ID   S10A1_RAT               Reviewed;          94 AA.
AC   P35467;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Protein S100-A1;
DE   AltName: Full=S-100 protein alpha chain;
DE   AltName: Full=S-100 protein subunit alpha;
DE   AltName: Full=S100 calcium-binding protein A1;
GN   Name=S100a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RA   Song W.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-94, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=1742602; DOI=10.1016/0361-9230(91)90061-n;
RA   Zimmer D.B., Song W., Zimmer W.E.;
RT   "Isolation of a rat S100 alpha cDNA and distribution of its mRNA in rat
RT   tissues.";
RL   Brain Res. Bull. 27:157-162(1991).
RN   [3]
RP   INTERACTION WITH AGER.
RX   PubMed=19910580; DOI=10.1161/circresaha.109.195834;
RA   Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J.,
RA   Parker T.G.;
RT   "S100B interaction with the receptor for advanced glycation end products
RT   (RAGE): a novel receptor-mediated mechanism for myocyte apoptosis
RT   postinfarction.";
RL   Circ. Res. 106:93-101(2010).
RN   [4]
RP   STRUCTURE BY NMR OF 2-94.
RX   PubMed=11790100; DOI=10.1021/bi0118308;
RA   Rustandi R.R., Baldisseri D.M., Inman K.G., Nizner P., Hamilton S.M.,
RA   Landar A., Landar A., Zimmer D.B., Weber D.J.;
RT   "Three-dimensional solution structure of the calcium-signaling protein apo-
RT   S100A1 as determined by NMR.";
RL   Biochemistry 41:788-796(2002).
RN   [5]
RP   STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM, AND FUNCTION.
RX   PubMed=16169012; DOI=10.1016/j.jmb.2005.08.027;
RA   Wright N.T., Varney K.M., Ellis K.C., Markowitz J., Gitti R.K.,
RA   Zimmer D.B., Weber D.J.;
RT   "The three-dimensional solution structure of Ca(2+)-bound S100A1 as
RT   determined by NMR spectroscopy.";
RL   J. Mol. Biol. 353:410-426(2005).
RN   [6]
RP   STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM AND RYR1, FUNCTION, AND
RP   INTERACTION WITH RYR1 AND RYR2.
RX   PubMed=18650434; DOI=10.1074/jbc.m804432200;
RA   Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
RA   Weber D.J.;
RT   "S100A1 and calmodulin compete for the same binding site on ryanodine
RT   receptor.";
RL   J. Biol. Chem. 283:26676-26683(2008).
RN   [7]
RP   STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM AND CAPZA1.
RX   PubMed=19452629; DOI=10.1016/j.jmb.2009.01.022;
RA   Wright N.T., Cannon B.R., Wilder P.T., Morgan M.T., Varney K.M.,
RA   Zimmer D.B., Weber D.J.;
RT   "Solution structure of S100A1 bound to the CapZ peptide (TRTK12).";
RL   J. Mol. Biol. 386:1265-1277(2009).
CC   -!- FUNCTION: Small calcium binding protein that plays important roles in
CC       several biological processes such as Ca(2+) homeostasis, chondrocyte
CC       biology and cardiomyocyte regulation. In response to an increase in
CC       intracellular Ca(2+) levels, binds calcium which triggers
CC       conformational changes. These changes allow interactions with specific
CC       target proteins and modulate their activity. Regulates a network in
CC       cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and
CC       mitochondrial function through interaction with the ryanodine receptors
CC       RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and
CC       mitochondrial F1-ATPase (PubMed:18650434). Facilitates diastolic Ca(2+)
CC       dissociation and myofilament mechanics in order to improve relaxation
CC       during diastole (By similarity) (PubMed:18650434).
CC       {ECO:0000250|UniProtKB:P23297, ECO:0000269|PubMed:18650434}.
CC   -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC       alpha and one beta chain. Also forms heterodimers with S100P (By
CC       similarity). Interacts with AGER (PubMed:19910580). Interacts with
CC       CAPZA1 (PubMed:19452629). Interacts with FKBP4. Interacts with RYR1 and
CC       RYR2 (PubMed:18650434). Interacts with CACYBP in a calcium-dependent
CC       manner. Interacts with PPP5C (via TPR repeats); the interaction is
CC       calcium-dependent and modulates PPP5C activity. Interacts with ATP2A2
CC       and PLN in a Ca(2+)-dependent manner (By similarity). Interacts with
CC       mitochondrial F1-ATPase subunits ATP5F1A and ATP5F1B; these
CC       interactions increase F1-ATPase activity (By similarity).
CC       {ECO:0000250|UniProtKB:P23297, ECO:0000250|UniProtKB:P56565,
CC       ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629,
CC       ECO:0000269|PubMed:19910580}.
CC   -!- INTERACTION:
CC       P35467; Q02790: FKBP4; Xeno; NbExp=7; IntAct=EBI-6477109, EBI-1047444;
CC       P35467; P07900: HSP90AA1; Xeno; NbExp=4; IntAct=EBI-6477109, EBI-296047;
CC       P35467; P08107: HSPA1B; Xeno; NbExp=4; IntAct=EBI-6477109, EBI-629985;
CC       P35467; P26882: PPID; Xeno; NbExp=7; IntAct=EBI-6477109, EBI-6477155;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}.
CC       Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P23297}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P56565}.
CC   -!- TISSUE SPECIFICITY: Although predominant among the water-soluble brain
CC       proteins, S100 is also found in a variety of other tissues.
CC       {ECO:0000269|PubMed:1742602}.
CC   -!- PTM: Glutathionylated; glutathionylation increases affinity to calcium
CC       about 10-fold. {ECO:0000250|UniProtKB:P23297}.
CC   -!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are
CC       different from the calcium binding sites. The physiological relevance
CC       of zinc binding is unclear. Physiological concentrations of potassium
CC       antagonize the binding of both divalent cations, especially affecting
CC       the high-affinity calcium-binding sites.
CC       {ECO:0000250|UniProtKB:P02639}.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; U26358; AAB53657.1; -; Genomic_DNA.
DR   EMBL; U26357; AAB53657.1; JOINED; Genomic_DNA.
DR   EMBL; S68809; AAB20539.2; -; mRNA.
DR   RefSeq; NP_001007637.1; NM_001007636.3.
DR   PDB; 1K2H; NMR; -; A/B=2-94.
DR   PDB; 1ZFS; NMR; -; A/B=2-94.
DR   PDB; 2K2F; NMR; -; A/B=2-94.
DR   PDB; 2KBM; NMR; -; A/B=2-94.
DR   PDBsum; 1K2H; -.
DR   PDBsum; 1ZFS; -.
DR   PDBsum; 2K2F; -.
DR   PDBsum; 2KBM; -.
DR   AlphaFoldDB; P35467; -.
DR   BMRB; P35467; -.
DR   SMR; P35467; -.
DR   BioGRID; 254914; 2.
DR   IntAct; P35467; 4.
DR   MINT; P35467; -.
DR   STRING; 10116.ENSRNOP00000017000; -.
DR   PhosphoSitePlus; P35467; -.
DR   jPOST; P35467; -.
DR   PaxDb; 10116-ENSRNOP00000017000; -.
DR   GeneID; 295214; -.
DR   KEGG; rno:295214; -.
DR   UCSC; RGD:3614; rat.
DR   AGR; RGD:3614; -.
DR   CTD; 6271; -.
DR   RGD; 3614; S100a1.
DR   VEuPathDB; HostDB:ENSRNOG00000012410; -.
DR   eggNOG; ENOG502SSF0; Eukaryota.
DR   HOGENOM; CLU_138624_2_0_1; -.
DR   InParanoid; P35467; -.
DR   OrthoDB; 4234580at2759; -.
DR   PhylomeDB; P35467; -.
DR   TreeFam; TF332727; -.
DR   EvolutionaryTrace; P35467; -.
DR   PRO; PR:P35467; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000012410; Expressed in heart and 20 other cell types or tissues.
DR   GO; GO:0031672; C:A band; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031674; C:I band; IDA:RGD.
DR   GO; GO:0031430; C:M band; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR   GO; GO:0030018; C:Z disc; IDA:RGD.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0044548; F:S100 protein binding; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR   CDD; cd05025; S-100A1; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR028486; S100-A1.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF134; PROTEIN S100-A1-RELATED; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; P35467; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cytoplasm; Metal-binding; Mitochondrion;
KW   Reference proteome; Repeat; S-nitrosylation; Sarcoplasmic reticulum.
FT   CHAIN           1..94
FT                   /note="Protein S100-A1"
FT                   /id="PRO_0000143963"
FT   DOMAIN          13..48
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          50..85
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000269|PubMed:16169012,
FT                   ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629"
FT   BINDING         33
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000269|PubMed:16169012,
FT                   ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:19452629"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434,
FT                   ECO:0000269|PubMed:19452629"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434,
FT                   ECO:0000269|PubMed:19452629"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434,
FT                   ECO:0000269|PubMed:19452629"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434,
FT                   ECO:0000269|PubMed:19452629"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:16169012, ECO:0000269|PubMed:18650434,
FT                   ECO:0000269|PubMed:19452629"
FT   MOD_RES         86
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P23297"
FT   CONFLICT        14
FT                   /note="N -> H (in Ref. 2; AAB20539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="K -> R (in Ref. 2; AAB20539)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..20
FT                   /evidence="ECO:0007829|PDB:1K2H"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:2K2F"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1ZFS"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:1K2H"
FT   HELIX           43..47
FT                   /evidence="ECO:0007829|PDB:1K2H"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2KBM"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:1K2H"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1ZFS"
FT   HELIX           72..85
FT                   /evidence="ECO:0007829|PDB:1K2H"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:2K2F"
SQ   SEQUENCE   94 AA;  10560 MW;  7B9C0A6C1C4FCCE0 CRC64;
     MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSSFLDVQK DADAVDKIMK
     ELDENGDGEV DFQEFVVLVA ALTVACNNFF WENS
//