S10AD_MOUSE
ID S10AD_MOUSE Reviewed; 98 AA.
AC P97352;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein S100-A13;
DE AltName: Full=S100 calcium-binding protein A13;
GN Name=S100a13;
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 [MRNA].
RX PubMed=8878558; DOI=10.1006/bbrc.1996.1551;
RA Wicki R., Schaefer B.W., Erne P., Heizmann C.W.;
RT "Characterization of the human and mouse cDNAs coding for S100A13, a new
RT member of the S100 protein family.";
RL Biochem. Biophys. Res. Commun. 227:594-599(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 SUBCELLULAR LOCATION.
RX PubMed=12135982; DOI=10.1083/jcb.200203084;
RA Prudovsky I., Bagala C., Tarantini F., Mandinova A., Soldi R., Bellum S.,
RA Maciag T.;
RT "The intracellular translocation of the components of the fibroblast growth
RT factor 1 release complex precedes their assembly prior to export.";
RL J. Cell Biol. 158:201-208(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12746488; DOI=10.1242/jcs.00471;
RA Mandinova A., Soldi R., Graziani I., Bagala C., Bellum S., Landriscina M.,
RA Tarantini F., Prudovsky I., Maciag T.;
RT "S100A13 mediates the copper-dependent stress-induced release of IL-1alpha
RT from both human U937 and murine NIH 3T3 cells.";
RL J. Cell Sci. 116:2687-2696(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH LIPID VESICLES.
RX PubMed=17991455; DOI=10.1016/j.bbamem.2007.09.007;
RA Kathir K.M., Ibrahim K., Rajalingam D., Prudovsky I., Yu C., Kumar T.K.;
RT "S100A13-lipid interactions-role in the non-classical release of the acidic
RT fibroblast growth factor.";
RL Biochim. Biophys. Acta 1768:3080-3089(2007).
RN [6]
RP FUNCTION, INTERACTION WITH SYT1 AND FGF1, COPPER BINDING, AND
RP IDENTIFICATION IN A COPPER-DEPENDENT MULTIPROTEIN COMPLEX CONTAINING SYT1;
RP FGF1 AND S100A13.
RX PubMed=11432880; DOI=10.1074/jbc.m102925200;
RA Landriscina M., Bagala C., Mandinova A., Soldi R., Micucci I., Bellum S.,
RA Prudovsky I., Maciag T.;
RT "Copper induces the assembly of a multiprotein aggregate implicated in the
RT release of fibroblast growth factor 1 in response to stress.";
RL J. Biol. Chem. 276:25549-25557(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19233122; DOI=10.1016/j.bbrc.2009.02.061;
RA Graziani I., Doyle A., Sterling S., Kirov A., Tarantini F., Landriscina M.,
RA Kumar T.K., Neivandt D., Prudovsky I.;
RT "Protein folding does not prevent the nonclassical export of FGF1 and
RT S100A13.";
RL Biochem. Biophys. Res. Commun. 381:350-354(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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 [9]
RP STRUCTURE BY NMR, AND SUBUNIT.
RA Vaithiyalingam S., Kumar T.K.S., Yu C.;
RT "Three-dimensional solution structure of S100A13.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the export of proteins that lack a signal
CC peptide and are secreted by an alternative pathway. Binds two calcium
CC ions per subunit. Binds one copper ion. Binding of one copper ion does
CC not interfere with calcium binding. Required for the copper-dependent
CC stress-induced export of IL1A and FGF1. The calcium-free protein binds
CC to lipid vesicles containing phosphatidylserine, but not to vesicles
CC containing phosphatidylcholine. {ECO:0000269|PubMed:11432880,
CC ECO:0000269|PubMed:12746488, ECO:0000269|PubMed:17991455}.
CC -!- SUBUNIT: Homodimer. Part of a copper-dependent multiprotein complex
CC containing S100A13, FGF1 and SYT1. Interacts with FGF1 and SYT1.
CC Interacts with IL1A (By similarity). {ECO:0000250|UniProtKB:Q99584,
CC ECO:0000269|PubMed:11432880, ECO:0000269|PubMed:17991455,
CC ECO:0000269|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is mediated
CC by exposure to stress and requires copper ions.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; X99921; CAA68189.1; -; mRNA.
DR EMBL; BC005687; AAH05687.1; -; mRNA.
DR PIR; JC5065; JC5065.
DR RefSeq; NP_033139.2; NM_009113.4.
DR PDB; 2CXJ; NMR; -; A/B=1-98.
DR PDBsum; 2CXJ; -.
DR AlphaFoldDB; P97352; -.
DR BMRB; P97352; -.
DR SMR; P97352; -.
DR STRING; 10090.ENSMUSP00000047737; -.
DR TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
DR iPTMnet; P97352; -.
DR PhosphoSitePlus; P97352; -.
DR EPD; P97352; -.
DR jPOST; P97352; -.
DR PaxDb; P97352; -.
DR PeptideAtlas; P97352; -.
DR PRIDE; P97352; -.
DR ProteomicsDB; 260964; -.
DR TopDownProteomics; P97352; -.
DR Antibodypedia; 34130; 173 antibodies from 29 providers.
DR DNASU; 20196; -.
DR Ensembl; ENSMUST00000048138; ENSMUSP00000047737; ENSMUSG00000042312.
DR GeneID; 20196; -.
DR KEGG; mmu:20196; -.
DR CTD; 6284; -.
DR MGI; MGI:109581; S100a13.
DR VEuPathDB; HostDB:ENSMUSG00000042312; -.
DR eggNOG; ENOG502S3RT; Eukaryota.
DR GeneTree; ENSGT00940000161854; -.
DR InParanoid; P97352; -.
DR OMA; FKVYAGN; -.
DR PhylomeDB; P97352; -.
DR TreeFam; TF332727; -.
DR ChiTaRS; S100a13; mouse.
DR EvolutionaryTrace; P97352; -.
DR PRO; PR:P97352; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P97352; protein.
DR Bgee; ENSMUSG00000042312; Expressed in gonadal fat pad and 223 other tissues.
DR ExpressionAtlas; P97352; baseline and differential.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028487; S100A13.
DR PANTHER; PTHR11639:SF57; PTHR11639:SF57; 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 3D-structure; Calcium; Copper; Cytoplasm; Lipid-binding; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Secreted;
KW Transport.
FT CHAIN 1..98
FT /note="Protein S100-A13"
FT /id="PRO_0000144020"
FT DOMAIN 18..53
FT /note="EF-hand"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:2CXJ"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:2CXJ"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2CXJ"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2CXJ"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2CXJ"
SQ SEQUENCE 98 AA; 11158 MW; 0A8CE8DA822BD530 CRC64;
MAAETLTELE AAIETVVSTF FTFAGREGRK GSLNINEFKE LATQQLPHLL KDVGSLDEKM
KTLDVNQDSE LRFSEYWRLI GELAKEVRKE KALGIRKK