PDT1_SCHPO
ID PDT1_SCHPO Reviewed; 521 AA.
AC Q10177;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Manganese transporter pdt1;
GN Name=pdt1; ORFNames=SPAC27F1.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=14723709; DOI=10.1111/j.1356-9597.2004.00699.x;
RA Maeda T., Sugiura R., Kita A., Saito M., Deng L., He Y., Yabin L.,
RA Fujita Y., Takegawa K., Shuntoh H., Kuno T.;
RT "Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively
RT regulate cell morphogenesis in fission yeast: the importance of Mn2+
RT homeostasis.";
RL Genes Cells 9:71-82(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-43, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Transports manganese ions into the cell. Regulates cell
CC morphogenesis through control of manganese homeostasis.
CC {ECO:0000269|PubMed:14723709}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93297.1; -; Genomic_DNA.
DR PIR; T38466; T38466.
DR RefSeq; NP_594537.1; NM_001019966.2.
DR AlphaFoldDB; Q10177; -.
DR SMR; Q10177; -.
DR BioGRID; 278751; 38.
DR STRING; 4896.SPAC27F1.08.1; -.
DR TCDB; 2.A.55.1.4; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR iPTMnet; Q10177; -.
DR SwissPalm; Q10177; -.
DR MaxQB; Q10177; -.
DR PaxDb; Q10177; -.
DR PRIDE; Q10177; -.
DR EnsemblFungi; SPAC27F1.08.1; SPAC27F1.08.1:pep; SPAC27F1.08.
DR GeneID; 2542283; -.
DR KEGG; spo:SPAC27F1.08; -.
DR PomBase; SPAC27F1.08; pdt1.
DR VEuPathDB; FungiDB:SPAC27F1.08; -.
DR eggNOG; KOG1291; Eukaryota.
DR HOGENOM; CLU_020088_4_2_1; -.
DR InParanoid; Q10177; -.
DR OMA; WGINSAM; -.
DR PhylomeDB; Q10177; -.
DR PRO; PR:Q10177; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IGI:PomBase.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0071421; P:manganese ion transmembrane transport; IMP:PomBase.
DR HAMAP; MF_00221; NRAMP; 1.
DR InterPro; IPR001046; NRAMP_fam.
DR PANTHER; PTHR11706; PTHR11706; 1.
DR Pfam; PF01566; Nramp; 1.
DR PRINTS; PR00447; NATRESASSCMP.
DR TIGRFAMs; TIGR01197; nramp; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Manganese; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..521
FT /note="Manganese transporter pdt1"
FT /id="PRO_0000212608"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 521 AA; 57641 MW; F14271E85FD7805A CRC64;
MSSQSYYMND LDDLRSLESS TLNKKDTAIN ELNPEQNDTR RSTDLLLEDK YGIQTGFSKY
WKKCTYGIRE YCKFIGPGFL IAVAYIDPGN YSTDLDAGSR FQYKLLFIVF LSNLFAVYLQ
SLCIRLGSVT GMDLARNCRE HYNRYICWSF YVLAEIAIIA TDIAEVIGTA VALKILMHIP
LVAGVVITIL DVLLVLIAWR PEGSMLSVRI FETAVALLVL VVAISFAVVL GRVHIGGAGT
VFKGFLPSST VFSREGLYSS IGILGATVMP HSLFLGSGLV QTRLRDLDVR RGNYTPVGDC
SDYRPTHETI KHSLTYSIVE VALSLFTFAL FTNSSILIVA GAVFYNTSGA DTSDLFSIYD
LLKEYVSISC GRLFAVALLF SGMSAGYVCT IAGQIVSEGY INWNLRPWLR RVITRAIAII
PCLVVSAAVG QSGLNQVLNA SQVCLSILLP FLTFPLVMFT CSRKVMRVVS DSTNEETGQL
IRETHDYSLG WTMTIVTWAI WLFLTALNLL LIVWLGMGVS F
