S10A1_RAT
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 03-AUG-2022, entry version 184.
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 jPOST; P35467; -.
DR PaxDb; P35467; -.
DR PRIDE; P35467; -.
DR GeneID; 295214; -.
DR KEGG; rno:295214; -.
DR UCSC; RGD:3614; rat.
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 OMA; NEFFVDS; -.
DR OrthoDB; 1495576at2759; -.
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 tissues.
DR Genevisible; P35467; RN.
DR GO; GO:0031672; C:A band; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
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:0043005; C:neuron projection; IDA:RGD.
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:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR CDD; cd05025; S-100A1; 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 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; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
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
