S10AE_MOUSE
ID S10AE_MOUSE Reviewed; 104 AA.
AC Q9D2Q8; Q9D1D8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein S100-A14;
DE AltName: Full=S100 calcium-binding protein A14;
DE Short=S114;
GN Name=S100a14; Synonyms=Gm1020, S100a15;
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=Embryo, and Stomach;
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 MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a role
CC in the regulation of cell survival and apoptosis. Depending on the
CC context, it can promote cell proliferation or apoptosis. Plays a role
CC in the regulation of cell migration by modulating the levels of MMP2, a
CC matrix protease that is under transcriptional control of P53/TP53. Does
CC not bind calcium (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with AGER (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AK003669; BAB22927.1; -; mRNA.
DR EMBL; AK019075; BAB31533.1; -; mRNA.
DR EMBL; BC025607; AAH25607.1; -; mRNA.
DR CCDS; CCDS17535.1; -.
DR RefSeq; NP_001156997.1; NM_001163525.2.
DR RefSeq; NP_001156998.1; NM_001163526.2.
DR RefSeq; NP_079669.2; NM_025393.4.
DR AlphaFoldDB; Q9D2Q8; -.
DR SMR; Q9D2Q8; -.
DR BioGRID; 211264; 1.
DR STRING; 10090.ENSMUSP00000126821; -.
DR iPTMnet; Q9D2Q8; -.
DR PhosphoSitePlus; Q9D2Q8; -.
DR MaxQB; Q9D2Q8; -.
DR PaxDb; Q9D2Q8; -.
DR PeptideAtlas; Q9D2Q8; -.
DR PRIDE; Q9D2Q8; -.
DR ProteomicsDB; 260875; -.
DR TopDownProteomics; Q9D2Q8; -.
DR Antibodypedia; 34129; 143 antibodies from 23 providers.
DR Ensembl; ENSMUST00000167598; ENSMUSP00000126821; ENSMUSG00000042306.
DR Ensembl; ENSMUST00000199538; ENSMUSP00000142428; ENSMUSG00000042306.
DR GeneID; 66166; -.
DR KEGG; mmu:66166; -.
DR UCSC; uc008qcv.2; mouse.
DR CTD; 57402; -.
DR MGI; MGI:1913416; S100a14.
DR VEuPathDB; HostDB:ENSMUSG00000042306; -.
DR eggNOG; ENOG502SB9V; Eukaryota.
DR GeneTree; ENSGT00940000161706; -.
DR InParanoid; Q9D2Q8; -.
DR OMA; EKIECLG; -.
DR OrthoDB; 1506806at2759; -.
DR PhylomeDB; Q9D2Q8; -.
DR BioGRID-ORCS; 66166; 1 hit in 68 CRISPR screens.
DR ChiTaRS; S100a11; mouse.
DR PRO; PR:Q9D2Q8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D2Q8; protein.
DR Bgee; ENSMUSG00000042306; Expressed in esophagus and 95 other tissues.
DR ExpressionAtlas; Q9D2Q8; baseline and differential.
DR Genevisible; Q9D2Q8; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042379; F:chemokine receptor binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; ISO:MGI.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028493; S100A14.
DR PANTHER; PTHR11639:SF4; PTHR11639:SF4; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Reference proteome; Repeat.
FT CHAIN 1..104
FT /note="Protein S100-A14"
FT /id="PRO_0000144022"
FT DOMAIN 27..61
FT /note="EF-hand"
FT CONFLICT 100
FT /note="P -> L (in Ref. 1; BAB22927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 104 AA; 11599 MW; 5CC04EFD2E82AAFC CRC64;
MGQCRSANAE DAQEFSDVER AIETLIKNFH KYSVAGKKET LTPAELRDLV TQQLPHLMPS
NCGLEEKIAN LGNCNDSKLE FGSFWELIGE AAKSVKMERP VTRS
