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ALA1_ARATH
ID   ALA1_ARATH              Reviewed;        1158 AA.
AC   P98204;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Phospholipid-transporting ATPase 1 {ECO:0000303|PubMed:11148289};
DE            Short=AtALA1 {ECO:0000303|PubMed:11148289};
DE            EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE   AltName: Full=Aminophospholipid flippase 1 {ECO:0000303|PubMed:11402198};
GN   Name=ALA1 {ECO:0000303|PubMed:11148289};
GN   OrderedLocusNames=At5g04930 {ECO:0000312|Araport:AT5G04930};
GN   ORFNames=MUG13.22 {ECO:0000312|EMBL:BAB11515.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11148289; DOI=10.2307/3871240;
RA   Gomes E., Jakobsen M.K., Axelsen K.B., Geisler M., Palmgren M.G.;
RT   "Chilling tolerance in Arabidopsis involves ALA1, a member of a new family
RT   of putative aminophospholipid translocases.";
RL   Plant Cell 12:2441-2454(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11402198; DOI=10.1104/pp.126.2.696;
RA   Axelsen K.B., Palmgren M.G.;
RT   "Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
RL   Plant Physiol. 126:696-706(2001).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22514601; DOI=10.1371/journal.pone.0033042;
RA   Lopez-Marques R.L., Poulsen L.R., Palmgren M.G.;
RT   "A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase
RT   ALA1, localizes to the plasma membrane following association with a beta-
RT   subunit.";
RL   PLoS ONE 7:E33042-E33042(2012).
CC   -!- FUNCTION: Involved in transport of phospholipids. Contributes to
CC       transmembrane flipping of lipids. Has activity with phosphatidylserine
CC       and with a much lower efficiency with phosphatidylethanolamine, but not
CC       with phosphatidylcholine. {ECO:0000269|PubMed:11148289}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000269|PubMed:11148289};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22514601}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22514601}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=Requires the presence of an ALIS
CC       protein to exit the endoplasmic reticulum to the cell membrane.
CC       {ECO:0000269|PubMed:22514601}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, flowers, anthers, leaves,
CC       vascular tissues and stems. {ECO:0000269|PubMed:11148289}.
CC   -!- MISCELLANEOUS: Knockdown mutants are cold sensitive.
CC       {ECO:0000269|PubMed:11148289}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000305}.
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DR   EMBL; AF175769; AAG01899.1; -; mRNA.
DR   EMBL; AB005245; BAB11515.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90805.1; -; Genomic_DNA.
DR   RefSeq; NP_568146.1; NM_120575.3.
DR   AlphaFoldDB; P98204; -.
DR   SMR; P98204; -.
DR   BioGRID; 15654; 4.
DR   IntAct; P98204; 1.
DR   STRING; 3702.AT5G04930.1; -.
DR   TCDB; 3.A.3.8.7; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; P98204; -.
DR   PaxDb; P98204; -.
DR   PRIDE; P98204; -.
DR   ProteomicsDB; 244924; -.
DR   EnsemblPlants; AT5G04930.1; AT5G04930.1; AT5G04930.
DR   GeneID; 830375; -.
DR   Gramene; AT5G04930.1; AT5G04930.1; AT5G04930.
DR   KEGG; ath:AT5G04930; -.
DR   Araport; AT5G04930; -.
DR   TAIR; locus:3355727; AT5G04930.
DR   eggNOG; KOG0206; Eukaryota.
DR   HOGENOM; CLU_000846_5_2_1; -.
DR   InParanoid; P98204; -.
DR   OMA; PRFFIFA; -.
DR   OrthoDB; 587717at2759; -.
DR   PhylomeDB; P98204; -.
DR   BioCyc; ARA:AT5G04930-MON; -.
DR   BRENDA; 7.6.2.1; 399.
DR   PRO; PR:P98204; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P98204; baseline and differential.
DR   Genevisible; P98204; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Endoplasmic reticulum; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1158
FT                   /note="Phospholipid-transporting ATPase 1"
FT                   /id="PRO_0000046385"
FT   TOPO_DOM        1..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..127
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..391
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..914
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        915..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        935..948
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        949..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        969..998
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        999..1020
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1021..1027
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1028..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1051..1056
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1057..1077
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1078..1090
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1091..1115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1116..1158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         859
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         863
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1158 AA;  130329 MW;  5CC042B40C8C974D CRC64;
     MDPRKSIDKP PHHDPILGVS SRWSVSSKDN KEVTFGDLGS KRIRHGSAGA DSEMLSMSQK
     EIKDEDARLI YINDPDRTNE RFEFTGNSIK TAKYSVFTFL PRNLFEQFHR VAYIYFLVIA
     VLNQLPQLAV FGRGASIMPL AFVLLVSAIK DAYEDFRRHR SDRVENNRLA LVFEDHQFRE
     KKWKHIRVGE VIKVQSNQTL PCDMVLLATS DPTGVVYVQT TNLDGESNLK TRYAKQETLL
     KAADMESFNG FIKCEKPNRN IYGFQANMEI DGRRLSLGPS NIILRGCELK NTAWALGVVV
     YAGGETKAML NNSGAPSKRS RLETRMNLEI ILLSLFLIVL CTIAAATAAV WLRTHRDDLD
     TILFYRRKDY SERPGGKNYK YYGWGWEIFF TFFMAVIVYQ IMIPISLYIS MELVRIGQAY
     FMTNDDQMYD ESSDSSFQCR ALNINEDLGQ IKYLFSDKTG TLTDNKMEFQ CACIEGVDYS
     DREPADSEHP GYSIEVDGII LKPKMRVRVD PVLLQLTKTG KATEEAKRAN EFFLSLAACN
     TIVPIVSNTS DPNVKLVDYQ GESPDEQALV YAAAAYGFLL IERTSGHIVI NVRGETQRFN
     VLGLHEFDSD RKRMSVILGC PDMSVKLFVK GADSSMFGVM DESYGGVIHE TKIQLHAYSS
     DGLRTLVVGM RELNDSEFEQ WHSSFEAAST ALIGRAGLLR KVAGNIETNL RIVGATAIED
     KLQRGVPEAI ESLRIAGIKV WVLTGDKQET AISIGFSSRL LTRNMRQIVI NSNSLDSCRR
     SLEEANASIA SNDESDNVAL IIDGTSLIYV LDNDLEDVLF QVACKCSAIL CCRVAPFQKA
     GIVALVKNRT SDMTLAIGDG ANDVSMIQMA DVGVGISGQE GRQAVMASDF AMGQFRFLVP
     LLLVHGHWNY QRMGYMILYN FYRNAVFVLI LFWYVLFTCY TLTTAITEWS SVLYSVIYTA
     IPTIIIGILD KDLGRQTLLD HPQLYGVGQR AEGYSTTLFW YTMIDTIWQS AAIFFIPMFA
     YWGSTIDTSS LGDLWTIAAV VVVNLHLAMD VIRWNWITHA AIWGSIVAAC ICVIVIDVIP
     TLPGYWAIFQ VGKTWMFWFC LLAIVVTSLL PRFAIKFLVE YYRPSDVRIA REAEKLGTFR
     ESQPVGVEMN LIQDPPRR
 
 
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