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Zinc transporter ZIP4 (Activated in W/Wv mouse stomach 2) (mAWMS2) (Solute carrier family 39 member 4) (Zrt- and Irt-like protein 4) (ZIP-4)

 S39A4_MOUSE             Reviewed;         660 AA.
Q78IQ7; Q8CHL4;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 116.
RecName: Full=Zinc transporter ZIP4;
AltName: Full=Activated in W/Wv mouse stomach 2;
Short=mAWMS2;
AltName: Full=Solute carrier family 39 member 4;
AltName: Full=Zrt- and Irt-like protein 4;
Short=ZIP-4;
Flags: Precursor;
Name=Slc39a4; Synonyms=Zip4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=12801924; DOI=10.1074/jbc.M305000200;
Dufner-Beattie J., Wang F., Kuo Y.-M., Gitschier J., Eide D.,
Andrews G.K.;
"The acrodermatitis enteropathica gene ZIP4 encodes a tissue-specific,
zinc-regulated zinc transporter in mice.";
J. Biol. Chem. 278:33474-33481(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 431-660.
Daigo Y., Takayama I., Fujino M.A.;
"Isolation and characterization of novel human and mouse genes, which
are expressed in the digestive tract.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[5]
SUBCELLULAR LOCATION.
PubMed=14612438; DOI=10.1074/jbc.M310799200;
Kim B.-E., Wang F., Dufner-Beattie J., Andrews G.K., Eide D.J.,
Petris M.J.;
"Zn2+-stimulated endocytosis of the mZIP4 zinc transporter regulates
its location at the plasma membrane.";
J. Biol. Chem. 279:4523-4530(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays an important role in cellular zinc homeostasis as
a zinc transporter. Regulated in response to zinc availability.
{ECO:0000269|PubMed:12801924}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14612438};
Multi-pass membrane protein {ECO:0000269|PubMed:14612438}.
Recycling endosome membrane {ECO:0000269|PubMed:14612438}; Multi-
pass membrane protein {ECO:0000269|PubMed:14612438}.
Note=Colocalized with TFRC in the recycling endosomes. Cycles
between endosomal compartments and the plasma membrane in response
to zinc availability.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q78IQ7-1; Sequence=Displayed;
Note=More abundant.;
Name=2; Synonyms=Short;
IsoId=Q78IQ7-2; Sequence=VSP_015913, VSP_015914;
-!- TISSUE SPECIFICITY: Highly expressed in the small intestine and
embryonic visceral yolk sac. Weakly expressed in the stomach and
liver. Found to the apical surface of enterocytes and visceral
endoderm cells during zinc deficiency.
{ECO:0000269|PubMed:12801924}.
-!- INDUCTION: Up-regulated under conditions of dietary zinc
deficiency. Down-regulated under conditions of dietary zinc
excess. {ECO:0000269|PubMed:12801924}.
-!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK146977; BAE27581.1; -; mRNA.
EMBL; AK147107; BAE27679.1; -; mRNA.
EMBL; BC023498; AAH23498.1; -; mRNA.
EMBL; AB052762; BAC53795.1; -; mRNA.
CCDS; CCDS27578.1; -. [Q78IQ7-1]
RefSeq; NP_082340.1; NM_028064.2. [Q78IQ7-1]
UniGene; Mm.276829; -.
SMR; Q78IQ7; -.
STRING; 10090.ENSMUSP00000073134; -.
iPTMnet; Q78IQ7; -.
PhosphoSitePlus; Q78IQ7; -.
SwissPalm; Q78IQ7; -.
PaxDb; Q78IQ7; -.
PRIDE; Q78IQ7; -.
Ensembl; ENSMUST00000073428; ENSMUSP00000073134; ENSMUSG00000063354. [Q78IQ7-1]
GeneID; 72027; -.
KEGG; mmu:72027; -.
UCSC; uc007wlb.1; mouse. [Q78IQ7-1]
CTD; 55630; -.
MGI; MGI:1919277; Slc39a4.
eggNOG; KOG2693; Eukaryota.
eggNOG; COG0428; LUCA.
GeneTree; ENSGT00760000119115; -.
HOVERGEN; HBG062532; -.
InParanoid; Q78IQ7; -.
KO; K14710; -.
OMA; DFVFRQH; -.
OrthoDB; EOG091G04FT; -.
PhylomeDB; Q78IQ7; -.
TreeFam; TF318470; -.
Reactome; R-MMU-442380; Zinc influx into cells by the SLC39 gene family.
PRO; PR:Q78IQ7; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000063354; -.
Genevisible; Q78IQ7; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:MGI.
GO; GO:0034224; P:cellular response to zinc ion starvation; IDA:MGI.
GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0071578; P:zinc II ion transmembrane import; IBA:GO_Central.
GO; GO:0006829; P:zinc II ion transport; IDA:MGI.
InterPro; IPR003689; ZIP.
Pfam; PF02535; Zip; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Endosome;
Glycoprotein; Ion transport; Membrane; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 660 Zinc transporter ZIP4.
/FTId=PRO_0000042621.
TOPO_DOM 23 337 Extracellular. {ECO:0000255}.
TRANSMEM 338 358 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 359 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 398 420 Extracellular. {ECO:0000255}.
TRANSMEM 421 441 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 442 571 Cytoplasmic. {ECO:0000255}.
TRANSMEM 572 592 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 593 599 Extracellular. {ECO:0000255}.
TRANSMEM 600 620 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 621 630 Cytoplasmic. {ECO:0000255}.
TRANSMEM 631 651 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 652 660 Extracellular. {ECO:0000255}.
COMPBIAS 223 269 His-rich.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 47 Missing (in isoform 2).
{ECO:0000303|PubMed:12801924}.
/FTId=VSP_015913.
VAR_SEQ 48 63 NTLVARVHCTDGPCEK -> MPGRLSLAQILSVCPQ (in
isoform 2).
{ECO:0000303|PubMed:12801924}.
/FTId=VSP_015914.
CONFLICT 431 435 FFLFE -> RPRVR (in Ref. 4).
{ECO:0000305}.
SEQUENCE 660 AA; 71063 MW; CA7236080C81B7BE CRC64;
MLPKSVTQGL VLALLVGTVA VARPRNLLSL LALGQGALDR LELDGLLNTL VARVHCTDGP
CEKCLSVENV LALGKPDKPQ PAPESVLESR HIIYLSAAAA LYLNNPEKTC KDIQAGLLAS
HVDDYLATLE SPEAMTLGLS QLLQKIEAHA ASQPTGEKTC VDLPQLLEEA EAAGVSKSAG
LVLTALLDHV INGSCFQGLP SPQYFVDFVF RLHSSDPPNI TLHELENLMH HLGVGGEDHS
DHDDHGDHAD HSHPDRKASH QDSELHTPHN SNSSVWDTLC LSAKDIMAVY GLSEEAGVSP
QAWAQLTPAL VQQQLSGACS PYPTIRIQDQ LSQTERYLYG SLATLLICLC AVFGLLLLTC
AKCSTATHYI MQTFLSLAVG ALTGDALLHL IPKVLGLHTH GGEGHTHEEE VGVGGQATWR
LLAVLGGFYI FFLFESFFNL LLPRDQDSEK DGPCSHGGHS HGISLQLAPS NLRQSKQTHE
SSRSDLVAEE TPELLNPETR RLRAELRLLP YLITLGDAVH NFADGLAVGA AFSSSWKTGL
ATSLAVFCHE LPHELGDFAA LLHAGLSVKR ALLLNLASAL TAFAGLYVAL AVGVGEEGEA
WILAVATGLF LYVALCDMLP AMMNVRDQRP WLLFLLHNVG LLGGWTVLLL LSLYEDNITF


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