S39AA_HUMAN
ID S39AA_HUMAN Reviewed; 831 AA.
AC Q9ULF5; A8K5C6; B4DGU0; Q3MJA4; Q68CR5; Q6DKH6; Q9Y3Z1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc transporter ZIP10;
DE AltName: Full=Solute carrier family 39 member 10;
DE AltName: Full=Zrt- and Irt-like protein 10;
DE Short=ZIP-10;
DE Flags: Precursor;
GN Name=SLC39A10; Synonyms=KIAA1265, ZIP10;
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 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [7]
RP FUNCTION.
RX PubMed=17359283; DOI=10.1111/j.1349-7006.2007.00446.x;
RA Kagara N., Tanaka N., Noguchi S., Hirano T.;
RT "Zinc and its transporter ZIP10 are involved in invasive behavior of breast
RT cancer cells.";
RL Cancer Sci. 98:692-697(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-553, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-536 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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: May act as a zinc-influx transporter.
CC {ECO:0000269|PubMed:17359283}.
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=Q9ULF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULF5-2; Sequence=VSP_055991;
CC -!- MISCELLANEOUS: High levels of expression are correlated with
CC invasiveness in several breast cancer lines.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB43393.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB033091; BAA86579.1; ALT_INIT; mRNA.
DR EMBL; AK291241; BAF83930.1; -; mRNA.
DR EMBL; AK294771; BAG57901.1; -; mRNA.
DR EMBL; AL050294; CAB43393.1; ALT_SEQ; mRNA.
DR EMBL; CR749813; CAH18673.1; -; mRNA.
DR EMBL; AC013274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC064834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70116.1; -; Genomic_DNA.
DR EMBL; BC073909; AAH73909.1; -; mRNA.
DR EMBL; BC101516; AAI01517.1; -; mRNA.
DR EMBL; BC112223; AAI12224.1; -; mRNA.
DR CCDS; CCDS33353.1; -. [Q9ULF5-1]
DR PIR; T08684; T08684.
DR RefSeq; NP_001120729.1; NM_001127257.1. [Q9ULF5-1]
DR RefSeq; NP_065075.1; NM_020342.2. [Q9ULF5-1]
DR RefSeq; XP_005246746.2; XM_005246689.4. [Q9ULF5-1]
DR RefSeq; XP_011509806.1; XM_011511504.2. [Q9ULF5-1]
DR RefSeq; XP_011509807.1; XM_011511505.2. [Q9ULF5-1]
DR RefSeq; XP_011509808.1; XM_011511506.2. [Q9ULF5-1]
DR AlphaFoldDB; Q9ULF5; -.
DR BioGRID; 121430; 184.
DR IntAct; Q9ULF5; 42.
DR MINT; Q9ULF5; -.
DR STRING; 9606.ENSP00000386766; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.5.4.6; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR GlyGen; Q9ULF5; 5 sites.
DR iPTMnet; Q9ULF5; -.
DR PhosphoSitePlus; Q9ULF5; -.
DR SwissPalm; Q9ULF5; -.
DR BioMuta; SLC39A10; -.
DR DMDM; 156630627; -.
DR EPD; Q9ULF5; -.
DR jPOST; Q9ULF5; -.
DR MassIVE; Q9ULF5; -.
DR MaxQB; Q9ULF5; -.
DR PaxDb; Q9ULF5; -.
DR PeptideAtlas; Q9ULF5; -.
DR PRIDE; Q9ULF5; -.
DR ProteomicsDB; 4160; -.
DR ProteomicsDB; 85012; -. [Q9ULF5-1]
DR Antibodypedia; 34052; 136 antibodies from 28 providers.
DR DNASU; 57181; -.
DR Ensembl; ENST00000359634.10; ENSP00000352655.5; ENSG00000196950.14. [Q9ULF5-1]
DR Ensembl; ENST00000409086.7; ENSP00000386766.3; ENSG00000196950.14. [Q9ULF5-1]
DR GeneID; 57181; -.
DR KEGG; hsa:57181; -.
DR MANE-Select; ENST00000359634.10; ENSP00000352655.5; NM_020342.3; NP_065075.1.
DR UCSC; uc002utg.5; human. [Q9ULF5-1]
DR CTD; 57181; -.
DR DisGeNET; 57181; -.
DR GeneCards; SLC39A10; -.
DR HGNC; HGNC:20861; SLC39A10.
DR HPA; ENSG00000196950; Tissue enhanced (thyroid).
DR MIM; 608733; gene.
DR neXtProt; NX_Q9ULF5; -.
DR OpenTargets; ENSG00000196950; -.
DR PharmGKB; PA134944068; -.
DR VEuPathDB; HostDB:ENSG00000196950; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000160335; -.
DR HOGENOM; CLU_015114_13_2_1; -.
DR InParanoid; Q9ULF5; -.
DR OMA; EVNTPGF; -.
DR PhylomeDB; Q9ULF5; -.
DR TreeFam; TF318470; -.
DR PathwayCommons; Q9ULF5; -.
DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR SignaLink; Q9ULF5; -.
DR BioGRID-ORCS; 57181; 253 hits in 1086 CRISPR screens.
DR ChiTaRS; SLC39A10; human.
DR GeneWiki; SLC39A10; -.
DR GenomeRNAi; 57181; -.
DR Pharos; Q9ULF5; Tbio.
DR PRO; PR:Q9ULF5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULF5; protein.
DR Bgee; ENSG00000196950; Expressed in middle temporal gyrus and 178 other tissues.
DR ExpressionAtlas; Q9ULF5; baseline and differential.
DR Genevisible; Q9ULF5; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; IEA:Ensembl.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..831
FT /note="Zinc transporter ZIP10"
FT /id="PRO_0000297632"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 126..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..191
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 536
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 553
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055991"
FT VARIANT 87
FT /note="T -> S (in dbSNP:rs13419724)"
FT /id="VAR_034658"
FT CONFLICT 426
FT /note="I -> T (in Ref. 3; CAB43393/CAH18673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 94132 MW; E196111D12BC20ED CRC64;
MKVHMHTKFC LICLLTFIFH HCNHCHEEHD HGPEALHRQH RGMTELEPSK FSKQAAENEK
KYYIEKLFER YGENGRLSFF GLEKLLTNLG LGERKVVEIN HEDLGHDHVS HLDILAVQEG
KHFHSHNHQH SHNHLNSENQ TVTSVSTKRN HKCDPEKETV EVSVKSDDKH MHDHNHRLRH
HHRLHHHLDH NNTHHFHNDS ITPSERGEPS NEPSTETNKT QEQSDVKLPK GKRKKKGRKS
NENSEVITPG FPPNHDQGEQ YEHNRVHKPD RVHNPGHSHV HLPERNGHDP GRGHQDLDPD
NEGELRHTRK REAPHVKNNA IISLRKDLNE DDHHHECLNV TQLLKYYGHG ANSPISTDLF
TYLCPALLYQ IDSRLCIEHF DKLLVEDINK DKNLVPEDEA NIGASAWICG IISITVISLL
SLLGVILVPI INQGCFKFLL TFLVALAVGT MSGDALLHLL PHSQGGHDHS HQHAHGHGHS
HGHESNKFLE EYDAVLKGLV ALGGIYLLFI IEHCIRMFKH YKQQRGKQKW FMKQNTEEST
IGRKLSDHKL NNTPDSDWLQ LKPLAGTDDS VVSEDRLNET ELTDLEGQQE SPPKNYLCIE
EEKIIDHSHS DGLHTIHEHD LHAAAHNHHG ENKTVLRKHN HQWHHKHSHH SHGPCHSGSD
LKETGIANIA WMVIMGDGIH NFSDGLAIGA AFSAGLTGGI STSIAVFCHE LPHELGDFAV
LLKAGMTVKQ AIVYNLLSAM MAYIGMLIGT AVGQYANNIT LWIFAVTAGM FLYVALVDML
PEMLHGDGDN EEHGFCPVGQ FILQNLGLLF GFAIMLVIAL YEDKIVFDIQ F
