S39A6_MOUSE
ID S39A6_MOUSE Reviewed; 765 AA.
AC Q8C145; Q7TPP9; Q7TQE0; Q8R518;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc transporter ZIP6;
DE AltName: Full=Endoplasmic reticulum membrane-linked protein;
DE Short=Ermelin;
DE AltName: Full=Solute carrier family 39 member 6;
DE AltName: Full=Zrt- and Irt-like protein 6;
DE Short=ZIP-6;
DE Flags: Precursor;
GN Name=Slc39a6; Synonyms=Zip6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-765, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=11891044; DOI=10.1016/s0378-1119(01)00885-x;
RA Suzuki A., Endo T.;
RT "Ermelin, an endoplasmic reticulum transmembrane protein, contains the
RT novel HELP domain conserved in eukaryotes.";
RL Gene 284:31-40(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68 AND ASN-275.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Found in the endoplasmic reticulum when
CC overexpressed. {ECO:0000269|PubMed:11891044}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and testis. In the
CC brain strongly expressed in the CA1 and CA3 regions, Purkinje cells in
CC cerebellum and dentate gyrus in hippocampus. In testis found in
CC spermatids or mature sperms in the central areas of seminiferous
CC tubules. {ECO:0000269|PubMed:11891044}.
CC -!- INDUCTION: Induced during neuronal differentiation neuroblastoma cells
CC line but down-regulated during myogenic differentiation of skeletal
CC muscle cells line. {ECO:0000269|PubMed:11891044}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54780.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB86300.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028976; BAC26223.1; -; mRNA.
DR EMBL; BC054780; AAH54780.2; ALT_INIT; mRNA.
DR EMBL; BC055012; AAH55012.1; -; mRNA.
DR EMBL; AB071697; BAB86300.1; ALT_SEQ; mRNA.
DR CCDS; CCDS50239.1; -.
DR RefSeq; NP_631882.2; NM_139143.3.
DR AlphaFoldDB; Q8C145; -.
DR BioGRID; 223167; 4.
DR STRING; 10090.ENSMUSP00000064667; -.
DR GlyConnect; 2833; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8C145; 5 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q8C145; -.
DR PhosphoSitePlus; Q8C145; -.
DR SwissPalm; Q8C145; -.
DR EPD; Q8C145; -.
DR jPOST; Q8C145; -.
DR MaxQB; Q8C145; -.
DR PaxDb; Q8C145; -.
DR PeptideAtlas; Q8C145; -.
DR PRIDE; Q8C145; -.
DR ProteomicsDB; 256684; -.
DR Antibodypedia; 5245; 292 antibodies from 35 providers.
DR DNASU; 106957; -.
DR Ensembl; ENSMUST00000070726; ENSMUSP00000064667; ENSMUSG00000024270.
DR GeneID; 106957; -.
DR KEGG; mmu:106957; -.
DR UCSC; uc008egv.1; mouse.
DR CTD; 25800; -.
DR MGI; MGI:2147279; Slc39a6.
DR VEuPathDB; HostDB:ENSMUSG00000024270; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000156387; -.
DR HOGENOM; CLU_015114_13_2_1; -.
DR InParanoid; Q8C145; -.
DR OMA; YEGDLMS; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q8C145; -.
DR TreeFam; TF318470; -.
DR Reactome; R-MMU-442380; Zinc influx into cells by the SLC39 gene family.
DR BioGRID-ORCS; 106957; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Slc39a6; mouse.
DR PRO; PR:Q8C145; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C145; protein.
DR Bgee; ENSMUSG00000024270; Expressed in hair follicle and 245 other tissues.
DR ExpressionAtlas; Q8C145; baseline and differential.
DR Genevisible; Q8C145; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:MGI.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071577; P:zinc ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..765
FT /note="Zinc transporter ZIP6"
FT /id="PRO_0000041651"
FT TOPO_DOM 21..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..734
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..765
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 96..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..495
FT /evidence="ECO:0000255"
FT COMPBIAS 96..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13433"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13433"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 102..107
FT /note="Missing (in Ref. 3; BAB86300)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> V (in Ref. 2; AAH55012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 86380 MW; C8938B9C3371377B CRC64;
MATDLSVIMI LTFALWVTSP LHELQSTAAF SQTTEKINSN WEPGVNVDLA VTMQRHHLQQ
LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHEHH ADHEHHSDHE HHSDHEHHSD
HEHHSDHEHH SDHEHHSHRS HTVAGKNNRK AFCPDLDSDN SGKNPRTSLG KGSRPAEHMN
GRRNIKESAS SSEVTSAVYN AVSEGTRFVE TIETPKPGRR TKDVNPSTPP SITEKSRVGR
LSRLARKKSN ESVSEPRKSF MYSRNTNDNI QECFNTTKLL TSHGMSIQAL LNATEFNYLC
PAIINQIDAR ACLIHTASEK KAEIPPKTYS LQIAWLGGFI AISIISFLSL LGVILVPLMN
RVFFKFLLSF LVALAVGTLS GDALLHLLPH SHASHQHSHS HEEPAMEMKR GPLFSHLSAQ
NIEESSYFDS TWKGLTALGG LYFMFLVEHV LTLIKQFKDK KKKNQKKPEN DEDVESKKQL
SKYDSQLSSN EEKVDPGERP ESYLRADSQE PSPFDSQQPT MLEEEEVMIA HAHPQEVYNE
YVPRGCKNKC HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA
GIATLAWMVI MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE LGDFAVLLKA
GMTVKQAVLY NALSAMLAYL GMATGIFIGH YAENVSMWIF ALTAGLFMYV ALVDMVPEML
HNDASDHGCS RWGYFFLQNA GILLGFGIML LISIFEHKIV FRINF
