ALIS1_ARATH
ID ALIS1_ARATH Reviewed; 350 AA.
AC Q9LTW0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=ALA-interacting subunit 1;
DE Short=AtALIS1;
DE AltName: Full=ALA3 beta-subunit 1;
GN Name=ALIS1; OrderedLocusNames=At3g12740; ORFNames=MBK21.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ALA3.
RX PubMed=18344284; DOI=10.1105/tpc.107.054767;
RA Poulsen L.R., Lopez-Marques R.L., McDowell S.C., Okkeri J., Licht D.,
RA Schulz A., Pomorski T., Harper J.F., Palmgren M.G.;
RT "The Arabidopsis P4-ATPase ALA3 localizes to the Golgi and requires a beta-
RT subunit to function in lipid translocation and secretory vesicle
RT formation.";
RL Plant Cell 20:658-676(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALA2 AND ALA3.
RX PubMed=20053675; DOI=10.1091/mbc.e09-08-0656;
RA Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K.,
RA Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.;
RT "Intracellular targeting signals and lipid specificity determinants of the
RT ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit.";
RL Mol. Biol. Cell 21:791-801(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Required for the lipid transport activity of the ALA/ALIS P4-
CC ATPase complex. {ECO:0000269|PubMed:18344284,
CC ECO:0000269|PubMed:20053675}.
CC -!- SUBUNIT: Associates with ALA3 to form a stable complex. Interacts with
CC ALA2 in a heterologous system. {ECO:0000269|PubMed:18344284,
CC ECO:0000269|PubMed:20053675}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein. Prevacuolar compartment membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=In a
CC heterologous system, the final intracellular localization after exit
CC from the endoplasmic reticulum is the prevacuolar compartment in the
CC presence of ALA2 and the Golgi in the presence of ALA3.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Found in petals and sepals, but not in reproductive tissues.
CC In siliques, detected in the upper part of the seed pod and in the area
CC between the seed pod and the stem, but not in developing seeds. Strong
CC expression in vascular shoot tissues and in stomatal guard cells of
CC young rosettes leaves. In roots, expressed in cells surrounding the
CC xylem and in central and peripheral columella cells.
CC {ECO:0000269|PubMed:18344284}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; AB024033; BAB02418.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75241.1; -; Genomic_DNA.
DR EMBL; AY045904; AAK76578.1; -; mRNA.
DR EMBL; AF410309; AAK95295.1; -; mRNA.
DR EMBL; AY091210; AAM14149.1; -; mRNA.
DR EMBL; AY087607; AAM65148.1; -; mRNA.
DR RefSeq; NP_566435.1; NM_112110.4.
DR AlphaFoldDB; Q9LTW0; -.
DR SMR; Q9LTW0; -.
DR STRING; 3702.AT3G12740.1; -.
DR TCDB; 8.A.27.1.4; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR iPTMnet; Q9LTW0; -.
DR PaxDb; Q9LTW0; -.
DR PRIDE; Q9LTW0; -.
DR ProteomicsDB; 244896; -.
DR EnsemblPlants; AT3G12740.1; AT3G12740.1; AT3G12740.
DR GeneID; 820456; -.
DR Gramene; AT3G12740.1; AT3G12740.1; AT3G12740.
DR KEGG; ath:AT3G12740; -.
DR Araport; AT3G12740; -.
DR TAIR; locus:2087695; AT3G12740.
DR eggNOG; KOG2952; Eukaryota.
DR HOGENOM; CLU_025025_1_1_1; -.
DR InParanoid; Q9LTW0; -.
DR OMA; HLDQPYE; -.
DR OrthoDB; 889671at2759; -.
DR PhylomeDB; Q9LTW0; -.
DR PRO; PR:Q9LTW0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTW0; baseline and differential.
DR Genevisible; Q9LTW0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IDA:TAIR.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR PANTHER; PTHR10926; PTHR10926; 1.
DR Pfam; PF03381; CDC50; 1.
DR PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..350
FT /note="ALA-interacting subunit 1"
FT /id="PRO_0000366954"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 350 AA; 39069 MW; 8B2BCDA56D82B1A6 CRC64;
MSSSNTPSSS AAAAGSIDSS AARRNSKRPK YSKFTQQELP ACKPILTPGW VISTFLIISV
IFIPLGVISL FASQDVVEIV DRYDSACIPL SDRANKVAYI QGTGNKSCTR TLIVPKRMKQ
PIYVYYQLEN FYQNHRRYVK SRSDSQLRSV KDENQIDACK PEDDFGGQPI VPCGLIAWSL
FNDTYVLSRN NQGLTVNKKG IAWKSDKEHK FGKNVFPKNF QKGNLTGGAS LDPNKPLSDQ
EDLIVWMRTA ALPTFRKLYG KIESDLEKGE NIQVTLQNNY NTYSFSGKKK LVLSTTSWLG
GKNDFLGIAY LTVGGICFVL ALAFTVMYLV KPRRLGDPTY LSWNRIPGGR
