ALIS5_ARATH
ID ALIS5_ARATH Reviewed; 350 AA.
AC Q8L8W0; Q9SAK3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ALA-interacting subunit 5;
DE Short=AtALIS5;
GN Name=ALIS5; OrderedLocusNames=At1g79450; ORFNames=T8K14.13;
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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH 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).
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L8W0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L8W0-2; Sequence=VSP_036590, VSP_036591;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30230.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX816946; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007202; AAD30230.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36244.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36245.1; -; Genomic_DNA.
DR EMBL; AY088777; AAM67090.1; -; mRNA.
DR EMBL; BX816946; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F96825; F96825.
DR RefSeq; NP_565210.1; NM_106593.4. [Q8L8W0-1]
DR RefSeq; NP_974175.1; NM_202446.1. [Q8L8W0-2]
DR AlphaFoldDB; Q8L8W0; -.
DR SMR; Q8L8W0; -.
DR STRING; 3702.AT1G79450.1; -.
DR PaxDb; Q8L8W0; -.
DR PRIDE; Q8L8W0; -.
DR ProteomicsDB; 244938; -. [Q8L8W0-1]
DR EnsemblPlants; AT1G79450.1; AT1G79450.1; AT1G79450. [Q8L8W0-1]
DR EnsemblPlants; AT1G79450.2; AT1G79450.2; AT1G79450. [Q8L8W0-2]
DR GeneID; 844283; -.
DR Gramene; AT1G79450.1; AT1G79450.1; AT1G79450. [Q8L8W0-1]
DR Gramene; AT1G79450.2; AT1G79450.2; AT1G79450. [Q8L8W0-2]
DR KEGG; ath:AT1G79450; -.
DR Araport; AT1G79450; -.
DR TAIR; locus:2206400; AT1G79450.
DR eggNOG; KOG2952; Eukaryota.
DR InParanoid; Q8L8W0; -.
DR OMA; RWVILTF; -.
DR PhylomeDB; Q8L8W0; -.
DR PRO; PR:Q8L8W0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L8W0; baseline and differential.
DR Genevisible; Q8L8W0; 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:0005739; C:mitochondrion; 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; Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SLK2"
FT CHAIN 2..350
FT /note="ALA-interacting subunit 5"
FT /id="PRO_0000366958"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
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:0000250|UniProtKB:Q9SLK2"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036590"
FT VAR_SEQ 68..74
FT /note="CLFASQG -> MFHSYLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036591"
FT CONFLICT 79
FT /note="V -> F (in Ref. 4; BX816946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38909 MW; 8F52E7AC7A08D8CF CRC64;
MSSTAASSTV GGGGSSEISG VKKTSKRPKY SRFTQQELPA CKPILTPRWV ILTFLVAGVV
FIPLGVICLF ASQGVVEIVD RYDTDCIPTS SRNNMVAYIQ GEGDKICKRT ITVTKAMKHP
VYVYYQLENF YQNHRRYVKS RNDAQLRSPK EEHDVKTCAP EDNVGGEPIV PCGLVAWSLF
NDTYSFSRNS QQLLVNKKGI SWKSDRENKF GKNVFPKNFQ KGAPIGGGTL NISKPLSEQE
DLIVWMRTAA LPTFRKLYGK IETDLHAGDT ITVLLQNNYN TYSFNGQKKL VLSTTSWLGG
RNDFLGIAYL TVGSICLFLA VTFAVLYLVK PRQLGDPSYL SWNRSAGGLQ
