LAZ1_ARATH
ID LAZ1_ARATH Reviewed; 485 AA.
AC F4JTN2; Q94AJ4; Q9SVE9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein LAZ1 {ECO:0000303|PubMed:20830211};
DE AltName: Full=Lazarus1 {ECO:0000303|PubMed:20830211};
GN Name=LAZ1 {ECO:0000303|PubMed:20830211};
GN OrderedLocusNames=At4g38360 {ECO:0000312|Araport:AT4G38360};
GN ORFNames=F22I13.130 {ECO:0000312|EMBL:CAB37492.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 2).
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 FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-360, TOPOLOGY,
RP SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=20830211; DOI=10.1371/journal.pone.0012586;
RA Malinovsky F.G., Brodersen P., Fiil B.K., McKinney L.V., Thorgrimsen S.,
RA Beck M., Nielsen H.B., Pietra S., Zipfel C., Robatzek S., Petersen M.,
RA Hofius D., Mundy J.;
RT "Lazarus1, a DUF300 protein, contributes to programmed cell death
RT associated with Arabidopsis acd11 and the hypersensitive response.";
RL PLoS ONE 5:E12586-E12586(2010).
CC -!- FUNCTION: Required for programmed cell death (PCD) associated with
CC hypersensitive response (HR). Involved both in the induction of
CC EDS1/PAD4 mediated HR and in accelerated cell death in the acd11
CC mutant. Not required for HR induction elicited through pathways
CC exclusively dependent on CC-NB-LRR resistance proteins.
CC {ECO:0000269|PubMed:20830211}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20830211}. Cell membrane
CC {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20830211}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:20830211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JTN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JTN2-2; Sequence=VSP_057592, VSP_057593;
CC -!- DISRUPTION PHENOTYPE: Suppresses acd11-dependent cell death. Laz1 acd11
CC double mutants survive throughout development to flower and set seeds,
CC in contrast to the fate of acd11. {ECO:0000269|PubMed:20830211}.
CC -!- SIMILARITY: Belongs to the TMEM184 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035539; CAB37492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80501.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86918.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86919.1; -; Genomic_DNA.
DR EMBL; AY046005; AAK76679.1; -; mRNA.
DR EMBL; AY079383; AAL85114.1; -; mRNA.
DR PIR; T05664; T05664.
DR RefSeq; NP_568039.1; NM_119998.2. [F4JTN2-2]
DR RefSeq; NP_974706.1; NM_202977.1. [F4JTN2-1]
DR AlphaFoldDB; F4JTN2; -.
DR STRING; 3702.AT4G38360.2; -.
DR iPTMnet; F4JTN2; -.
DR PaxDb; F4JTN2; -.
DR PRIDE; F4JTN2; -.
DR ProteomicsDB; 238555; -. [F4JTN2-1]
DR EnsemblPlants; AT4G38360.1; AT4G38360.1; AT4G38360. [F4JTN2-2]
DR EnsemblPlants; AT4G38360.2; AT4G38360.2; AT4G38360. [F4JTN2-1]
DR GeneID; 829993; -.
DR Gramene; AT4G38360.1; AT4G38360.1; AT4G38360. [F4JTN2-2]
DR Gramene; AT4G38360.2; AT4G38360.2; AT4G38360. [F4JTN2-1]
DR KEGG; ath:AT4G38360; -.
DR Araport; AT4G38360; -.
DR TAIR; locus:2121763; AT4G38360.
DR eggNOG; KOG2641; Eukaryota.
DR HOGENOM; CLU_012923_0_0_1; -.
DR InParanoid; F4JTN2; -.
DR OMA; LETHEPI; -.
DR PRO; PR:F4JTN2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTN2; baseline and differential.
DR Genevisible; F4JTN2; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:InterPro.
DR GO; GO:0012501; P:programmed cell death; IMP:UniProtKB.
DR GO; GO:0007033; P:vacuole organization; IGI:TAIR.
DR GO; GO:0098876; P:vesicle-mediated transport to the plasma membrane; IGI:TAIR.
DR InterPro; IPR031171; LAZ1.
DR InterPro; IPR005178; Ostalpha/TMEM184C.
DR PANTHER; PTHR23423; PTHR23423; 1.
DR PANTHER; PTHR23423:SF77; PTHR23423:SF77; 1.
DR Pfam; PF03619; Solute_trans_a; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..485
FT /note="Protein LAZ1"
FT /id="PRO_0000432837"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..53
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 168..188
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..196
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 197..217
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 242..262
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..277
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20830211"
FT TRANSMEM 278..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20830211"
FT REGION 400..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 384..415
FT /evidence="ECO:0000255"
FT COMPBIAS 400..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 285..304
FT /note="MGIASVVHLYVFPAKPYGLM -> CRWVLLPLFTCMYSQQSLMV (in
FT isoform 2)"
FT /id="VSP_057592"
FT VAR_SEQ 305..485
FT /note="Missing (in isoform 2)"
FT /id="VSP_057593"
FT MUTAGEN 360
FT /note="D->N: In laz1-4; Altered subcellular localization
FT and reduced activity."
FT /evidence="ECO:0000269|PubMed:20830211"
SQ SEQUENCE 485 AA; 54711 MW; 5C7270BEDD312A45 CRC64;
MDILKSYHLL AAAYSAPAWA SFMAGAFLVL TLSLSLFLVF DHLSTYKNPE EQKFLIGVIL
MVPCYSIESF ASLVKPSISV DCGILRDCYE SFAMYCFGRY LVACIGGEER TIEFMERQGR
KSFKTPLLDH KDEKGIIKHP FPMNLFLKPW RLSPWFYQVV KFGIVQYMII KSLTALTALI
LEAFGVYCEG EFKWGCGYPY LAVVLNFSQS WALYCLVQFY GATKDELAHI QPLAKFLTFK
SIVFLTWWQG VAIALLSSLG LFKSSIAQSL QLKTSVQDFI ICIEMGIASV VHLYVFPAKP
YGLMGDRFTG SVSVLGDYAS VDCPIDPDEI RDSERPTKVR LPHPDVDIRS GMTIKESMRD
VFVGGGEYIV KDVRFTVTQA VEPMEKSITK FNEKLHKISQ NIKKHDKEKR RVKDDSCMSS
SPSRRVIRGI DDPLLNGSFS DSGVTRTKKH RRKSGYTSAE SGGESSSDQA YGGFEVRGRR
WITKD
