TTM1_CAEEL
ID TTM1_CAEEL Reviewed; 410 AA.
AC O45923; A0A0K3AU82; O45922;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc transporter ttm-1 {ECO:0000305};
DE AltName: Full=Toxin-regulated target of MAPK 1 {ECO:0000312|WormBase:Y39E4A.2b};
DE AltName: Full=Toxin-regulated target of p38MAPK {ECO:0000303|PubMed:23717214};
GN Name=ttm-1 {ECO:0000312|WormBase:Y39E4A.2b};
GN ORFNames=Y39E4A.2 {ECO:0000312|WormBase:Y39E4A.2b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15256590; DOI=10.1073/pnas.0404073101;
RA Huffman D.L., Abrami L., Sasik R., Corbeil J., van der Goot F.G.,
RA Aroian R.V.;
RT "Mitogen-activated protein kinase pathways defend against bacterial pore-
RT forming toxins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10995-11000(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF 145-PHE--ALA-360.
RX PubMed=23717214; DOI=10.1371/journal.pgen.1003522;
RA Roh H.C., Collier S., Deshmukh K., Guthrie J., Robertson J.D., Kornfeld K.;
RT "ttm-1 encodes CDF transporters that excrete zinc from intestinal cells of
RT C. elegans and act in a parallel negative feedback circuit that promotes
RT homeostasis.";
RL PLoS Genet. 9:E1003522-E1003522(2013).
CC -!- FUNCTION: Promotes excretion of zinc from intestinal cells into the
CC intestinal lumen in response to increased dietary zinc
CC (PubMed:23717214). Involved in cadmium resistance, possibly by
CC promoting its transport from cells (PubMed:15256590). Involved in
CC resistance to B.thuringiensis pore-forming toxin Cry5B downstream of
CC the sek-1 and pmk-1 MAPK kinase pathway (PubMed:15256590).
CC {ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:23717214}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform b]: Apical cell membrane
CC {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:Y39E4A.2b};
CC IsoId=O45923-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y39E4A.2a};
CC IsoId=O45923-2; Sequence=VSP_060102;
CC Name=c {ECO:0000312|WormBase:Y39E4A.2c};
CC IsoId=O45923-3; Sequence=VSP_060103;
CC -!- TISSUE SPECIFICITY: Isoform a: Expressed in the hypodermis and the
CC intestine. Isoform b: Expressed in the intestine, head neurons, seam
CC cells, hypodermis, and the vulva. {ECO:0000269|PubMed:23717214}.
CC -!- INDUCTION: By B.thuringiensis pore-forming toxin Cry5B
CC (PubMed:15256590). Isoform a: Not induced by zinc. Isoform b: Induced
CC by zinc specifically in intestinal cells (PubMed:23717214).
CC {ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:23717214}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hypersensitivity
CC to low, chronic doses of the B.thuringiensis pore-forming toxin Cry5B
CC and heavy metal Cd(2+) exposure. {ECO:0000269|PubMed:15256590}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; BX284603; CAA16327.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA16328.1; -; Genomic_DNA.
DR EMBL; BX284603; CTQ86604.1; -; Genomic_DNA.
DR PIR; T26756; T26756.
DR PIR; T26757; T26757.
DR RefSeq; NP_001299904.1; NM_001312975.1. [O45923-3]
DR RefSeq; NP_499691.1; NM_067290.3. [O45923-2]
DR RefSeq; NP_499692.1; NM_067291.5. [O45923-1]
DR AlphaFoldDB; O45923; -.
DR SMR; O45923; -.
DR DIP; DIP-25801N; -.
DR IntAct; O45923; 4.
DR STRING; 6239.Y39E4A.2b; -.
DR TCDB; 2.A.4.3.12; the cation diffusion facilitator (cdf) family.
DR PaxDb; O45923; -.
DR EnsemblMetazoa; Y39E4A.2a.1; Y39E4A.2a.1; WBGene00012712. [O45923-2]
DR EnsemblMetazoa; Y39E4A.2b.1; Y39E4A.2b.1; WBGene00012712. [O45923-1]
DR EnsemblMetazoa; Y39E4A.2c.1; Y39E4A.2c.1; WBGene00012712. [O45923-3]
DR GeneID; 176715; -.
DR KEGG; cel:CELE_Y39E4A.2; -.
DR UCSC; Y39E4A.2b; c. elegans.
DR CTD; 176715; -.
DR WormBase; Y39E4A.2a; CE16616; WBGene00012712; ttm-1. [O45923-2]
DR WormBase; Y39E4A.2b; CE16617; WBGene00012712; ttm-1. [O45923-1]
DR WormBase; Y39E4A.2c; CE50587; WBGene00012712; ttm-1. [O45923-3]
DR eggNOG; KOG1482; Eukaryota.
DR GeneTree; ENSGT00940000157545; -.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; O45923; -.
DR OMA; RATKMYA; -.
DR OrthoDB; 820567at2759; -.
DR PhylomeDB; O45923; -.
DR PRO; PR:O45923; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012712; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061088; P:regulation of sequestering of zinc ion; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR GO; GO:0093002; P:response to nematicide; IMP:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasmic vesicle; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc transport.
FT CHAIN 1..410
FT /note="Zinc transporter ttm-1"
FT /id="PRO_0000446893"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..129
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..208
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..97
FT /note="MTISMISPSSIRLSSDKRDSSSSNLPANIEEDTQSVSSSDSGVSADSIDHHH
FT HGHGHGHSHGGHGHSHTHNNDDSSSDCSGAGGGAHKHSHDEKYQK -> MAEIDVSDRR
FT GLVSDDENFAETFSTEEGDGEGGGGGDFVGRRSILTTHCHYWDENDDDMVARVERGGST
FT DSASSREDT (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060102"
FT VAR_SEQ 1..97
FT /note="MTISMISPSSIRLSSDKRDSSSSNLPANIEEDTQSVSSSDSGVSADSIDHHH
FT HGHGHGHSHGGHGHSHTHNNDDSSSDCSGAGGGAHKHSHDEKYQK -> MVARVERGGS
FT TDSASSREDT (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060103"
FT MUTAGEN 145..360
FT /note="Missing: In ok3503; Impaired zinc excretion in
FT response to increased levels of dietary zinc."
FT /evidence="ECO:0000269|PubMed:23717214"
SQ SEQUENCE 410 AA; 44082 MW; 8379EA941809270C CRC64;
MTISMISPSS IRLSSDKRDS SSSNLPANIE EDTQSVSSSD SGVSADSIDH HHHGHGHGHS
HGGHGHSHTH NNDDSSSDCS GAGGGAHKHS HDEKYQKGRR AEKVLWAVAA LSAVFIAAEF
VGGFWAQSLA IMTDAGHMLS DLLSFIISIF AIRCARLPAS KRLSFGYERA EVLGALTSVI
ILWVLTTVLV VVAIQRIVNN EHEVDADVML ITAGVGVLFN IVMGLVLHFG TGGHGHTHGG
HSSHGHAHDG KNVNVRAALI HVIGDLVQSI GVLIAALIIR FTGWTLADPI CTFLFSIIVL
FTTVTVMRDI FFVLMEATPS HYDLSDVKKA LSALEGVKGV HDLHLWSIGM DKTAFSVHLA
LESPNRAMEN VAEARSLIRR RFGVAVATVQ VEPFDEKIDS CDTCQQQETA
