SAMC1_ARATH
ID SAMC1_ARATH Reviewed; 325 AA.
AC Q94AG6; Q9SVB2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=S-adenosylmethionine carrier 1, chloroplastic/mitochondrial;
DE AltName: Full=S-adenosylmethionine transporter 1;
DE Short=AtSAMT1;
DE Flags: Precursor;
GN Name=SAMC1; Synonyms=SAMT1; OrderedLocusNames=At4g39460;
GN ORFNames=F23K16.90;
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 [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP FUNCTION, SUBSTRATE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17098813; DOI=10.1105/tpc.105.040741;
RA Bouvier F., Linka N., Isner J.C., Mutterer J., Weber A.P.M., Camara B.;
RT "Arabidopsis SAMT1 defines a plastid transporter regulating plastid
RT biogenesis and plant development.";
RL Plant Cell 18:3088-3105(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16950860; DOI=10.1104/pp.106.086975;
RA Palmieri L., Arrigoni R., Blanco E., Carrari F., Zanor M.I.,
RA Studart-Guimareas C., Fernie A.R., Palmieri F.;
RT "Molecular identification of an Arabidopsis S-adenosylmethionine
RT transporter. Analysis of organ distribution, bacterial expression,
RT reconstitution into liposomes, and functional characterization.";
RL Plant Physiol. 142:855-865(2006).
RN [3]
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 [4]
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 [5]
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 [6]
RP CLEAVAGE OF TRANSIT PEPTIDE AFTER ALA-38, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
CC -!- FUNCTION: Transporter involved in exchange reactions through membranes.
CC Has a low uniporter activity. Specifically mediates the transport of S-
CC adenosylmethionine (SAM) and its closest analogs. Probably involved in
CC the uptake of SAM in exchange for S-adenosylhomocysteine (SAHC), which
CC is produced from SAM in the mitochondrial matrix and plastidial stroma
CC by methyltransferase activities. {ECO:0000269|PubMed:16950860,
CC ECO:0000269|PubMed:17098813}.
CC -!- ACTIVITY REGULATION: Inhibited strongly by tannic acid, bromocresol
CC purple, mercuric chloride, mersalyl, p-hydroxymercuribenzoate, S-
CC adenosylhomocysteine, S-adenosylcysteine and adenosylornithine, and to
CC a lesser extent by N-ethylmaleimide, bathophenanthroline and pyridoxal-
CC 5'-P. {ECO:0000269|PubMed:16950860}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95 uM for the SAM/SAM exchange {ECO:0000269|PubMed:16950860};
CC Vmax=1.2 mmol/min/g enzyme {ECO:0000269|PubMed:16950860};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein. Plastid, chloroplast membrane; Multi-pass membrane protein.
CC Note=Detected in chloroplast envelope, but not in thylakoid membranes
CC or in chloroplast stroma (PubMed:17098813). According to another
CC report, localization is restricted to the mitochondria
CC (PubMed:16950860). {ECO:0000269|PubMed:16950860,
CC ECO:0000269|PubMed:17098813}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, cotyledons, leaves and
CC flowers. Lower levels of expression in stems and roots. Not detected in
CC senescent leaves, petals and pollen grains.
CC {ECO:0000269|PubMed:16950860, ECO:0000269|PubMed:17098813}.
CC -!- DISRUPTION PHENOTYPE: Severely growth-retarded phenotype and reduced
CC chlorophyll and plastoquinone contents. Unable to germinate when
CC homozygous. {ECO:0000269|PubMed:16950860, ECO:0000269|PubMed:17098813}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB44681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ627908; CAF29517.1; -; mRNA.
DR EMBL; AM260490; CAJ91123.1; -; mRNA.
DR EMBL; AL078620; CAB44681.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87074.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87075.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66368.1; -; Genomic_DNA.
DR EMBL; AY046052; AAK76726.1; -; mRNA.
DR EMBL; AY079349; AAL85080.1; -; mRNA.
DR PIR; T09362; T09362.
DR RefSeq; NP_001190968.1; NM_001204039.1.
DR RefSeq; NP_001328265.1; NM_001342543.1.
DR RefSeq; NP_568060.1; NM_120106.3.
DR AlphaFoldDB; Q94AG6; -.
DR IntAct; Q94AG6; 1.
DR STRING; 3702.AT4G39460.2; -.
DR TCDB; 2.A.29.18.2; the mitochondrial carrier (mc) family.
DR PaxDb; Q94AG6; -.
DR PRIDE; Q94AG6; -.
DR ProteomicsDB; 232731; -.
DR EnsemblPlants; AT4G39460.1; AT4G39460.1; AT4G39460.
DR EnsemblPlants; AT4G39460.2; AT4G39460.2; AT4G39460.
DR EnsemblPlants; AT4G39460.3; AT4G39460.3; AT4G39460.
DR GeneID; 830101; -.
DR Gramene; AT4G39460.1; AT4G39460.1; AT4G39460.
DR Gramene; AT4G39460.2; AT4G39460.2; AT4G39460.
DR Gramene; AT4G39460.3; AT4G39460.3; AT4G39460.
DR KEGG; ath:AT4G39460; -.
DR Araport; AT4G39460; -.
DR TAIR; locus:2122452; AT4G39460.
DR eggNOG; KOG0768; Eukaryota.
DR HOGENOM; CLU_015166_3_0_1; -.
DR InParanoid; Q94AG6; -.
DR OMA; PRVGWIS; -.
DR OrthoDB; 1538959at2759; -.
DR PhylomeDB; Q94AG6; -.
DR PRO; PR:Q94AG6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AG6; baseline and differential.
DR Genevisible; Q94AG6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0000095; F:S-adenosyl-L-methionine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0015805; P:S-adenosyl-L-methionine transport; IDA:TAIR.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Mitochondrion; Plastid; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..38
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:12766230"
FT CHAIN 39..325
FT /note="S-adenosylmethionine carrier 1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000424771"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 52..124
FT /note="Solcar 1"
FT REPEAT 133..215
FT /note="Solcar 2"
FT REPEAT 228..310
FT /note="Solcar 3"
SQ 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
