ALIS3_ARATH
ID ALIS3_ARATH Reviewed; 349 AA.
AC Q9SLK2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ALA-interacting subunit 3;
DE Short=AtALIS3;
GN Name=ALIS3; OrderedLocusNames=At1g54320; ORFNames=F20D21.14, F20D21_50;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 TISSUE SPECIFICITY, INTERACTION WITH ALA3, AND NOMENCLATURE.
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 [5]
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 [6]
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:0000250, ECO:0000269|PubMed:20053675}.
CC -!- SUBUNIT: Interacts with ALA2 and ALA3 in a heterologous system.
CC {ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}.
CC -!- INTERACTION:
CC Q9SLK2; Q93Z00: TCP14; NbExp=2; IntAct=EBI-4463103, EBI-4424563;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20053675}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20053675}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20053675}. Note=In a heterologous system, the final
CC intracellular localization after exit from the endoplasmic reticulum is
CC the prevacuolar compartment in the presence of ALA2 and the Golgi in
CC the presence of ALA3.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:18344284}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; AC005287; AAD25612.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33080.1; -; Genomic_DNA.
DR EMBL; AY045672; AAK74030.1; -; mRNA.
DR EMBL; AY053406; AAK96636.1; -; mRNA.
DR EMBL; AF446869; AAL38602.1; -; mRNA.
DR PIR; G96584; G96584.
DR RefSeq; NP_564656.1; NM_104310.4.
DR AlphaFoldDB; Q9SLK2; -.
DR SMR; Q9SLK2; -.
DR BioGRID; 27098; 33.
DR IntAct; Q9SLK2; 30.
DR STRING; 3702.AT1G54320.1; -.
DR iPTMnet; Q9SLK2; -.
DR SwissPalm; Q9SLK2; -.
DR PaxDb; Q9SLK2; -.
DR PRIDE; Q9SLK2; -.
DR ProteomicsDB; 244979; -.
DR EnsemblPlants; AT1G54320.1; AT1G54320.1; AT1G54320.
DR GeneID; 841873; -.
DR Gramene; AT1G54320.1; AT1G54320.1; AT1G54320.
DR KEGG; ath:AT1G54320; -.
DR Araport; AT1G54320; -.
DR TAIR; locus:2020018; AT1G54320.
DR eggNOG; KOG2952; Eukaryota.
DR HOGENOM; CLU_025025_1_1_1; -.
DR InParanoid; Q9SLK2; -.
DR OMA; TWNNDQP; -.
DR OrthoDB; 889671at2759; -.
DR PhylomeDB; Q9SLK2; -.
DR PRO; PR:Q9SLK2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SLK2; baseline and differential.
DR Genevisible; Q9SLK2; AT.
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; IBA:GO_Central.
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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033036; P:macromolecule localization; IEA:UniProt.
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..349
FT /note="ALA-interacting subunit 3"
FT /id="PRO_0000366956"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
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 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 349 AA; 38955 MW; 3B9110441D2D9C35 CRC64;
MSSNTASSSA GAAGSGDSSA ARKNSKRPKY SKFTQQELPA CKPILTPGWV ISTFLIVSVI
FIPLGVISLF ASQDVVEIVD RYDTECIPAP ARTNKVAYIQ GDGDKVCNRD LKVTKRMKQP
IYVYYQLENF YQNHRRYVKS RSDSQLRSTK YENQISACKP EDDVGGQPIV PCGLIAWSLF
NDTYALSRNN VSLAVNKKGI AWKSDKEHKF GNKVFPKNFQ KGNITGGATL DPRIPLSEQE
DLIVWMRTAA LPTFRKLYGK IESDLEMGDT IHVKLNNNYN TYSFNGKKKL VLSTTSWLGG
KNDFLGIAYL TVGGICFILA LAFTIMYLVK PRRLGDPSYL SWNRNPGGR
