S10AG_MOUSE
ID S10AG_MOUSE Reviewed; 124 AA.
AC Q9D708; Q3TVE3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein S100-A16;
DE AltName: Full=Protein S100F {ECO:0000312|EMBL:AAP46153.1};
DE AltName: Full=S100 calcium binding protein A16;
GN Name=S100a16 {ECO:0000312|MGI:MGI:1915110};
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 {ECO:0000312|EMBL:BAB26486.1};
RC TISSUE=Tongue {ECO:0000312|EMBL:BAB26486.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH20031.1};
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 [5]
RP DOMAIN.
RX PubMed=14684152; DOI=10.1016/j.bbrc.2003.11.115;
RA Marenholz I., Heizmann C.W.;
RT "S100A16, a ubiquitously expressed EF-hand protein which is up-regulated in
RT tumors.";
RL Biochem. Biophys. Res. Commun. 313:237-244(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBUNIT,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17030513; DOI=10.1074/jbc.m605798200;
RA Sturchler E., Cox J.A., Durussel I., Weibel M., Heizmann C.W.;
RT "S100A16, a novel calcium-binding protein of the EF-hand superfamily.";
RL J. Biol. Chem. 281:38905-38917(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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).
RN [8]
RP FUNCTION, INTERACTION WITH TP53, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21266506; DOI=10.1210/en.2010-1059;
RA Liu Y., Zhang R., Xin J., Sun Y., Li J., Wei D., Zhao A.Z.;
RT "Identification of S100A16 as a novel adipogenesis promoting factor in 3T3-
RT L1 cells.";
RL Endocrinology 152:903-911(2011).
RN [9]
RP FUNCTION.
RX PubMed=23526364; DOI=10.1007/s11033-012-2413-2;
RA Li D., Zhang R., Zhu W., Xue Y., Zhang Y., Huang Q., Liu M., Liu Y.;
RT "S100A16 inhibits osteogenesis but stimulates adipogenesis.";
RL Mol. Biol. Rep. 40:3465-3473(2013).
CC -!- FUNCTION: Calcium-binding protein. Binds one calcium ion per monomer
CC (PubMed:17030513). Can promote differentiation of adipocytes (in
CC vitro). Overexpression in 3T3-L1 preadipocytes increases their
CC proliferation, enhances adipogenesis and reduces insulin-stimulated
CC glucose uptake (PubMed:21266506, PubMed:23526364).
CC {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506,
CC ECO:0000269|PubMed:23526364}.
CC -!- SUBUNIT: Homodimer (PubMed:17030513). Interacts with TP53
CC (PubMed:21266506). {ECO:0000269|PubMed:17030513,
CC ECO:0000269|PubMed:21266506}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17030513,
CC ECO:0000269|PubMed:21266506}. Cytoplasm {ECO:0000269|PubMed:17030513,
CC ECO:0000269|PubMed:21266506}. Note=Primarily nucleolar. A high
CC intracellular calcium level induces nucleolar exit and
CC nucleocytoplasmic transport, whereas a low intracellular calcium level
CC leads to nuclear translocation and accumulation within specific region
CC of nucleoli (PubMed:17030513).
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:17030513). Widely distributed
CC throughout the adult brain and predominantly expressed within specific
CC astrocyte populations (PubMed:17030513). Expressed at high level in
CC adipose tissues of obese animals (PubMed:21266506).
CC {ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21266506}.
CC -!- DOMAIN: S100A16 proteins, but not other S100 proteins, have only one
CC functional Ca(2+) binding site per monomer (PubMed:14684152,
CC PubMed:17030513). Upon Ca(2+) binding, undergoes conformational changes
CC leading to the exposure of hydrophobic patches which could be
CC implicated in the Ca(2+)-dependent nuclear export. Binds Zn(2+)
CC (PubMed:17030513). Ca(2+) and Zn(2+) do not bind to the same site
CC (PubMed:17030513). Does not bind Cu(2+) (PubMed:17030513).
CC {ECO:0000269|PubMed:17030513, ECO:0000303|PubMed:14684152}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000255}.
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DR EMBL; AY221962; AAP46153.1; -; mRNA.
DR EMBL; AK009762; BAB26486.1; -; mRNA.
DR EMBL; AK160178; BAE35676.1; -; mRNA.
DR EMBL; AK160512; BAE35835.1; -; mRNA.
DR EMBL; AK167006; BAE39183.1; -; mRNA.
DR EMBL; AC160552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466547; EDL15119.1; -; Genomic_DNA.
DR EMBL; CH466547; EDL15120.1; -; Genomic_DNA.
DR EMBL; CH466547; EDL15121.1; -; Genomic_DNA.
DR EMBL; CH466547; EDL15122.1; -; Genomic_DNA.
DR EMBL; BC020031; AAH20031.1; -; mRNA.
DR CCDS; CCDS17536.1; -.
DR RefSeq; NP_080692.1; NM_026416.2.
DR RefSeq; XP_006502011.1; XM_006501948.2.
DR RefSeq; XP_006502012.1; XM_006501949.3.
DR RefSeq; XP_006502013.1; XM_006501950.3.
DR RefSeq; XP_006502014.1; XM_006501951.1.
DR RefSeq; XP_006502015.1; XM_006501952.1.
DR AlphaFoldDB; Q9D708; -.
DR SMR; Q9D708; -.
DR STRING; 10090.ENSMUSP00000096510; -.
DR iPTMnet; Q9D708; -.
DR PhosphoSitePlus; Q9D708; -.
DR jPOST; Q9D708; -.
DR MaxQB; Q9D708; -.
DR PaxDb; Q9D708; -.
DR PRIDE; Q9D708; -.
DR ProteomicsDB; 260876; -.
DR Antibodypedia; 47029; 197 antibodies from 29 providers.
DR DNASU; 67860; -.
DR Ensembl; ENSMUST00000098910; ENSMUSP00000096509; ENSMUSG00000074457.
DR Ensembl; ENSMUST00000098911; ENSMUSP00000096510; ENSMUSG00000074457.
DR Ensembl; ENSMUST00000107331; ENSMUSP00000102954; ENSMUSG00000074457.
DR Ensembl; ENSMUST00000107333; ENSMUSP00000102956; ENSMUSG00000074457.
DR Ensembl; ENSMUST00000107334; ENSMUSP00000102957; ENSMUSG00000074457.
DR Ensembl; ENSMUST00000107335; ENSMUSP00000102958; ENSMUSG00000074457.
DR GeneID; 67860; -.
DR KEGG; mmu:67860; -.
DR UCSC; uc008qcw.1; mouse.
DR CTD; 140576; -.
DR MGI; MGI:1915110; S100a16.
DR VEuPathDB; HostDB:ENSMUSG00000074457; -.
DR eggNOG; ENOG502S6F9; Eukaryota.
DR GeneTree; ENSGT00390000000920; -.
DR InParanoid; Q9D708; -.
DR OMA; DCYTDLE; -.
DR OrthoDB; 1555271at2759; -.
DR PhylomeDB; Q9D708; -.
DR TreeFam; TF332727; -.
DR BioGRID-ORCS; 67860; 0 hits in 71 CRISPR screens.
DR ChiTaRS; S100a16; mouse.
DR PRO; PR:Q9D708; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D708; protein.
DR Bgee; ENSMUSG00000074457; Expressed in esophagus and 247 other tissues.
DR ExpressionAtlas; Q9D708; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IDA:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028485; S100-A16.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF76; PTHR11639:SF76; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..124
FT /note="Protein S100-A16"
FT /id="PRO_0000441802"
FT DOMAIN 23..37
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305|PubMed:14684152"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 97..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT CONFLICT 39
FT /note="R -> Q (in Ref. 1; BAE35676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 14324 MW; 644E9AC026C5AE7D CRC64;
MADCYTELEK AVVVLVENFY KYVSKHSLVK NKISKSSFRK MLQRELNHML TDTGNRKAAD
KLIQNLDANH DGRICFDEYW TMIGGITSPM ANLIRQQECQ QESQQECQQE SQQESQQESQ
QGSS
