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Database: UniProt
Entry: E3MFB2_CAERE
LinkDB: E3MFB2_CAERE
Original site: E3MFB2_CAERE 
ID   E3MFB2_CAERE            Unreviewed;       770 AA.
AC   E3MFB2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Proton-coupled zinc antiporter SLC30A5 {ECO:0000256|ARBA:ARBA00040846};
DE   AltName: Full=Solute carrier family 30 member 5 {ECO:0000256|ARBA:ARBA00042217};
DE   AltName: Full=Zinc transporter 5 {ECO:0000256|ARBA:ARBA00042038};
GN   ORFNames=CRE_20737 {ECO:0000313|EMBL:EFP01058.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out);
CC         Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00034428};
CC   -!- SUBUNIT: Heterodimer with SLC30A6/ZNT6; form a functional zinc ion
CC       transmembrane transporter. {ECO:0000256|ARBA:ARBA00038531}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004557}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004638}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004638}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004205}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004205}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; DS268441; EFP01058.1; -; Genomic_DNA.
DR   RefSeq; XP_003105160.1; XM_003105112.1.
DR   AlphaFoldDB; E3MFB2; -.
DR   STRING; 31234.E3MFB2; -.
DR   EnsemblMetazoa; CRE20737.1; CRE20737.1; WBGene00060873.
DR   eggNOG; KOG1484; Eukaryota.
DR   HOGENOM; CLU_013430_11_0_1; -.
DR   InParanoid; E3MFB2; -.
DR   OMA; NINTDRL; -.
DR   OrthoDB; 1218545at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:InterPro.
DR   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   InterPro; IPR045316; Msc2-like.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45755; -; 1.
DR   PANTHER; PTHR45755:SF1; ZINC TRANSPORTER 5; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        25..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        492..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        529..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        584..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        611..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          554..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  84858 MW;  20AC89E818385FD7 CRC64;
     MLAQDFVKKD DRNFTPTQSS RSASYFVVLV LTKILRCIGI FFVDILAKSS HIVNLLWLCK
     IICTCILFPL QKPLSAGKSL KRGLLPMILK LSLLNGVIEI LWFYGITLCG PLRSVLVFEL
     SSTVLLSAIV SFFKGGAVST TSKTRGFFLL IVGFVALFLM DKDGTIEDPH HTTHAHHSGL
     NHLFYHLIGL FGMADHKGGL CILILSLCLR TGYETTFRHL AVEVGGAKRL YTLVTAGSAV
     ILTPVAVLSW ALSSSSIASM GFFEYSILLI IVAVFVFVLD FYAESICFQH VADPIMAAAR
     WSSVTMFACA FGLAYLWYGH QNLGDHALTG GVSITVVCFI LGEFLKNFNQ IVVNGIEKLN
     SFFSASISLT HSNAPKHRGG QFVGISNTGL PLFTYGEAFL QKTSKSLMRF MKDTLNEILA
     NNDSRRIFWF LCVNLGFCGI EFLYGFWTNS LGLISDGFHM LFDCSALVMG LVASVMARWP
     PSKHFTFGFG RVEILSGFIN ALFLCVIALF ILIEALERLF DPPNINTDRL LFVAVSGLLV
     NLFGMYSLGE HGHSHGGSSH GHSHGGGGSH SHGHSHGNAN MQGVFLHVLA DTLGSVFVII
     STLLIQWFGW VWVDPLCSLI LSLLIIGSVY PLLVSSVNTL LQDIPEEDEF EYHVNEILEI
     EHVESYSNAH MWQHNDINVA SVHVQVKDEA NAQMVRHRVA NILKSTGAGH STVQVEKKAF
     AHRIQQLCPN YKIGYTVVRG SVIRDKTQHG HSHDDGHGHS HDHSGGGHHH
//
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