ZNT4_RAT
ID ZNT4_RAT Reviewed; 430 AA.
AC O55174;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Zinc transporter 4 {ECO:0000305|PubMed:10600821};
DE Short=ZnT-4;
DE AltName: Full=Dri 27 protein {ECO:0000303|PubMed:10600821};
DE AltName: Full=Solute carrier family 30 member 4 {ECO:0000312|RGD:619750};
GN Name=Slc30a4 {ECO:0000312|RGD:619750};
GN Synonyms=Znt4 {ECO:0000303|PubMed:10600821};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION, AND REGION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=10600821; DOI=10.1152/ajpgi.1999.277.6.g1231;
RA Murgia C., Vespignani I., Cerase J., Nobili F., Perozzi G.;
RT "Cloning, expression, and vesicular localization of zinc transporter Dri
RT 27/ZnT4 in intestinal tissue and cells.";
RL Am. J. Physiol. 277:G1231-G1239(1999).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=12388418; DOI=10.1152/ajprenal.00094.2002;
RA Ranaldi G., Perozzi G., Truong-Tran A., Zalewski P., Murgia C.;
RT "Intracellular distribution of labile Zn(II) and zinc transporter
RT expression in kidney and MDCK cells.";
RL Am. J. Physiol. 283:F1365-F1375(2002).
CC -!- FUNCTION: Zinc ion transporter mediating zinc import from cytoplasm
CC potentially into the endocytic compartment (By similarity). Controls
CC zinc deposition in milk (By similarity). {ECO:0000250|UniProtKB:O14863,
CC ECO:0000250|UniProtKB:O35149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O14863};
CC -!- SUBUNIT: Homodimerization could regulate efficiency for zinc transport.
CC {ECO:0000250|UniProtKB:O14863}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:10600821};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within
CC the basal region of epithelial cells. {ECO:0000269|PubMed:10600821,
CC ECO:0000269|PubMed:12388418}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain and
CC testis. Also expressed in small intestine, medulla, lung, kidney,
CC stomach and colon. Expressed at lower level in other tissues.
CC {ECO:0000269|PubMed:10600821}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated in the intestine.
CC {ECO:0000269|PubMed:10600821}.
CC -!- INDUCTION: No change in response to zinc deprivation.
CC {ECO:0000269|PubMed:10600821}.
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; Y16774; CAA76372.1; -; mRNA.
DR RefSeq; NP_742063.1; NM_172066.1.
DR AlphaFoldDB; O55174; -.
DR SMR; O55174; -.
DR STRING; 10116.ENSRNOP00000000184; -.
DR PaxDb; O55174; -.
DR PRIDE; O55174; -.
DR GeneID; 64469; -.
DR KEGG; rno:64469; -.
DR UCSC; RGD:619750; rat.
DR CTD; 7782; -.
DR RGD; 619750; Slc30a4.
DR eggNOG; KOG1482; Eukaryota.
DR InParanoid; O55174; -.
DR OrthoDB; 820567at2759; -.
DR PhylomeDB; O55174; -.
DR PRO; PR:O55174; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0061088; P:regulation of sequestering of zinc ion; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0055069; P:zinc ion homeostasis; ISO:RGD.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IEP:RGD.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 2: Evidence at transcript level;
KW Endosome; Ion transport; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..430
FT /note="Zinc transporter 4"
FT /id="PRO_0000206101"
FT TOPO_DOM 1..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..143
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..216
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..311
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 240..265
FT /note="Zinc binding"
FT /evidence="ECO:0000269|PubMed:10600821"
FT REGION 245..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35149"
SQ SEQUENCE 430 AA; 47702 MW; F34CED3FA4FF05FB CRC64;
MAGPGAWKRL KSLLRKDDAP LFLNDTSAFD FLDEVSDEGL SRFNKLRVVV ADDDSEAPER
PVNGAHPALQ ADDDSLLDQE LPLTNSQLSL KMDPCDNCSK RRELLKQRKV KTRLTIAAVL
YLLFMIGELV GGYMANSLAI MTDALHMLTD LSAIILTLLA LWLSSKSPTR RFTFGFHRLE
VLSAMISVML VYVLMGFLLY EAMQRTIHMN YEINGDVMLI TAAVGVAVNV IMGFLLNQSG
HHHSHAHSHS LPSNSPSMVS SGHSHGQDSL AVRAAFVHAL GDLVQSVGVL IAAYIIRFKP
EYKIADPICT YIFSLLVAFT TLRIIWDTVV IILEGVPSHL NVDYIKESLM KIEDVYSVED
LNIWSLTSGK ATAIVHMQLI PGSSSKWEEV QSKAKHLLLN TFGMYKCTVQ LQSYRQEATR
TCANCQSSST
