TSPO_ARATH
ID TSPO_ARATH Reviewed; 196 AA.
AC O82245;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translocator protein homolog;
DE Short=AtTSPO;
GN Name=TSPO; OrderedLocusNames=At2g47770; ORFNames=F17A22.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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.
RX PubMed=15215507; DOI=10.1093/pcp/pch088;
RA Lindemann P., Koch A., Degenhardt B., Hause G., Grimm B., Papadopoulos V.;
RT "A novel Arabidopsis thaliana protein is a functional peripheral-type
RT benzodiazepine receptor.";
RL Plant Cell Physiol. 45:723-733(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19548979; DOI=10.1111/j.1365-313x.2009.03950.x;
RA Guillaumot D., Guillon S., Deplanque T., Vanhee C., Gumy C., Masquelier D.,
RA Morsomme P., Batoko H.;
RT "The Arabidopsis TSPO-related protein is a stress and abscisic acid-
RT regulated, endoplasmic reticulum-Golgi-localized membrane protein.";
RL Plant J. 60:242-256(2009).
RN [6]
RP FUNCTION.
RX PubMed=19838071; DOI=10.4161/psb.4.11.9796;
RA Guillaumot D., Guillon S., Morsomme P., Batoko H.;
RT "ABA, porphyrins and plant TSPO-related protein.";
RL Plant Signal. Behav. 4:1087-1090(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21689410; DOI=10.1186/1471-2229-11-108;
RA Balsemao-Pires E., Jaillais Y., Olson B.J., Andrade L.R., Umen J.G.,
RA Chory J., Sachetto-Martins G.;
RT "The Arabidopsis translocator protein (AtTSPO) is regulated at multiple
RT levels in response to salt stress and perturbations in tetrapyrrole
RT metabolism.";
RL BMC Plant Biol. 11:108-108(2011).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20847098; DOI=10.1093/jxb/erq283;
RA Vanhee C., Guillon S., Masquelier D., Degand H., Deleu M., Morsomme P.,
RA Batoko H.;
RT "A TSPO-related protein localizes to the early secretory pathway in
RT Arabidopsis, but is targeted to mitochondria when expressed in yeast.";
RL J. Exp. Bot. 62:497-508(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-91 AND HIS-115.
RX PubMed=21317376; DOI=10.1105/tpc.110.081570;
RA Vanhee C., Zapotoczny G., Masquelier D., Ghislain M., Batoko H.;
RT "The Arabidopsis multistress regulator TSPO is a heme binding membrane
RT protein and a potential scavenger of porphyrins via an autophagy-dependent
RT degradation mechanism.";
RL Plant Cell 23:785-805(2011).
CC -!- FUNCTION: Stress-induced membrane protein that can bind heme and may
CC play a role in the transport of tetrapyrrole intermediates during salt
CC stress and contribute to the detoxification of highly reactive
CC porphyrins in the cytoplasm. {ECO:0000269|PubMed:15215507,
CC ECO:0000269|PubMed:19548979, ECO:0000269|PubMed:19838071,
CC ECO:0000269|PubMed:21317376, ECO:0000269|PubMed:21689410}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Plastid, chloroplast membrane; Multi-pass membrane protein.
CC Note=Localizes in chloroplast upon salt stress.
CC -!- TISSUE SPECIFICITY: Specifically expressed in seeds (at protein level).
CC {ECO:0000269|PubMed:19548979}.
CC -!- INDUCTION: By abscisic acid (ABA) and osmotic and salt stresses (at
CC protein level). Induced by methyl viologen.
CC {ECO:0000269|PubMed:19548979, ECO:0000269|PubMed:21689410}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19548979}.
CC -!- MISCELLANEOUS: Plants overexpressing TSPO show increased sensitivity to
CC ABA and salt stress. Cultured cells overexpressing TSPO have reduced
CC greening and chlorophyll a content under light-growing conditions.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AC005309; AAC63632.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10886.1; -; Genomic_DNA.
DR EMBL; AF428356; AAL16286.1; -; mRNA.
DR EMBL; AY045981; AAK76655.1; -; mRNA.
DR EMBL; AY079391; AAL85122.1; -; mRNA.
DR PIR; C84919; C84919.
DR RefSeq; NP_566110.1; NM_130344.2.
DR AlphaFoldDB; O82245; -.
DR SMR; O82245; -.
DR BioGRID; 4724; 13.
DR IntAct; O82245; 5.
DR STRING; 3702.AT2G47770.1; -.
DR TCDB; 9.A.24.1.3; the mitochondrial cholesterol/porphyrin/5-aminolevulinic acid uptake translocator protein (tspo) family.
DR PaxDb; O82245; -.
DR PRIDE; O82245; -.
DR ProteomicsDB; 232401; -.
DR EnsemblPlants; AT2G47770.1; AT2G47770.1; AT2G47770.
DR GeneID; 819389; -.
DR Gramene; AT2G47770.1; AT2G47770.1; AT2G47770.
DR KEGG; ath:AT2G47770; -.
DR Araport; AT2G47770; -.
DR TAIR; locus:2043358; AT2G47770.
DR eggNOG; ENOG502RZ33; Eukaryota.
DR HOGENOM; CLU_120171_0_0_1; -.
DR InParanoid; O82245; -.
DR OMA; WALHLTC; -.
DR OrthoDB; 1592225at2759; -.
DR PhylomeDB; O82245; -.
DR PRO; PR:O82245; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82245; baseline and differential.
DR Genevisible; O82245; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IDA:TAIR.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR CDD; cd15904; TSPO_MBR; 1.
DR Gene3D; 1.20.1260.100; -; 1.
DR InterPro; IPR038330; TspO/MBR-related_sf.
DR InterPro; IPR004307; TspO_MBR.
DR PANTHER; PTHR10057; PTHR10057; 1.
DR Pfam; PF03073; TspO_MBR; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Endoplasmic reticulum; Golgi apparatus; Membrane; Plastid;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..196
FT /note="Translocator protein homolog"
FT /id="PRO_0000415610"
FT TRANSMEM 47..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..196
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 91
FT /note="H->A: Unable to bind heme."
FT /evidence="ECO:0000269|PubMed:21317376"
FT MUTAGEN 115
FT /note="H->A: No effect on the ability to bind heme."
FT /evidence="ECO:0000269|PubMed:21317376"
SQ SEQUENCE 196 AA; 21062 MW; ACA367D6722291B3 CRC64;
MDSQDIRYRG GDDRDAATTA MAETERKSAD DNKGKRDQKR AMAKRGLKSL TVAVAAPVLV
TLFATYFLGT SDGYGNRAKS SSWIPPLWLL HTTCLASSGL MGLAAWLVWV DGGFHKKPNA
LYLYLAQFLL CLVWDPVTFR VGSGVAGLAV WLGQSAALFG CYKAFNEISP VAGNLVKPCL
AWAAFVAAVN VKLAVA
