ZNT2_HUMAN
ID ZNT2_HUMAN Reviewed; 323 AA.
AC Q9BRI3; Q71RC8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc transporter 2;
DE Short=ZnT-2;
DE AltName: Full=Solute carrier family 30 member 2;
GN Name=SLC30A2; Synonyms=ZNT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [5]
RP SUBUNIT, VARIANT TNZD ARG-87, AND CHARACTERIZATION OF VARIANT TNZD ARG-87.
RX PubMed=22733820; DOI=10.1074/jbc.m112.368159;
RA Lasry I., Seo Y.A., Ityel H., Shalva N., Pode-Shakked B., Glaser F.,
RA Berman B., Berezovsky I., Goncearenco A., Klar A., Levy J., Anikster Y.,
RA Kelleher S.L., Assaraf Y.G.;
RT "A dominant negative heterozygous G87R mutation in the zinc transporter,
RT ZnT-2 (SLC30A2), results in transient neonatal zinc deficiency.";
RL J. Biol. Chem. 287:29348-29361(2012).
RN [6]
RP VARIANT TNZD ARG-54, AND CHARACTERIZATION OF VARIANT TNZD ARG-54.
RX PubMed=17065149; DOI=10.1074/jbc.m605821200;
RA Chowanadisai W., Lonnerdal B., Kelleher S.L.;
RT "Identification of a mutation in SLC30A2 (ZnT-2) in women with low milk
RT zinc concentration that results in transient neonatal zinc deficiency.";
RL J. Biol. Chem. 281:39699-39707(2006).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22733820}.
CC -!- INTERACTION:
CC Q9BRI3; O95870: ABHD16A; NbExp=3; IntAct=EBI-8644112, EBI-348517;
CC Q9BRI3; Q08AM2: ADAM33; NbExp=8; IntAct=EBI-8644112, EBI-10225815;
CC Q9BRI3; Q9BZ11-2: ADAM33; NbExp=3; IntAct=EBI-8644112, EBI-10303054;
CC Q9BRI3; P41181: AQP2; NbExp=3; IntAct=EBI-8644112, EBI-12701138;
CC Q9BRI3; Q13520: AQP6; NbExp=3; IntAct=EBI-8644112, EBI-13059134;
CC Q9BRI3; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-8644112, EBI-12069500;
CC Q9BRI3; Q6UWT4: C5orf46; NbExp=5; IntAct=EBI-8644112, EBI-11986083;
CC Q9BRI3; P13236: CCL4; NbExp=8; IntAct=EBI-8644112, EBI-2873970;
CC Q9BRI3; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-8644112, EBI-10271156;
CC Q9BRI3; P25942: CD40; NbExp=3; IntAct=EBI-8644112, EBI-525714;
CC Q9BRI3; P11912: CD79A; NbExp=3; IntAct=EBI-8644112, EBI-7797864;
CC Q9BRI3; A0A0S2Z5R8: CD99L2; NbExp=3; IntAct=EBI-8644112, EBI-16434925;
CC Q9BRI3; Q6IBD0: CDW52; NbExp=3; IntAct=EBI-8644112, EBI-12011352;
CC Q9BRI3; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-8644112, EBI-18013275;
CC Q9BRI3; O43889-2: CREB3; NbExp=3; IntAct=EBI-8644112, EBI-625022;
CC Q9BRI3; O14569: CYB561D2; NbExp=3; IntAct=EBI-8644112, EBI-717654;
CC Q9BRI3; O00559: EBAG9; NbExp=3; IntAct=EBI-8644112, EBI-8787095;
CC Q9BRI3; P54852: EMP3; NbExp=3; IntAct=EBI-8644112, EBI-3907816;
CC Q9BRI3; P34910-2: EVI2B; NbExp=3; IntAct=EBI-8644112, EBI-17640610;
CC Q9BRI3; Q9Y624: F11R; NbExp=3; IntAct=EBI-8644112, EBI-742600;
CC Q9BRI3; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-8644112, EBI-18636064;
CC Q9BRI3; P14324: FDPS; NbExp=3; IntAct=EBI-8644112, EBI-948245;
CC Q9BRI3; O15552: FFAR2; NbExp=3; IntAct=EBI-8644112, EBI-2833872;
CC Q9BRI3; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-8644112, EBI-12175685;
CC Q9BRI3; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-8644112, EBI-713304;
CC Q9BRI3; Q8N3T1: GALNT15; NbExp=5; IntAct=EBI-8644112, EBI-3925203;
CC Q9BRI3; P36382: GJA5; NbExp=3; IntAct=EBI-8644112, EBI-750433;
CC Q9BRI3; P29033: GJB2; NbExp=3; IntAct=EBI-8644112, EBI-3905204;
CC Q9BRI3; O95377: GJB5; NbExp=3; IntAct=EBI-8644112, EBI-3909454;
CC Q9BRI3; P16278: GLB1; NbExp=3; IntAct=EBI-8644112, EBI-989638;
CC Q9BRI3; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-8644112, EBI-17231387;
CC Q9BRI3; Q8N6U8: GPR161; NbExp=3; IntAct=EBI-8644112, EBI-6255622;
CC Q9BRI3; O15529: GPR42; NbExp=3; IntAct=EBI-8644112, EBI-18076404;
CC Q9BRI3; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-8644112, EBI-13067820;
CC Q9BRI3; Q04756: HGFAC; NbExp=3; IntAct=EBI-8644112, EBI-1041722;
CC Q9BRI3; Q13651: IL10RA; NbExp=3; IntAct=EBI-8644112, EBI-1031656;
CC Q9BRI3; Q8N6L0: KASH5; NbExp=9; IntAct=EBI-8644112, EBI-749265;
CC Q9BRI3; O15554: KCNN4; NbExp=3; IntAct=EBI-8644112, EBI-2924473;
CC Q9BRI3; P01374: LTA; NbExp=5; IntAct=EBI-8644112, EBI-524105;
CC Q9BRI3; Q6FG55: LTA; NbExp=3; IntAct=EBI-8644112, EBI-11984863;
CC Q9BRI3; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-8644112, EBI-10329546;
CC Q9BRI3; Q5J8X5: MS4A13; NbExp=6; IntAct=EBI-8644112, EBI-12070086;
CC Q9BRI3; Q9Y375: NDUFAF1; NbExp=3; IntAct=EBI-8644112, EBI-741874;
CC Q9BRI3; Q8IXM6: NRM; NbExp=3; IntAct=EBI-8644112, EBI-10262547;
CC Q9BRI3; P35372-10: OPRM1; NbExp=3; IntAct=EBI-8644112, EBI-12807478;
CC Q9BRI3; A6NKB5-5: PCNX2; NbExp=3; IntAct=EBI-8644112, EBI-17616589;
CC Q9BRI3; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-8644112, EBI-18063495;
CC Q9BRI3; Q59EV6: PPGB; NbExp=3; IntAct=EBI-8644112, EBI-14210385;
CC Q9BRI3; P15151: PVR; NbExp=11; IntAct=EBI-8644112, EBI-3919694;
CC Q9BRI3; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-8644112, EBI-8652744;
CC Q9BRI3; P14151-2: SELL; NbExp=3; IntAct=EBI-8644112, EBI-17865914;
CC Q9BRI3; E9PK97: SERPING1; NbExp=3; IntAct=EBI-8644112, EBI-16434941;
CC Q9BRI3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-8644112, EBI-18159983;
CC Q9BRI3; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-8644112, EBI-17595455;
CC Q9BRI3; Q9Y6M5: SLC30A1; NbExp=4; IntAct=EBI-8644112, EBI-10982148;
CC Q9BRI3; Q6XR72: SLC30A10; NbExp=3; IntAct=EBI-8644112, EBI-13917996;
CC Q9BRI3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-8644112, EBI-8644112;
CC Q9BRI3; Q99726: SLC30A3; NbExp=7; IntAct=EBI-8644112, EBI-10294651;
CC Q9BRI3; O14863: SLC30A4; NbExp=4; IntAct=EBI-8644112, EBI-13918058;
CC Q9BRI3; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-8644112, EBI-10314552;
CC Q9BRI3; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-8644112, EBI-12898013;
CC Q9BRI3; P30825: SLC7A1; NbExp=3; IntAct=EBI-8644112, EBI-4289564;
CC Q9BRI3; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-8644112, EBI-13292283;
CC Q9BRI3; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-8644112, EBI-17280858;
CC Q9BRI3; Q9NYW4: TAS2R5; NbExp=3; IntAct=EBI-8644112, EBI-17933167;
CC Q9BRI3; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-8644112, EBI-13351685;
CC Q9BRI3; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-8644112, EBI-12845616;
CC Q9BRI3; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-8644112, EBI-18178701;
CC Q9BRI3; Q9H2L4: TMEM60; NbExp=5; IntAct=EBI-8644112, EBI-2852148;
CC Q9BRI3; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-8644112, EBI-12015604;
CC Q9BRI3; Q9NP84: TNFRSF12A; NbExp=9; IntAct=EBI-8644112, EBI-2851995;
CC Q9BRI3; Q12999: TSPAN31; NbExp=3; IntAct=EBI-8644112, EBI-17678331;
CC Q9BRI3; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-8644112, EBI-11988865;
CC Q9BRI3; Q9BWQ6: YIPF2; NbExp=3; IntAct=EBI-8644112, EBI-751204;
CC Q9BRI3; Q99376: Tfrc; Xeno; NbExp=3; IntAct=EBI-8644112, EBI-2112551;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17897319};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17897319}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Lysosome membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRI3-2; Sequence=VSP_039754;
CC -!- DISEASE: Zinc deficiency, transient neonatal (TNZD) [MIM:608118]: A
CC disorder occurring in breast-fed infants as a consequence of low milk
CC zinc concentration in their nursing mothers, which cannot be corrected
CC by maternal zinc supplementation. A large amount of zinc, an essential
CC trace mineral, is required for normal growth particularly in infants,
CC and breast milk normally contains adequate zinc to meet the requirement
CC for infants up to 4 to 6 months of age. Zinc deficiency can lead to
CC dermatitis, alopecia, decreased growth, and impaired immune function.
CC The disorder shows autosomal dominant inheritance with incomplete
CC penetrance. {ECO:0000269|PubMed:17065149, ECO:0000269|PubMed:22733820}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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; AF370409; AAQ15245.1; -; mRNA.
DR EMBL; AL391650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006251; AAH06251.1; -; mRNA.
DR CCDS; CCDS272.1; -. [Q9BRI3-1]
DR CCDS; CCDS30644.1; -. [Q9BRI3-2]
DR RefSeq; NP_001004434.1; NM_001004434.2. [Q9BRI3-2]
DR RefSeq; NP_115902.1; NM_032513.4. [Q9BRI3-1]
DR AlphaFoldDB; Q9BRI3; -.
DR SMR; Q9BRI3; -.
DR BioGRID; 113561; 99.
DR IntAct; Q9BRI3; 74.
DR MINT; Q9BRI3; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.4.3.6; the cation diffusion facilitator (cdf) family.
DR iPTMnet; Q9BRI3; -.
DR PhosphoSitePlus; Q9BRI3; -.
DR BioMuta; SLC30A2; -.
DR DMDM; 60390858; -.
DR MassIVE; Q9BRI3; -.
DR PeptideAtlas; Q9BRI3; -.
DR PRIDE; Q9BRI3; -.
DR ProteomicsDB; 78767; -. [Q9BRI3-1]
DR ProteomicsDB; 78768; -. [Q9BRI3-2]
DR Antibodypedia; 15992; 51 antibodies from 19 providers.
DR DNASU; 7780; -.
DR Ensembl; ENST00000374276.4; ENSP00000363394.3; ENSG00000158014.15. [Q9BRI3-2]
DR Ensembl; ENST00000374278.7; ENSP00000363396.3; ENSG00000158014.15. [Q9BRI3-1]
DR GeneID; 7780; -.
DR KEGG; hsa:7780; -.
DR MANE-Select; ENST00000374276.4; ENSP00000363394.3; NM_001004434.3; NP_001004434.1. [Q9BRI3-2]
DR UCSC; uc001blg.2; human. [Q9BRI3-1]
DR CTD; 7780; -.
DR DisGeNET; 7780; -.
DR GeneCards; SLC30A2; -.
DR HGNC; HGNC:11013; SLC30A2.
DR HPA; ENSG00000158014; Tissue enriched (pancreas).
DR MalaCards; SLC30A2; -.
DR MIM; 608118; phenotype.
DR MIM; 609617; gene.
DR neXtProt; NX_Q9BRI3; -.
DR OpenTargets; ENSG00000158014; -.
DR PharmGKB; PA35883; -.
DR VEuPathDB; HostDB:ENSG00000158014; -.
DR GeneTree; ENSGT00940000156072; -.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; Q9BRI3; -.
DR OMA; GHEKMLH; -.
DR OrthoDB; 973492at2759; -.
DR PhylomeDB; Q9BRI3; -.
DR TreeFam; TF313382; -.
DR PathwayCommons; Q9BRI3; -.
DR Reactome; R-HSA-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR SignaLink; Q9BRI3; -.
DR BioGRID-ORCS; 7780; 4 hits in 1060 CRISPR screens.
DR ChiTaRS; SLC30A2; human.
DR GenomeRNAi; 7780; -.
DR Pharos; Q9BRI3; Tbio.
DR PRO; PR:Q9BRI3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BRI3; protein.
DR Bgee; ENSG00000158014; Expressed in kidney epithelium and 92 other tissues.
DR Genevisible; Q9BRI3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061090; P:positive regulation of sequestering of zinc ion; IDA:BHF-UCL.
DR GO; GO:0061088; P:regulation of sequestering of zinc ion; IBA:GO_Central.
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; Disease variant; Ion transport; Lysosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole;
KW Zinc; Zinc transport.
FT CHAIN 1..323
FT /note="Zinc transporter 2"
FT /id="PRO_0000206094"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..126
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..200
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..323
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT VAR_SEQ 90
FT /note="V -> VGGYLAHSLAVMTDAAHLLTDFASMLISLFSLWMSSRPATKTMNFGW
FT QRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_039754"
FT VARIANT 54
FT /note="H -> R (in TNZD; there are lower free protein levels
FT compared to wild-type due to abnormal intracellular
FT perinuclear aggregation of the mutant protein which is most
FT likely due to protein misfolding; dbSNP:rs587776926)"
FT /evidence="ECO:0000269|PubMed:17065149"
FT /id="VAR_069309"
FT VARIANT 87
FT /note="G -> R (in TNZD; inactivating mutation inflicting a
FT dominant negative effect; the mutant protein shows
FT mislocalization being largely retained in the Golgi
FT apparatus or endoplasmic reticulum or in the perinuclear
FT region; dbSNP:rs185398527)"
FT /evidence="ECO:0000269|PubMed:22733820"
FT /id="VAR_069310"
SQ SEQUENCE 323 AA; 35178 MW; F487412DEC7B38CB CRC64;
MEAKEKQHLL DARPAIRSYT GSLWQEGAGW IPLPRPGLDL QAIELAAQSN HHCHAQKGPD
SHCDPKKGKA QRQLYVASAI CLLFMIGEVV EILGALVSVL SIWVVTGVLV YLAVERLISG
DYEIDGGTML ITSGCAVAVN IIMGLTLHQS GHGHSHGTTN QQEENPSVRA AFIHVIGDFM
QSMGVLVAAY ILYFKPEYKY VDPICTFVFS ILVLGTTLTI LRDVILVLME GTPKGVDFTA
VRDLLLSVEG VEALHSLHIW ALTVAQPVLS VHIAIAQNTD AQAVLKTASS RLQGKFHFHT
VTIQIEDYSE DMKDCQACQG PSD
