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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
 
 
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