S39A3_HUMAN
ID S39A3_HUMAN Reviewed; 314 AA.
AC Q9BRY0; B3KMJ3; Q8WUG1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc transporter ZIP3;
DE AltName: Full=Solute carrier family 39 member 3;
DE AltName: Full=Zrt- and Irt-like protein 3;
DE Short=ZIP-3;
GN Name=SLC39A3; Synonyms=ZIP3;
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).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Duodenum, and Lymph;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Acts as a zinc-influx transporter. {ECO:0000305}.
CC -!- INTERACTION:
CC Q9BRY0-2; Q9BWQ6: YIPF2; NbExp=3; IntAct=EBI-17714201, EBI-751204;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRY0-2; Sequence=VSP_029920, VSP_029921;
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; AK002044; BAG51005.1; -; mRNA.
DR EMBL; BC005869; AAH05869.2; -; mRNA.
DR EMBL; BC020571; AAH20571.1; -; mRNA.
DR CCDS; CCDS12093.1; -. [Q9BRY0-1]
DR CCDS; CCDS45909.1; -. [Q9BRY0-2]
DR RefSeq; NP_653165.2; NM_144564.4. [Q9BRY0-1]
DR RefSeq; NP_998733.1; NM_213568.1. [Q9BRY0-2]
DR AlphaFoldDB; Q9BRY0; -.
DR SMR; Q9BRY0; -.
DR BioGRID; 119011; 70.
DR IntAct; Q9BRY0; 8.
DR STRING; 9606.ENSP00000269740; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.5.3.3; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; Q9BRY0; -.
DR PhosphoSitePlus; Q9BRY0; -.
DR BioMuta; SLC39A3; -.
DR DMDM; 74732942; -.
DR EPD; Q9BRY0; -.
DR jPOST; Q9BRY0; -.
DR MassIVE; Q9BRY0; -.
DR MaxQB; Q9BRY0; -.
DR PaxDb; Q9BRY0; -.
DR PeptideAtlas; Q9BRY0; -.
DR PRIDE; Q9BRY0; -.
DR ProteomicsDB; 78852; -. [Q9BRY0-1]
DR ProteomicsDB; 78853; -. [Q9BRY0-2]
DR Antibodypedia; 23039; 122 antibodies from 27 providers.
DR DNASU; 29985; -.
DR Ensembl; ENST00000269740.9; ENSP00000269740.3; ENSG00000141873.11. [Q9BRY0-1]
DR Ensembl; ENST00000455372.2; ENSP00000393715.1; ENSG00000141873.11. [Q9BRY0-2]
DR GeneID; 29985; -.
DR KEGG; hsa:29985; -.
DR MANE-Select; ENST00000269740.9; ENSP00000269740.3; NM_144564.5; NP_653165.2.
DR UCSC; uc002lwg.4; human. [Q9BRY0-1]
DR CTD; 29985; -.
DR DisGeNET; 29985; -.
DR GeneCards; SLC39A3; -.
DR HGNC; HGNC:17128; SLC39A3.
DR HPA; ENSG00000141873; Tissue enhanced (testis).
DR MIM; 612168; gene.
DR neXtProt; NX_Q9BRY0; -.
DR OpenTargets; ENSG00000141873; -.
DR PharmGKB; PA38203; -.
DR VEuPathDB; HostDB:ENSG00000141873; -.
DR eggNOG; KOG1558; Eukaryota.
DR GeneTree; ENSGT00940000160231; -.
DR HOGENOM; CLU_040462_4_1_1; -.
DR InParanoid; Q9BRY0; -.
DR OMA; HHHGHFN; -.
DR OrthoDB; 981397at2759; -.
DR PhylomeDB; Q9BRY0; -.
DR TreeFam; TF317098; -.
DR PathwayCommons; Q9BRY0; -.
DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR SignaLink; Q9BRY0; -.
DR BioGRID-ORCS; 29985; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; SLC39A3; human.
DR GeneWiki; SLC39A3; -.
DR GenomeRNAi; 29985; -.
DR Pharos; Q9BRY0; Tbio.
DR PRO; PR:Q9BRY0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BRY0; protein.
DR Bgee; ENSG00000141873; Expressed in left testis and 141 other tissues.
DR ExpressionAtlas; Q9BRY0; baseline and differential.
DR Genevisible; Q9BRY0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..314
FT /note="Zinc transporter ZIP3"
FT /id="PRO_0000312868"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U1X7"
FT VAR_SEQ 71..105
FT /note="LQKVLSLGHISTDYPLAETILLLGFFMTVFLEQLI -> VRAPWALAAALGT
FT LWPRDSDAFSTLMPSSVKALML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029920"
FT VAR_SEQ 106..314
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029921"
FT VARIANT 100
FT /note="F -> L (in dbSNP:rs11539244)"
FT /id="VAR_037599"
FT VARIANT 257
FT /note="P -> L (in dbSNP:rs35594294)"
FT /id="VAR_037600"
SQ SEQUENCE 314 AA; 33601 MW; 572ADE958735D2CE CRC64;
MVKLLVAKIL CMVGVFFFML LGSLLPVKII ETDFEKAHRS KKILSLCNTF GGGVFLATCF
NALLPAVREK LQKVLSLGHI STDYPLAETI LLLGFFMTVF LEQLILTFRK EKPSFIDLET
FNAGSDVGSD SEYESPFMGG ARGHALYVEP HGHGPSLSVQ GLSRASPVRL LSLAFALSAH
SVFEGLALGL QEEGEKVVSL FVGVAVHETL VAVALGISMA RSAMPLRDAA KLAVTVSAMI
PLGIGLGLGI ESAQGVPGSV ASVLLQGLAG GTFLFITFLE ILAKELEEKS DRLLKVLFLV
LGYTVLAGMV FLKW
