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Heavy metal tolerance protein

 HMT1_SCHPO              Reviewed;         830 AA.
Q02592; O13675; Q9UQW7; Q9USI3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 3.
20-JUN-2018, entry version 146.
RecName: Full=Heavy metal tolerance protein;
Flags: Precursor;
Name=hmt1; ORFNames=SPCC737.09c, SPCC74.08c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SP223;
PubMed=1396551;
Ortiz D.F., Kreppel L., Speiser D.M., Scheel G., McDonald G., Ow D.W.;
"Heavy metal tolerance in the fission yeast requires an ATP-binding
cassette-type vacuolar membrane transporter.";
EMBO J. 11:3491-3499(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- FUNCTION: Involved in metal tolerance. Probably involved in the
transport of metal-bound phytochelatins. Compartmentalizes cadmium
within vacuoles, thereby protecting cells from cadmium toxicity.
-!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane
protein.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Heavy Metal importer (TC 3.A.1.210) subfamily.
{ECO:0000305}.
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EMBL; Z14055; CAA78419.1; -; mRNA.
EMBL; CU329672; CAA20865.1; -; Genomic_DNA.
PIR; S25198; S25198.
RefSeq; NP_588371.3; NM_001023362.3.
ProteinModelPortal; Q02592; -.
SMR; Q02592; -.
BioGrid; 280210; 19.
STRING; 4896.SPCC737.09c.1; -.
TCDB; 3.A.1.210.2; the atp-binding cassette (abc) superfamily.
MaxQB; Q02592; -.
PaxDb; Q02592; -.
PRIDE; Q02592; -.
EnsemblFungi; SPCC737.09c.1; SPCC737.09c.1:pep; SPCC737.09c.
GeneID; 3361134; -.
KEGG; spo:SPCC737.09c; -.
EuPathDB; FungiDB:SPCC737.09c; -.
PomBase; SPCC737.09c; hmt1.
InParanoid; Q02592; -.
OMA; SNLWISV; -.
OrthoDB; EOG092C3H79; -.
PhylomeDB; Q02592; -.
Reactome; R-SPO-1369007; Mitochondrial ABC transporters.
PRO; PR:Q02592; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IDA:PomBase.
GO; GO:0005524; F:ATP binding; ISM:PomBase.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IMP:PomBase.
GO; GO:0044604; F:phytochelatin transmembrane transporter ATPase activity; IMP:PomBase.
GO; GO:0036249; P:cadmium ion import into vacuole; IMP:PomBase.
GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
GO; GO:0071996; P:glutathione transmembrane import into vacuole; IMP:PomBase.
GO; GO:0036246; P:phytochelatin 2 import into vacuole; IMP:PomBase.
GO; GO:0071995; P:phytochelatin import into vacuole; IMP:PomBase.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
2: Evidence at transcript level;
ATP-binding; Cadmium resistance; Complete proteome; Glycoprotein;
Membrane; Nucleotide-binding; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport; Vacuole.
SIGNAL 1 27
CHAIN 28 830 Heavy metal tolerance protein.
/FTId=PRO_0000000259.
TRANSMEM 51 71 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 88 108 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 126 146 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 156 176 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 263 283 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 304 324 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 381 401 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 403 423 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 490 511 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 265 550 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 584 818 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 617 628 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 429 433 Glutathione binding. {ECO:0000250}.
REGION 492 495 Glutathione binding. {ECO:0000250}.
BINDING 542 542 Glutathione; via amide nitrogen.
{ECO:0000250}.
BINDING 593 593 ATP. {ECO:0000250}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 79 79 R -> A (in Ref. 1; CAA78419).
{ECO:0000305}.
CONFLICT 439 439 S -> T (in Ref. 1; CAA78419).
{ECO:0000305}.
CONFLICT 812 812 A -> R (in Ref. 1; CAA78419).
{ECO:0000305}.
SEQUENCE 830 AA; 93994 MW; 909FBD10D51F50A9 CRC64;
MVLRYNSPRL NILELVLLYV GFFSIGSLNL LQKRKATSDP YRRKNRFGKE PIGIISWWIL
GIALTYVVDI SNLVIYALRV PNWWPCKTTV VCLILFLLFW IIVLISCADS KALPKNADSI
LKAYRLSVLY VWAIDIVFET IFIVYSPHPN ETFQGIVLAD HVARLVLCVF ATAIYLTYRR
KRHTHDPLDF EERQLTEESN VNENAISQNP STVQLGVSAS TSNFGTLKST SKKPSDKSWA
EYFRSFSTLL PYLWPTKDYR LQFQIFICIV LLFLGRAVNI LAPRQLGVLT EKLTKHSEKI
PWSDVILFVI YRFLQGNMGV IGSLRSFLWV PVSQYAYRAI STKALRHVLN LSYDFHLNKR
AGEVLTALTK GSSLNTFAEQ VVFQIGPVLL DLGVAMVYFF IKFDIYFTLI VLIMTLCYCY
VTVKITSWRT EARRKMVNSW RESYAVQNDA IMNFETVKNF DADDFENERY GHAVDIYLKQ
ERKVLFSLNF LNIVQGGIFT FSLAIACLLS AYRVTFGFNT VGDFVILLTY MIQLQQPLNF
FGTLYRSLQN SIIDTERLLE IFEEKPTVVE KPNAPDLKVT QGKVIFSHVS FAYDPRKPVL
SDINFVAQPG KVIALVGESG GGKSTIMRIL LRFFDVNSGS ITIDDQDIRN VTLSSLRSSI
GVVPQDSTLF NDTILYNIKY AKPSATNEEI YAAAKAAQIH DRILQFPDGY NSRVGERGLK
LSGGEKQRVA VARAILKDPS IILLDEATSA LDTNTERQIQ AALNRLASGR TAIVIAHRLS
TITNADLILC ISNGRIVETG THEELIKRDG GAYKKMWFQQ AMGKTSAETH


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