CTR4_SCHPO
ID CTR4_SCHPO Reviewed; 289 AA.
AC O94722;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Copper transport protein ctr4;
DE Short=Copper transporter 4;
GN Name=ctr4; ORFNames=SPCC1393.10;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=FY254;
RX PubMed=10593913; DOI=10.1074/jbc.274.51.36252;
RA Labbe S., Pena M.M.O., Fernandes A.R., Thiele D.J.;
RT "A copper-sensing transcription factor regulates iron uptake genes in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 274:36252-36260(1999).
RN [2]
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 [3]
RP INTERACTION WITH CTR5, AND SUBCELLULAR LOCATION.
RX PubMed=11274192; DOI=10.1074/jbc.m102004200;
RA Zhou H., Thiele D.J.;
RT "Identification of a novel high affinity copper transport complex in the
RT fission yeast Schizosaccharomyces pombe.";
RL J. Biol. Chem. 276:20529-20535(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP 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: Required for high affinity copper (probably reduced Cu I)
CC transport into the cell.
CC -!- SUBUNIT: Interacts with ctr5. {ECO:0000269|PubMed:11274192}.
CC -!- INTERACTION:
CC O94722; Q9P7F9: ctr5; NbExp=2; IntAct=EBI-1561952, EBI-1561942;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11274192}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:11274192}.
CC -!- INDUCTION: By copper deprivation, and repressed by copper sufficiency.
CC -!- SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family.
CC SLC31A subfamily. {ECO:0000305}.
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DR EMBL; AF175405; AAD51064.1; -; Genomic_DNA.
DR EMBL; AJ243833; CAB52305.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB38165.1; -; Genomic_DNA.
DR PIR; T43663; T43663.
DR RefSeq; NP_587968.1; NM_001022959.2.
DR AlphaFoldDB; O94722; -.
DR BioGRID; 275315; 9.
DR IntAct; O94722; 1.
DR STRING; 4896.SPCC1393.10.1; -.
DR TCDB; 1.A.56.1.5; the copper transporter (ctr) family.
DR iPTMnet; O94722; -.
DR MaxQB; O94722; -.
DR PaxDb; O94722; -.
DR PRIDE; O94722; -.
DR EnsemblFungi; SPCC1393.10.1; SPCC1393.10.1:pep; SPCC1393.10.
DR GeneID; 2538731; -.
DR KEGG; spo:SPCC1393.10; -.
DR PomBase; SPCC1393.10; ctr4.
DR VEuPathDB; FungiDB:SPCC1393.10; -.
DR eggNOG; KOG3386; Eukaryota.
DR HOGENOM; CLU_079690_0_1_1; -.
DR InParanoid; O94722; -.
DR OMA; FITKHWH; -.
DR PhylomeDB; O94722; -.
DR PRO; PR:O94722; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0098705; P:copper ion import across plasma membrane; IMP:PomBase.
DR InterPro; IPR007274; Cop_transporter.
DR PANTHER; PTHR12483; PTHR12483; 1.
DR Pfam; PF04145; Ctr; 1.
PE 1: Evidence at protein level;
KW Copper; Copper transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Copper transport protein ctr4"
FT /id="PRO_0000195048"
FT TOPO_DOM 1..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 289 AA; 32020 MW; D6A07DF015B81322 CRC64;
MSFFSAAKQS LGNSLIKLGT SMAQNSQGPV DDSSLSQLEN LLPPLQILTA RAAMAAMNMS
NDTSMSGMNM TNSTTPMSGM NMTNSTTSMS GMNMSNSTTS MSGMNMTNTT TTAKASSCKL
SMYWNWYTID ACFITKHWHI TSKHMFVGSI FGIIFMMMAL ELVRRGQREF DRWCVRRFSP
ASNSCCHSGA PVHSGPSMAL RIFLHFLRSC FYLVQYIVAY IAMLLAMYYN GYVILFLFCG
TFFGYFLFGA DTISTKASSS VQTKTIVQVA DEKHEHDSSQ YSDTTPTTE
