HMT1_CAEEL
ID HMT1_CAEEL Reviewed; 801 AA.
AC G5EFD4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Heavy metal tolerance factor 1 {ECO:0000305};
GN Name=hmt-1 {ECO:0000303|PubMed:15840570, ECO:0000312|WormBase:W09D6.6};
GN ORFNames=W09D6.6 {ECO:0000312|WormBase:W09D6.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15840570; DOI=10.1074/jbc.m503362200;
RA Vatamaniuk O.K., Bucher E.A., Sundaram M.V., Rea P.A.;
RT "CeHMT-1, a putative phytochelatin transporter, is required for cadmium
RT tolerance in Caenorhabditis elegans.";
RL J. Biol. Chem. 280:23684-23690(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31053883; DOI=10.1007/s00018-019-03105-5;
RA Rakvacs Z., Kucsma N., Gera M., Igriczi B., Kiss K., Barna J., Kovacs D.,
RA Vellai T., Bencs L., Reisecker J.M., Szoboszlai N., Szakacs G.;
RT "The human ABCB6 protein is the functional homologue of HMT-1 proteins
RT mediating cadmium detoxification.";
RL Cell. Mol. Life Sci. 76:4131-4144(2019).
CC -!- FUNCTION: May play a pivotal role in the detoxification of heavy metals
CC such as cadmium but do not depend exclusively on phytochelatins (PC)
CC synthesis. {ECO:0000269|PubMed:15840570, ECO:0000269|PubMed:31053883}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15840570};
CC Multi-pass membrane protein {ECO:0000255}. Early endosome
CC {ECO:0000269|PubMed:31053883}. Late endosome
CC {ECO:0000269|PubMed:31053883}. Recycling endosome
CC {ECO:0000269|PubMed:31053883}.
CC -!- TISSUE SPECIFICITY: Expressed in coelomocytes, as well as in head and
CC tail neurons, and in the intestinal cells.
CC {ECO:0000269|PubMed:15840570}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hypersensitivity
CC to Cd(2+) and exhibit Cd(2+)-elicited changes in cellular morphology.
CC Even at the lowest Cd(2+) concentrations they arrest in the early
CC larval stages and eventually die. The intestinal epithelial cells of
CC hmt-1 RNAi worms upon exposure to toxic levels of Cd(2+) elaborate
CC punctate refractive inclusions within the vicinity of the nucleus.
CC {ECO:0000269|PubMed:15840570, ECO:0000269|PubMed:31053883}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; AF497513; AAM33380.1; -; mRNA.
DR EMBL; AF497514; AAM33381.1; -; Genomic_DNA.
DR EMBL; BX284603; CAB04947.3; -; Genomic_DNA.
DR PIR; T26313; T26313.
DR RefSeq; NP_001022812.1; NM_001027641.3.
DR AlphaFoldDB; G5EFD4; -.
DR SMR; G5EFD4; -.
DR STRING; 6239.W09D6.6; -.
DR EPD; G5EFD4; -.
DR PaxDb; G5EFD4; -.
DR PeptideAtlas; G5EFD4; -.
DR EnsemblMetazoa; W09D6.6.1; W09D6.6.1; WBGene00001815.
DR GeneID; 176540; -.
DR KEGG; cel:CELE_W09D6.6; -.
DR CTD; 41925; -.
DR WormBase; W09D6.6; CE31731; WBGene00001815; hmt-1.
DR eggNOG; KOG0056; Eukaryota.
DR GeneTree; ENSGT00940000156160; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; G5EFD4; -.
DR OMA; TDPWVRP; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; G5EFD4; -.
DR BRENDA; 7.2.2.2; 1045.
DR Reactome; R-CEL-1369007; Mitochondrial ABC transporters.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001815; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:WormBase.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IDA:WormBase.
DR GO; GO:0015439; F:ABC-type heme transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0070574; P:cadmium ion transmembrane transport; IDA:WormBase.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IDA:UniProtKB.
DR GO; GO:0071585; P:detoxification of cadmium ion; IMP:WormBase.
DR GO; GO:0010273; P:detoxification of copper ion; IMP:WormBase.
DR GO; GO:0015886; P:heme transport; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IMP:WormBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endosome; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..801
FT /note="Heavy metal tolerance factor 1"
FT /id="PRO_0000452719"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..101
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..167
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 248..264
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 286..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 365..371
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 391..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 483..489
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 511..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 227..516
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 550..784
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 583..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 801 AA; 90575 MW; BAB7C44C2A412686 CRC64;
MGFSPFLDEC RAEGLWPIGP SCNKIISFGV YTFFIVVNFI VLCIPNSNSA NNNYRRMTDD
DASSTSKLTI SKILSICTIF AVICQSIFYF CFTFYFHPYT HLLLAFCVSK LFFWILSLCS
FSKWRNQPST PISLAFAFSA ALLIHCIPLT DWKKYFEPTS KNRGDLTFYI IELALVTVVF
FFTIVTGLFN FSGCSSRESA WNNLSKKVVT VAPYIWPTKS ISLQLRVVFC LFLLIIGRLI
NVSLPILSKW IVDELATPDT FQYSLLFLAT FLKFLQGNGA MGGFLNTVRT YLWIPIQQYT
TRELEVELFK HLHSLSLRWH LSRKTGQVLR VMDRGTSSVN NILNYILFNV VPTIADIVIA
VIFFFSAFNA YFGLIVFGTM ALYLTVTISI TEWRTQYIRE ANEKDNATSA IATDSLINYE
TVKYYGNEEF EVNRFKNAIE SYQVTEWKTQ ASLAFLNCLQ NAIIGIGMIG GSVFVVYMIV
HEKTLTVGDY VLFTTYLLQL YTPLNFFGTI YRVIQKAFVD MENMFDLMND EVEVKDLPHA
LPYTDPRGTI SVKNLTFEYN TGLPVIKNIS FEIGNGQTVA LVGSSGSGKS TLIRLLFRLF
ESTEGSIEFD GIDVRNYTMH SLRQQIGIVP QDTVLFNDTI MYNIRFGRPD ASDEEVIEAA
KAAMIHEKIT SLPEGYATMV GERGLKLSGG EKQRVAIART ILKKPQFIFL DEATSALDTP
TERAIQKCLE KLCKSRTGVV VAHRLSTVVN ADLILVLDKG IILERGNHKE LLAQQGTYAS
MWEAQIAEQR AKSIELGEEL P
