL; AY091777; AAM10325.1; -; mRNA.
PIR; C96622; C96622.
RefSeq; NP_176191.1; NM_104675.3.
UniGene; At.36777; -.
ProteinModelPortal; Q9XIE6; -.
BioGrid; 27500; 1.
STRING; 3702.AT1G59820.1; -.
TCDB; 3.A.3.8.6; the p-type atpase (p-atpase) superfamily.
iPTMnet; Q9XIE6; -.
PaxDb; Q9XIE6; -.
PRIDE; Q9XIE6; -.
EnsemblPlants; AT1G59820.1; AT1G59820.1; AT1G59820.
GeneID; 842275; -.
Gramene; AT1G59820.1; AT1G59820.1; AT1G59820.
KEGG; ath:AT1G59820; -.
Araport; AT1G59820; -.
TAIR; locus:2025961; AT1G59820.
eggNOG; ENOG410ITKD; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
HOGENOM; HOG000202528; -.
InParanoid; Q9XIE6; -.
KO; K14802; -.
OMA; GMSCKLI; -.
OrthoDB; 587717at2759; -.
PhylomeDB; Q9XIE6; -.
BioCyc; ARA:AT1G59820-MONOMER; -.
BRENDA; 3.6.99.B1; 399.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-936837; Ion transport by P-type ATPases.
PRO; PR:Q9XIE6; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9XIE6; baseline and differential.
Genevisible; Q9XIE6; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0005548; F:phospholipid transporter activity; IDA:TAIR.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IBA:GO_Central.
GO; GO:0048194; P:Golgi vesicle budding; IMP:TAIR.
GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Endoplasmic reticulum;
Golgi apparatus; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
Transmembrane helix.
CHAIN 1 1213 Phospholipid-transporting ATPase 3.
/FTId=PRO_0000046387.
TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.
TRANSMEM 68 89 Helical. {ECO:0000255}.
TOPO_DOM 90 93 Extracellular. {ECO:0000255}.
TRANSMEM 94 116 Helical. {ECO:0000255}.
TOPO_DOM 117 297 Cytoplasmic. {ECO:0000255}.
TRANSMEM 298 319 Helical. {ECO:0000255}.
TOPO_DOM 320 346 Extracellular. {ECO:0000255}.
TRANSMEM 347 364 Helical. {ECO:0000255}.
TOPO_DOM 365 900 Cytoplasmic. {ECO:0000255}.
TRANSMEM 901 920 Helical. {ECO:0000255}.
TOPO_DOM 921 934 Extracellular. {ECO:0000255}.
TRANSMEM 935 954 Helical. {ECO:0000255}.
TOPO_DOM 955 984 Cytoplasmic. {ECO:0000255}.
TRANSMEM 985 1006 Helical. {ECO:0000255}.
TOPO_DOM 1007 1013 Extracellular. {ECO:0000255}.
TRANSMEM 1014 1036 Helical. {ECO:0000255}.
TOPO_DOM 1037 1042 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1043 1063 Helical. {ECO:0000255}.
TOPO_DOM 1064 1076 Extracellular. {ECO:0000255}.
TRANSMEM 1077 1087 Helical. {ECO:0000255}.
TOPO_DOM 1088 1213 Cytoplasmic. {ECO:0000255}.
ACT_SITE 413 413 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 845 845 Magnesium. {ECO:0000250}.
METAL 849 849 Magnesium. {ECO:0000250}.
MUTAGEN 413 413 D->A: Loss of internalization of
phospholipids.
{ECO:0000269|PubMed:18344284}.
SEQUENCE 1213 AA; 137753 MW; 938642DEFDA28B66 CRC64;
MVRSGSFSVD SSATHQRTPS RTVTLGHIQP QAPTYRTVYC NDRESNQPVR FKGNSISTTK
YNVFTFLPKG LFEQFRRIAN IYFLGISCLS MTPISPVSPI TNVAPLSMVL LVSLIKEAFE
DWKRFQNDMS INNSTVEILQ DQQWVSIPWR KLQVGDIVKI KKDGFFPADI LFMSSTNSDG
ICYVETANLD GETNLKIRKA LERTWDYLVP EKAYEFKGEI QCEQPNNSLY TFTGNLVVQK
QTLPLSPDQL LLRGCSLRNT EYIVGAVVFT GHETKVMMNA MNAPSKRSTL EKKLDKLIIT
IFCVLVTMCL IGAIGCSIVT DREDKYLGLH NSDWEYRNGL MIGFFTFFTL VTLFSSIIPI
SLYVSIEMIK FIQSTQFINR DLNMYHAETN TPASARTSNL NEELGQVEYI FSDKTGTLTR
NLMEFFKCSI GGVSYGCGVT EIEKGIAQRH GLKVQEEQRS TGAIREKGFN FDDPRLMRGA
WRNEPNPDLC KELFRCLAIC HTVLPEGDES PEKIVYQAAS PDEAALVTAA KNFGFFFYRR
TPTMVYVRES HVEKMGKIQD VAYEILNVLE FNSTRKRQSV VCRFPDGRLV LYCKGADNVI
FERLANGMDD VRKVTREHLE HFGSSGLRTL CLAYKDLNPE TYDSWNEKFI QAKSALRDRE
KKLDEVAELI EKDLILIGST AIEDKLQEGV PTCIETLSRA GIKIWVLTGD KMETAINIAY
ACNLINNEMK QFVISSETDA IREAEERGDQ VEIARVIKEE VKRELKKSLE EAQHSLHTVA
GPKLSLVIDG KCLMYALDPS LRVMLLSLSL NCTSVVCCRV SPLQKAQVTS LVRKGAQKIT
LSIGDGANDV SMIQAAHVGI GISGMEGMQA VMASDFAIAQ FRFLTDLLLV HGRWSYLRIC
KVVMYFFYKN LTFTLTQFWF TFRTGFSGQR FYDDWFQSLF NVVFTALPVI VLGLFEKDVS
ASLSKRYPEL YREGIRNSFF KWRVVAVWAT SAVYQSLVCY LFVTTSSFGA VNSSGKVFGL
WDVSTMVFTC LVIAVNVRIL LMSNSITRWH YITVGGSILA WLVFAFVYCG IMTPHDRNEN
VYFVIYVLMS TFYFYFTLLL VPIVSLLGDF IFQGVERWFF PYDYQIVQEI HRHESDASKA
DQLEVENELT PQEARSYAIS QLPRELSKHT GFAFDSPGYE SFFASQLGIY APQKAWDVAR
RASMRSRPKV PKK


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Pathways :
WP2199: Seed Development
WP1691: Proteasome
WP470: Proteasome Degradation
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[ALA3 ITB2 At1g59820 F23H11.14] Phospholipid-transporting ATPase 3 (AtALA3) (EC 7.6.2.1) (Aminophospholipid ATPase 3) (Aminophospholipid flippase 3) (Protein IRREGULAR TRICHOME BRANCH 2)
[Atp8b1] Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (P4-ATPase flippase complex alpha subunit ATP8B1)
[ALA2 At5g44240 MLN1.17] Phospholipid-transporting ATPase 2 (AtALA2) (EC 7.6.2.1) (Aminophospholipid ATPase 2) (Aminophospholipid flippase 2)
[ATP8B1 ATPIC FIC1 PFIC] Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (Familial intrahepatic cholestasis type 1) (P4-ATPase flippase complex alpha subunit ATP8B1)
[ATP8A2 ATPIB] Phospholipid-transporting ATPase IB (EC 7.6.2.1) (ATPase class I type 8A member 2) (ML-1) (P4-ATPase flippase complex alpha subunit ATP8A2)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[DNF2 YDR093W YD8557.01] Phospholipid-transporting ATPase DNF2 (EC 7.6.2.1) (Flippase DNF2)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[DNF1 YER166W SYGP-ORF7] Phospholipid-transporting ATPase DNF1 (EC 7.6.2.1) (Flippase DNF1)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Wrnip1 Whip] ATPase WRNIP1 (EC 3.6.1.3) (Werner helicase-interacting protein 1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Tas1r3 Sac T1r3 Tr3] Taste receptor type 1 member 3 (Saccharin preference protein) (Sweet taste receptor T1R3)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)

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