MOT1_CHLRE
ID MOT1_CHLRE Reviewed; 519 AA.
AC A6YCJ2; A8J9T7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Molybdate transporter 1;
GN Name=MOT1; Synonyms=SULTR4; ORFNames=CHLREDRAFT_151770;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND INDUCTION BY NITRATE.
RC STRAIN=21gr / CC-1690, and 704;
RX PubMed=18077439; DOI=10.1073/pnas.0704646104;
RA Tejada-Jimenez M., Llamas A., Sanz-Luque E., Galvan A., Fernandez E.;
RT "A high-affinity molybdate transporter in eukaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20126-20130(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-486.
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- FUNCTION: High affinity molybdate transporter. Acts through an energy-
CC dependent process. {ECO:0000269|PubMed:18077439}.
CC -!- ACTIVITY REGULATION: 60% inhibition by 20 uM tungstate or by lack of
CC glucose in the medium, but no inhibition by sulfate.
CC {ECO:0000269|PubMed:18077439}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 nM for molybdate anion {ECO:0000269|PubMed:18077439};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by nitrate, but not by molybdate.
CC {ECO:0000269|PubMed:18077439}.
CC -!- DISRUPTION PHENOTYPE: Decreased nitrate reductase activity due to a
CC reduced molybdate uptake. No effect in strain 704 due to the presence
CC of a second molybdate transporter. {ECO:0000269|PubMed:18077439}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; EF437943; ABR24508.1; -; mRNA.
DR EMBL; DS496147; EDO99355.1; -; Genomic_DNA.
DR AlphaFoldDB; A6YCJ2; -.
DR STRING; 3055.EDO99355; -.
DR TCDB; 2.A.53.5.2; the sulfate permease (sulp) family.
DR PaxDb; A6YCJ2; -.
DR EnsemblPlants; PNW83960; PNW83960; CHLRE_04g214050v5.
DR GeneID; 5724237; -.
DR Gramene; PNW83960; PNW83960; CHLRE_04g214050v5.
DR eggNOG; ENOG502QRGR; Eukaryota.
DR HOGENOM; CLU_032158_0_1_1; -.
DR InParanoid; A6YCJ2; -.
DR OMA; AGMLCHW; -.
DR OrthoDB; 684963at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015098; F:molybdate ion transmembrane transporter activity; IDA:UniProtKB.
DR InterPro; IPR031563; MOT1/MOT2.
DR PANTHER; PTHR31970; PTHR31970; 1.
DR Pfam; PF16983; MFS_MOT1; 2.
PE 1: Evidence at protein level;
KW Membrane; Molybdenum; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..519
FT /note="Molybdate transporter 1"
FT /id="PRO_0000417395"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 519 AA; 53012 MW; 4196C7CE1ABA87C0 CRC64;
MALQNAWQNT KERARETWAQ LTWSEVSGSL GDLGTFLPLL IGLVQKVHLD LGTTLTITGL
YNIISGWQFR IPMCVQPMKT IAAVALAGGA AGLDLPQLLH AGLFVAGCVG LLGASQAIDL
FNWLVPPPVI RGVQLAVGVK LAMKGVDMAL RLHGGPSSGW RPWLGTEGLV VGAVALAAMI
ATTLPPRAAR RGTLEAADEG GLGPRPTDTA FEPLLRRLPA CCGGGDRAPQ VEGAAVSAER
AGLLAHAEGG ERSGNLDDGT EAGVGAAAGG GGCGGGGGGG RIPSALIAVV VGLAMAVLHR
PGLVWELRLG PTLPRLLRPS WPDFKTGALR GGLPQLPLTT LNSVIAVTQL ANALFGDKPE
AERRRWRPSA VALSVALLNG AGVWLGAMPC CHGAGGLAAQ YKFGARTGHA PILLGCIKAA
LGLLFGGSLV VLLEAFPQPL LGALLTVSGI ELASVVRHTR SPRGYTFALL TAVAILALDN
TGTGFLVGLV GVAAVAAYEG AVAAAAARWP RVFARGGRA
