S39AA_MOUSE
ID S39AA_MOUSE Reviewed; 833 AA.
AC Q6P5F6; Q80TG2; Q8BX42; Q8C0L2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 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=Brain, and Egg;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-833.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-833.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
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 [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-198 AND ASN-218.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198; ASN-218 AND ASN-341.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC33542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC052880; AAH52880.1; -; mRNA.
DR EMBL; BC059214; AAH59214.1; ALT_INIT; mRNA.
DR EMBL; BC062918; AAH62918.1; -; mRNA.
DR EMBL; AK122483; BAC65765.1; -; mRNA.
DR EMBL; AK030685; BAC27077.1; -; mRNA.
DR EMBL; AK049099; BAC33542.1; ALT_INIT; mRNA.
DR CCDS; CCDS14936.1; -.
DR RefSeq; NP_766241.2; NM_172653.2.
DR RefSeq; XP_006495996.1; XM_006495933.3.
DR RefSeq; XP_006495997.1; XM_006495934.3.
DR RefSeq; XP_006495998.1; XM_006495935.2.
DR AlphaFoldDB; Q6P5F6; -.
DR BioGRID; 230584; 2.
DR STRING; 10090.ENSMUSP00000027131; -.
DR GlyConnect; 2830; 8 N-Linked glycans (2 sites).
DR GlyGen; Q6P5F6; 4 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; Q6P5F6; -.
DR PhosphoSitePlus; Q6P5F6; -.
DR EPD; Q6P5F6; -.
DR MaxQB; Q6P5F6; -.
DR PaxDb; Q6P5F6; -.
DR PeptideAtlas; Q6P5F6; -.
DR PRIDE; Q6P5F6; -.
DR ProteomicsDB; 256899; -.
DR Antibodypedia; 34052; 136 antibodies from 28 providers.
DR DNASU; 227059; -.
DR Ensembl; ENSMUST00000027131; ENSMUSP00000027131; ENSMUSG00000025986.
DR GeneID; 227059; -.
DR KEGG; mmu:227059; -.
DR UCSC; uc007axc.1; mouse.
DR CTD; 57181; -.
DR MGI; MGI:1914515; Slc39a10.
DR VEuPathDB; HostDB:ENSMUSG00000025986; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000160335; -.
DR HOGENOM; CLU_015114_13_2_1; -.
DR InParanoid; Q6P5F6; -.
DR OMA; EVNTPGF; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q6P5F6; -.
DR TreeFam; TF318470; -.
DR BioGRID-ORCS; 227059; 18 hits in 80 CRISPR screens.
DR ChiTaRS; Slc39a10; mouse.
DR PRO; PR:Q6P5F6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6P5F6; protein.
DR Bgee; ENSMUSG00000025986; Expressed in brain blood vessel and 242 other tissues.
DR ExpressionAtlas; Q6P5F6; baseline and differential.
DR Genevisible; Q6P5F6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:MGI.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:MGI.
DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; IMP:MGI.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IMP:MGI.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..833
FT /note="Zinc transporter ZIP10"
FT /id="PRO_0000297633"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULF5"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULF5"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULF5"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CONFLICT 346
FT /note="L -> S (in Ref. 2; BAC65765)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="I -> F (in Ref. 3; BAC27077)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="F -> Y (in Ref. 2; BAC65765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 94394 MW; BA51B66A2296AFC2 CRC64;
MKVHIHTKFC LICLLTFIFH HCNHCHEDHD HGPEELHRHH RGMTESESSK FSVQDAENEK
KYYIEKLFDR YGENGRLSFF GLEKLLTNLG LGEIKVVEIN HEDLGHDHVS HLDILAVQEG
KHFHSHTHQH FHNHLNAENH TTTSVTSKRN HKCDPEKEAA ELPIKADDKH LHDRNHRFHH
RHRLHHHLDH NTTRHVHNDS VAHSEHGEPG HSPSPETNKT QEQSEVKSVK VRRKEKGKRK
KENSEVNTPG FLPNHDHSEQ YEHNRVHKLD RVHSPGHPHA HLPEHSGHEL GHGHQELDPD
NEGELRHTRK REAPHVRKSA IYSTPSHKDQ SEDDRQHECL NVTQLLKHFG LGPNSPISPD
LFTYLCPALL YQIDSRLCIE HFDKLLVEDL NKDKTLVPED KTNIGASAWI CGIISITVIS
LLSLLGVILV PIINQGCFKF LLTFLVALAV GTMSGDALLH LLPHSQGGHD HSHQHTHGHG
HSHGHESKEF LEEYDAVLKG LVALGGIYLL FIIEHCIRMF KHYKQQRGKQ KWFMKQSTEE
STIGRKLSDH KLNSTPDADW LQLKPLAGTD DSVVSEDRLN ETELTDLEAQ QESPPKNYLG
VEEEKIMDHS HSDGLHTIHE HEVHVTSHNH HDEDKAVLRK HSHQWHHRHA HHSHGPCHSG
SDLKETGIAN IAWMVIMGDG IHNFSDGLAI GAAFSAGLTG GISTSIAVFC HELPHELGDF
AVLLKAGMTV KQAIVYNLLS AMMAYIGMLI GTAVGQYANN ITLWIFAITA GMFLYVALVD
MLPEMLHGDG DHEEHGFCPV GQFILQNLGL LFGFAIMLVI ALYEDKIVFD IQF
