S39A6_RAT
ID S39A6_RAT Reviewed; 741 AA.
AC Q4V887;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Zinc transporter ZIP6;
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 {ECO:0000312|EMBL:AAH97493.1}; Synonyms=Zip6;
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] {ECO:0000312|EMBL:AAH97493.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH97493.1};
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May act as a zinc-influx transporter.
CC {ECO:0000250|UniProtKB:Q13433}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13433};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13433}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13433}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000255}.
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DR EMBL; BC097493; AAH97493.1; -; mRNA.
DR RefSeq; NP_001019916.1; NM_001024745.1.
DR AlphaFoldDB; Q4V887; -.
DR STRING; 10116.ENSRNOP00000034256; -.
DR GlyGen; Q4V887; 6 sites.
DR iPTMnet; Q4V887; -.
DR PhosphoSitePlus; Q4V887; -.
DR jPOST; Q4V887; -.
DR PaxDb; Q4V887; -.
DR PRIDE; Q4V887; -.
DR Ensembl; ENSRNOT00000036306; ENSRNOP00000034256; ENSRNOG00000028703.
DR GeneID; 291733; -.
DR KEGG; rno:291733; -.
DR UCSC; RGD:1304664; rat.
DR CTD; 25800; -.
DR RGD; 1304664; Slc39a6.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000156387; -.
DR InParanoid; Q4V887; -.
DR OMA; YEGDLMS; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q4V887; -.
DR TreeFam; TF318470; -.
DR Reactome; R-RNO-442380; Zinc influx into cells by the SLC39 gene family.
DR PRO; PR:Q4V887; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000028703; Expressed in ovary and 19 other tissues.
DR Genevisible; Q4V887; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:RGD.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; ISO:RGD.
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..741
FT /note="Zinc transporter ZIP6"
FT /id="PRO_0000278127"
FT TOPO_DOM 21..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..672
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..741
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 95..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..475
FT /evidence="ECO:0000255"
FT COMPBIAS 95..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13433"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 741 AA; 83231 MW; 1110AB62B640D500 CRC64;
MATNLSVIMI LTFALWVTNP LHELQSTAAF SQTTEKINSN WESGINVDVA VTMQRHHLQQ
LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHERH SDHERHSDHE RHSHRGHAAA
GKNSRKAFCP DLDSDNSGKN PNTSQGKGSR PAEHVNGRRN GKESASSSEV TSAVYNTVSE
GTHFLETIET PKPGRRTKDI NPSTPPSITE KSRVGRLSRL ARRKGNDSVS EPRKSFMYSR
TSNDNIQECF NATKLLTSHG MSVQALLNAT EFNYLCPAII NQIDARSCLI HTASEKKAEI
PPKTYSLQIA WLGGFIAISI ISFLSLLGVI LVPLMNRVFF KFLLSFLVAL AVGTLSGDAL
LHLLPHSHAS HHHSHSHEEP AMEMKRGPLF SHLSAQNLEE SSYFDSTWKG LTALGGLYFM
FLVEHVLTLI KQFKDKKKKN QKKPENDEDV ESKKQLSKYE SQLSTNEEKV DTGERPESYL
QADSQEPSPF DSQQPTLLEE EEVMIAHAHP QEVYNEYVPR GCKNKCHSHF HDTLGQSDDL
IHHHHDYHHI LHHHHHQNHH PHSHSQRYSR EELKDAGIAT LAWMVIMGDG LHNFSDGLAI
GAAFTEGLSS GLSTSVAVFC HELPHELGDF AVLLKAGMTV KQAVLYNALS AMLAYLGMAT
GIFIGHYAEN VSMWIFALTA GLFMYVALVD MVPEMLHNDA SDHGCSRWGY FFLQNAGILL
GFGIMLLISI FEHKIVFRIN F
