PCL1_SCHPO
ID PCL1_SCHPO Reviewed; 242 AA.
AC Q9P6J2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Fe(2+)/Mn(2+) transporter pcl1;
DE AltName: Full=Pombe ccc1-like protein 1 {ECO:0000312|PomBase:SPBC1683.10c};
GN Name=pcl1 {ECO:0000312|EMBL:CAB91172.1}; ORFNames=SPBC1683.10c;
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] {ECO:0000312|EMBL:CAB91172.1}
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] {ECO:0000305}
RP INDUCTION.
RX PubMed=16963626; DOI=10.1128/ec.00199-06;
RA Mercier A., Pelletier B., Labbe S.;
RT "A transcription factor cascade involving Fep1 and the CCAAT-binding factor
RT Php4 regulates gene expression in response to iron deficiency in the
RT fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 5:1866-1881(2006).
RN [3] {ECO:0000305}
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] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP 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: Has a role in both calcium and manganese homeostasis.
CC Involved in the transfer of iron and Mn(2+) from the cytosol to the
CC vacuole for storage of these metals (By similarity).
CC {ECO:0000250|UniProtKB:P47818}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16823372}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P47818, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P47818, ECO:0000255}.
CC -!- INDUCTION: Transcriptionally repressed by CCAAT complex in response to
CC low iron supply conditions. {ECO:0000269|PubMed:16963626}.
CC -!- SIMILARITY: Belongs to the CCC1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB91172.1; -; Genomic_DNA.
DR RefSeq; NP_595066.1; NM_001020972.2.
DR AlphaFoldDB; Q9P6J2; -.
DR SMR; Q9P6J2; -.
DR BioGRID; 276441; 8.
DR STRING; 4896.SPBC1683.10c.1; -.
DR TCDB; 2.A.89.3.8; the vacuolar iron transporter (vit) family.
DR iPTMnet; Q9P6J2; -.
DR MaxQB; Q9P6J2; -.
DR PaxDb; Q9P6J2; -.
DR PRIDE; Q9P6J2; -.
DR EnsemblFungi; SPBC1683.10c.1; SPBC1683.10c.1:pep; SPBC1683.10c.
DR GeneID; 2539895; -.
DR KEGG; spo:SPBC1683.10c; -.
DR PomBase; SPBC1683.10c; pcl1.
DR VEuPathDB; FungiDB:SPBC1683.10c; -.
DR eggNOG; KOG4473; Eukaryota.
DR HOGENOM; CLU_038957_3_0_1; -.
DR InParanoid; Q9P6J2; -.
DR OMA; SRIGWLR; -.
DR PhylomeDB; Q9P6J2; -.
DR PRO; PR:Q9P6J2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; TAS:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; ISO:PomBase.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; ISO:PomBase.
DR GO; GO:0034755; P:iron ion transmembrane transport; ISO:PomBase.
DR GO; GO:0071421; P:manganese ion transmembrane transport; ISO:PomBase.
DR InterPro; IPR008217; Ccc1_fam.
DR PANTHER; PTHR31851; PTHR31851; 1.
DR Pfam; PF01988; VIT1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..242
FT /note="Fe(2+)/Mn(2+) transporter pcl1"
FT /id="PRO_0000355075"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..48
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..180
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P47818, ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 242 AA; 25625 MW; 155DCAB434885934 CRC64;
MWSIFEARPK EAHSVNKIGW LRASVLGAND GILSLSGLLV GVVAANADIK VILITGVAGL
MSGALSMAVG EYVSVSSQAD LEDADLQLER REMDADWDAE VDELAAIYRG RGLDEELSRT
VAVQLMEYNA LEAHARDELG INIHTTAKPT LAALSSAASF SVGGIFPLLT SLITPLEYLS
LVLPIATMFF LGMLGFVGAH IGGAKRVRAI LRAVVLGLLA MAATALVGRL LEIHALSLQY
AI
