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S-adenosylmethionine carrier 1, chloroplastic/mitochondrial (S-adenosylmethionine transporter 1) (AtSAMT1)

 SAMC1_ARATH             Reviewed;         325 AA.
Q94AG6; Q9SVB2;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 112.
RecName: Full=S-adenosylmethionine carrier 1, chloroplastic/mitochondrial;
AltName: Full=S-adenosylmethionine transporter 1;
Short=AtSAMT1;
Flags: Precursor;
Name=SAMC1; Synonyms=SAMT1; OrderedLocusNames=At4g39460;
ORFNames=F23K16.90;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
FUNCTION, SUBSTRATE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=17098813; DOI=10.1105/tpc.105.040741;
Bouvier F., Linka N., Isner J.C., Mutterer J., Weber A.P.M.,
Camara B.;
"Arabidopsis SAMT1 defines a plastid transporter regulating plastid
biogenesis and plant development.";
Plant Cell 18:3088-3105(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ENZYME
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=16950860; DOI=10.1104/pp.106.086975;
Palmieri L., Arrigoni R., Blanco E., Carrari F., Zanor M.I.,
Studart-Guimareas C., Fernie A.R., Palmieri F.;
"Molecular identification of an Arabidopsis S-adenosylmethionine
transporter. Analysis of organ distribution, bacterial expression,
reconstitution into liposomes, and functional characterization.";
Plant Physiol. 142:855-865(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
CLEAVAGE OF TRANSIT PEPTIDE AFTER ALA-38, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=cv. Wassilewskija;
PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200;
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis
thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
-!- FUNCTION: Transporter involved in exchange reactions through
membranes. Has a low uniporter activity. Specifically mediates the
transport of S-adenosylmethionine (SAM) and its closest analogs.
Probably involved in the uptake of SAM in exchange for S-
adenosylhomocysteine (SAHC), which is produced from SAM in the
mitochondrial matrix and plastidial stroma by methyltransferase
activities. {ECO:0000269|PubMed:16950860,
ECO:0000269|PubMed:17098813}.
-!- ENZYME REGULATION: Inhibited strongly by tannic acid, bromocresol
purple, mercuric chloride, mersalyl, p-hydroxymercuribenzoate, S-
adenosylhomocysteine, S-adenosylcysteine and adenosylornithine,
and to a lesser extent by N-ethylmaleimide, bathophenanthroline
and pyridoxal-5'-P. {ECO:0000269|PubMed:16950860}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=95 uM for the SAM/SAM exchange {ECO:0000269|PubMed:16950860};
Vmax=1.2 mmol/min/g enzyme {ECO:0000269|PubMed:16950860};
-!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
protein. Plastid, chloroplast membrane; Multi-pass membrane
protein. Note=Detected in chloroplast envelope, but not in
thylakoid membranes or in chloroplast stroma (PubMed:17098813).
According to another report, localization is restricted to the
mitochondria (PubMed:16950860). {ECO:0000269|PubMed:16950860,
ECO:0000269|PubMed:17098813}.
-!- TISSUE SPECIFICITY: Expressed in seedlings, cotyledons, leaves and
flowers. Lower levels of expression in stems and roots. Not
detected in senescent leaves, petals and pollen grains.
{ECO:0000269|PubMed:16950860, ECO:0000269|PubMed:17098813}.
-!- DISRUPTION PHENOTYPE: Severely growth-retarded phenotype and
reduced chlorophyll and plastoquinone contents. Unable to
germinate when homozygous. {ECO:0000269|PubMed:16950860,
ECO:0000269|PubMed:17098813}.
-!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB44681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ627908; CAF29517.1; -; mRNA.
EMBL; AM260490; CAJ91123.1; -; mRNA.
EMBL; AL078620; CAB44681.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161595; CAB80609.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE87074.1; -; Genomic_DNA.
EMBL; CP002687; AEE87075.1; -; Genomic_DNA.
EMBL; CP002687; ANM66368.1; -; Genomic_DNA.
EMBL; AY046052; AAK76726.1; -; mRNA.
EMBL; AY079349; AAL85080.1; -; mRNA.
PIR; T09362; T09362.
RefSeq; NP_001190968.1; NM_001204039.1.
RefSeq; NP_001328265.1; NM_001342543.1.
RefSeq; NP_568060.1; NM_120106.3.
UniGene; At.21435; -.
ProteinModelPortal; Q94AG6; -.
IntAct; Q94AG6; 1.
STRING; 3702.AT4G39460.1; -.
TCDB; 2.A.29.18.2; the mitochondrial carrier (mc) family.
PaxDb; Q94AG6; -.
EnsemblPlants; AT4G39460.1; AT4G39460.1; AT4G39460.
EnsemblPlants; AT4G39460.2; AT4G39460.2; AT4G39460.
EnsemblPlants; AT4G39460.3; AT4G39460.3; AT4G39460.
GeneID; 830101; -.
Gramene; AT4G39460.1; AT4G39460.1; AT4G39460.
Gramene; AT4G39460.2; AT4G39460.2; AT4G39460.
Gramene; AT4G39460.3; AT4G39460.3; AT4G39460.
KEGG; ath:AT4G39460; -.
Araport; AT4G39460; -.
TAIR; locus:2122452; AT4G39460.
eggNOG; KOG0768; Eukaryota.
eggNOG; ENOG4110BII; LUCA.
HOGENOM; HOG000038810; -.
InParanoid; Q94AG6; -.
KO; K15111; -.
OMA; LKTRVML; -.
OrthoDB; EOG09360K34; -.
PhylomeDB; Q94AG6; -.
Reactome; R-ATH-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
PRO; PR:Q94AG6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q94AG6; baseline and differential.
Genevisible; Q94AG6; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0000095; F:S-adenosyl-L-methionine transmembrane transporter activity; IDA:TAIR.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
GO; GO:0015805; P:S-adenosyl-L-methionine transport; IDA:TAIR.
Gene3D; 1.50.40.10; -; 2.
InterPro; IPR002067; Mit_carrier.
InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
InterPro; IPR023395; Mt_carrier_dom_sf.
Pfam; PF00153; Mito_carr; 3.
PRINTS; PR00926; MITOCARRIER.
SUPFAM; SSF103506; SSF103506; 1.
PROSITE; PS50920; SOLCAR; 3.
1: Evidence at protein level;
Chloroplast; Complete proteome; Membrane; Mitochondrion; Plastid;
Reference proteome; Repeat; S-adenosyl-L-methionine; Transit peptide;
Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 38 Chloroplast and mitochondrion.
{ECO:0000269|PubMed:12766230}.
CHAIN 39 325 S-adenosylmethionine carrier 1,
chloroplastic/mitochondrial.
/FTId=PRO_0000424771.
TRANSMEM 55 75 Helical. {ECO:0000255}.
TRANSMEM 97 117 Helical. {ECO:0000255}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TRANSMEM 285 305 Helical. {ECO:0000255}.
REPEAT 52 124 Solcar 1.
REPEAT 133 215 Solcar 2.
REPEAT 228 310 Solcar 3.
SEQUENCE 325 AA; 34861 MW; BBA74F93939E6318 CRC64;
MAPLTLSVDV KSSSATSHDV SKRVMQSSQL KINKGFFASV NTQEDKPFDF FRTLFEGFIA
GGTAGVVVET ALYPIDTIKT RLQAARGGGK IVLKGLYSGL AGNIAGVLPA SALFVGVYEP
TKQKLLKTFP DHLSAVAHLT AGAIGGLAAS LIRVPTEVVK QRMQTGQFTS APSAVRMIAS
KEGFRGLYAG YRSFLLRDLP FDAIQFCIYE QLCLGYKKAA RRELSDPENA LIGAFAGALT
GAVTTPLDVI KTRLMVQGSA KQYQGIVDCV QTIVREEGAP ALLKGIGPRV LWIGIGGSIF
FGVLESTKRT LAQRRPNTVK ETKEE


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