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Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)

 S10A1_RAT               Reviewed;          94 AA.
P35467;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 163.
RecName: Full=Protein S100-A1;
AltName: Full=S-100 protein alpha chain;
AltName: Full=S-100 protein subunit alpha;
AltName: Full=S100 calcium-binding protein A1;
Name=S100a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley;
Song W.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-94, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=1742602; DOI=10.1016/0361-9230(91)90061-N;
Zimmer D.B., Song W., Zimmer W.E.;
"Isolation of a rat S100 alpha cDNA and distribution of its mRNA in
rat tissues.";
Brain Res. Bull. 27:157-162(1991).
[3]
INTERACTION WITH AGER.
PubMed=19910580; DOI=10.1161/CIRCRESAHA.109.195834;
Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J.,
Parker T.G.;
"S100B interaction with the receptor for advanced glycation end
products (RAGE): a novel receptor-mediated mechanism for myocyte
apoptosis postinfarction.";
Circ. Res. 106:93-101(2010).
[4]
STRUCTURE BY NMR OF 2-94.
PubMed=11790100; DOI=10.1021/bi0118308;
Rustandi R.R., Baldisseri D.M., Inman K.G., Nizner P., Hamilton S.M.,
Landar A., Landar A., Zimmer D.B., Weber D.J.;
"Three-dimensional solution structure of the calcium-signaling protein
apo-S100A1 as determined by NMR.";
Biochemistry 41:788-796(2002).
[5]
STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM, AND FUNCTION.
PubMed=16169012; DOI=10.1016/j.jmb.2005.08.027;
Wright N.T., Varney K.M., Ellis K.C., Markowitz J., Gitti R.K.,
Zimmer D.B., Weber D.J.;
"The three-dimensional solution structure of Ca(2+)-bound S100A1 as
determined by NMR spectroscopy.";
J. Mol. Biol. 353:410-426(2005).
[6]
STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM AND RYR1, FUNCTION,
AND INTERACTION WITH RYR1 AND RYR2.
PubMed=18650434; DOI=10.1074/jbc.M804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
[7]
STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM AND CAPZA1.
PubMed=19452629; DOI=10.1016/j.jmb.2009.01.022;
Wright N.T., Cannon B.R., Wilder P.T., Morgan M.T., Varney K.M.,
Zimmer D.B., Weber D.J.;
"Solution structure of S100A1 bound to the CapZ peptide (TRTK12).";
J. Mol. Biol. 386:1265-1277(2009).
-!- FUNCTION: Probably acts as a Ca(2+) signal transducer (By
similarity). In response to an increase in intracellular Ca(2+)
levels, binds calcium which triggers a conformational change
(PubMed:16169012, PubMed:18650434). This conformational change
allows interaction of S1001A with specific target proteins, such
as TPR-containing proteins, and the modulation of their activity
(By similarity). {ECO:0000250|UniProtKB:P23297,
ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434}.
-!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or
one alpha and one beta chain (By similarity). Also forms
heterodimers with S100P (By similarity). Interacts with AGER
(PubMed:19910580). Interacts with CAPZA1 (PubMed:19452629).
Interacts with FKBP4. Interacts with RYR1 and RYR2
(PubMed:18650434). Interacts with CACYBP in a calcium-dependent
manner (By similarity). Interacts with PPP5C (via TPR repeats);
the interaction is calcium-dependent and modulates PPP5C activity
(By similarity). {ECO:0000250|UniProtKB:P23297,
ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629,
ECO:0000269|PubMed:19910580}.
-!- INTERACTION:
Q02790:FKBP4 (xeno); NbExp=7; IntAct=EBI-6477109, EBI-1047444;
P07900:HSP90AA1 (xeno); NbExp=4; IntAct=EBI-6477109, EBI-296047;
P08107:HSPA1B (xeno); NbExp=4; IntAct=EBI-6477109, EBI-629985;
P26882:PPID (xeno); NbExp=7; IntAct=EBI-6477109, EBI-6477155;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}.
-!- TISSUE SPECIFICITY: Although predominant among the water-soluble
brain proteins, S100 is also found in a variety of other tissues.
{ECO:0000269|PubMed:1742602}.
-!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are
different from the calcium binding sites. The physiological
relevance of zinc binding is unclear. Physiological concentrations
of potassium antagonize the binding of both divalent cations,
especially affecting the high-affinity calcium-binding sites.
{ECO:0000250|UniProtKB:P02639}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U26358; AAB53657.1; -; Genomic_DNA.
EMBL; U26357; AAB53657.1; JOINED; Genomic_DNA.
EMBL; S68809; AAB20539.2; -; mRNA.
RefSeq; NP_001007637.1; NM_001007636.3.
PDB; 1K2H; NMR; -; A/B=2-94.
PDB; 1ZFS; NMR; -; A/B=2-94.
PDB; 2K2F; NMR; -; A/B=2-94.
PDB; 2KBM; NMR; -; A/B=2-94.
PDBsum; 1K2H; -.
PDBsum; 1ZFS; -.
PDBsum; 2K2F; -.
PDBsum; 2KBM; -.
ProteinModelPortal; P35467; -.
SMR; P35467; -.
BioGrid; 254914; 1.
IntAct; P35467; 4.
MINT; P35467; -.
STRING; 10116.ENSRNOP00000017000; -.
PaxDb; P35467; -.
PRIDE; P35467; -.
Ensembl; ENSRNOT00000017000; ENSRNOP00000017000; ENSRNOG00000012410.
GeneID; 295214; -.
KEGG; rno:295214; -.
UCSC; RGD:3614; rat.
CTD; 6271; -.
RGD; 3614; S100a1.
eggNOG; ENOG410IXZ2; Eukaryota.
eggNOG; ENOG4111987; LUCA.
GeneTree; ENSGT00760000119034; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P35467; -.
OMA; TAAMGSE; -.
OrthoDB; EOG091G10JX; -.
PhylomeDB; P35467; -.
TreeFam; TF332727; -.
EvolutionaryTrace; P35467; -.
PRO; PR:P35467; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000012410; -.
Genevisible; P35467; RN.
GO; GO:0031672; C:A band; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; TAS:RGD.
GO; GO:0031674; C:I band; IDA:RGD.
GO; GO:0031430; C:M band; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IDA:RGD.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
CDD; cd05025; S-100A1; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR028486; S100-A1.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
PANTHER; PTHR11639:SF66; PTHR11639:SF66; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm; Metal-binding;
Reference proteome; Repeat; S-nitrosylation.
CHAIN 1 94 Protein S100-A1.
/FTId=PRO_0000143963.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 50 85 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 20 33 1; low affinity.
{ECO:0000269|PubMed:16169012,
ECO:0000269|PubMed:18650434,
ECO:0000269|PubMed:19452629}.
CA_BIND 63 74 2; high affinity.
{ECO:0000269|PubMed:16169012,
ECO:0000269|PubMed:18650434,
ECO:0000269|PubMed:19452629}.
MOD_RES 86 86 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P23297}.
CONFLICT 14 14 N -> H (in Ref. 2; AAB20539).
{ECO:0000305}.
CONFLICT 57 57 K -> R (in Ref. 2; AAB20539).
{ECO:0000305}.
HELIX 4 20 {ECO:0000244|PDB:1K2H}.
STRAND 22 25 {ECO:0000244|PDB:2K2F}.
STRAND 27 30 {ECO:0000244|PDB:1ZFS}.
HELIX 31 41 {ECO:0000244|PDB:1K2H}.
HELIX 43 47 {ECO:0000244|PDB:1K2H}.
HELIX 49 51 {ECO:0000244|PDB:2KBM}.
HELIX 52 64 {ECO:0000244|PDB:1K2H}.
STRAND 68 70 {ECO:0000244|PDB:1ZFS}.
HELIX 72 85 {ECO:0000244|PDB:1K2H}.
HELIX 91 93 {ECO:0000244|PDB:2K2F}.
SEQUENCE 94 AA; 10560 MW; 7B9C0A6C1C4FCCE0 CRC64;
MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSSFLDVQK DADAVDKIMK
ELDENGDGEV DFQEFVVLVA ALTVACNNFF WENS


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