S100B_RAT
ID S100B_RAT Reviewed; 92 AA.
AC P04631;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein S100-B;
DE AltName: Full=S-100 protein beta chain;
DE AltName: Full=S-100 protein subunit beta;
DE AltName: Full=S100 calcium-binding protein B;
GN Name=S100b;
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 [MRNA].
RX PubMed=6093041; DOI=10.1093/nar/12.19.7455;
RA Kuwano R., Usui H., Maeda T., Fukui T., Yamanari N., Ohtsuka E.,
RA Ikehara M., Takahashi Y.;
RT "Molecular cloning and the complete nucleotide sequence of cDNA to mRNA for
RT S-100 protein of rat brain.";
RL Nucleic Acids Res. 12:7455-7465(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kuwano R., Usui H., Maeda T., Araki K., Kurihara T., Yamakuni T.,
RA Ohtsuka E., Ikehara M., Takahashi Y.;
RT "Molecular cloning and nucleotide sequences of cDNA and genomic DNA for
RT alpha and beta subunits of S100 protein.";
RL Taniguchi Symp. Brain Sci. 19:243-255(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1653388; DOI=10.1016/0169-328x(91)90061-2;
RA Maeda T., Usui H., Araki K., Kuwano R., Takahashi Y., Suzuki Y.;
RT "Structure and expression of rat S-100 beta subunit gene.";
RL Brain Res. Mol. Brain Res. 10:193-202(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-92.
RX PubMed=3818655; DOI=10.1016/s0021-9258(18)61388-2;
RA Dunn R., Landry C., O'Hanlon D., Dunn J., Allore R., Brown I., Marks A.;
RT "Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells
RT following treatment with anti-microtubular drugs.";
RL J. Biol. Chem. 262:3562-3566(1987).
RN [6]
RP PROTEIN SEQUENCE OF 7-21 AND 35-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH CACYBP.
RX PubMed=12042313; DOI=10.1074/jbc.m203602200;
RA Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.;
RT "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand
RT proteins of the S100 family.";
RL J. Biol. Chem. 277:28848-28852(2002).
RN [8]
RP FUNCTION, INTERACTION WITH AGER, AND INDUCTION.
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 [9]
RP FUNCTION, AND INTERACTION WITH ATAD3A.
RX PubMed=20351179; DOI=10.1128/mcb.01468-09;
RA Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N.,
RA Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J.;
RT "The calcium-dependent interaction between S100B and the mitochondrial AAA
RT ATPase ATAD3A and the role of this complex in the cytoplasmic processing of
RT ATAD3A.";
RL Mol. Cell. Biol. 30:2724-2736(2010).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=8794737; DOI=10.1021/bi9612226;
RA Drohat A.C., Amburgey J.C., Abildgaard F., Starich M.R., Baldisseri D.M.,
RA Weber D.J.;
RT "Solution structure of rat apo-S100B(beta beta) as determined by NMR
RT spectroscopy.";
RL Biochemistry 35:11577-11588(1996).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=9485423; DOI=10.1021/bi972635p;
RA Drohat A.C., Baldisseri D.M., Rustandi R.R., Weber D.J.;
RT "Solution structure of calcium-bound rat S100B(betabeta) as determined by
RT nuclear magnetic resonance spectroscopy.";
RL Biochemistry 37:2729-2740(1998).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=10211826; DOI=10.1110/ps.8.4.800;
RA Drohat A.C., Tjandra N., Baldisseri D.M., Weber D.J.;
RT "The use of dipolar couplings for determining the solution structure of rat
RT apo-S100B.";
RL Protein Sci. 8:800-809(1999).
RN [13]
RP STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
RX PubMed=12470955; DOI=10.1016/s0022-2836(02)01152-x;
RA Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M.,
RA Weber D.J.;
RT "Solution NMR structure of S100B bound to the high-affinity target peptide
RT TRTK-12.";
RL J. Mol. Biol. 324:1003-1014(2002).
CC -!- FUNCTION: Weakly binds calcium but binds zinc very tightly-distinct
CC binding sites with different affinities exist for both ions on each
CC monomer. Physiological concentrations of potassium ion antagonize the
CC binding of both divalent cations, especially affecting high-affinity
CC calcium-binding sites. Binds to and initiates the activation of STK38
CC by releasing autoinhibitory intramolecular interactions within the
CC kinase. Interaction with AGER after myocardial infarction may play a
CC role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.
CC Could assist ATAD3A cytoplasmic processing, preventing aggregation and
CC favoring mitochondrial localization. May mediate calcium-dependent
CC regulation on many physiological processes by interacting with other
CC proteins, such as TPR-containing proteins, and modulating their
CC activity. {ECO:0000269|PubMed:19910580, ECO:0000269|PubMed:20351179}.
CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC alpha and one beta chain. The S100B dimer binds two molecules of STK38.
CC Interacts with CACYBP in a calcium-dependent manner. Interacts with
CC ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A
CC mitochondrial targeting. Interacts with S100A6. The S100B dimer
CC interacts with two molecules of CAPZA1. Interacts with AGER. Interacts
CC with PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with TPPP; this interaction
CC inhibits TPPP dimerization (By similarity).
CC {ECO:0000250|UniProtKB:P04271, ECO:0000269|PubMed:12042313,
CC ECO:0000269|PubMed:12470955, ECO:0000269|PubMed:19910580,
CC ECO:0000269|PubMed:20351179}.
CC -!- INTERACTION:
CC P04631; Q63495: Ager; NbExp=3; IntAct=EBI-2696631, EBI-6479195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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:1653388}.
CC -!- INDUCTION: Up-regulated in periinfarct ventricular myocardium.
CC {ECO:0000269|PubMed:19910580}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; X01090; CAA25567.1; -; mRNA.
DR EMBL; M54919; AAA42096.1; -; mRNA.
DR EMBL; S53527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S53522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC087026; AAH87026.1; -; mRNA.
DR EMBL; M15705; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A60046; A26557.
DR RefSeq; NP_037323.1; NM_013191.1.
DR RefSeq; XP_008771090.1; XM_008772868.1.
DR RefSeq; XP_017457057.1; XM_017601568.1.
DR PDB; 1B4C; NMR; -; A/B=1-92.
DR PDB; 1DT7; NMR; -; A/B=1-92.
DR PDB; 1MWN; NMR; -; A/B=1-92.
DR PDB; 1QLK; NMR; -; A/B=1-92.
DR PDB; 1SYM; NMR; -; A/B=1-92.
DR PDB; 1XYD; NMR; -; A/B=1-92.
DR PDB; 2K7O; NMR; -; A/B=2-92.
DR PDBsum; 1B4C; -.
DR PDBsum; 1DT7; -.
DR PDBsum; 1MWN; -.
DR PDBsum; 1QLK; -.
DR PDBsum; 1SYM; -.
DR PDBsum; 1XYD; -.
DR PDBsum; 2K7O; -.
DR AlphaFoldDB; P04631; -.
DR BMRB; P04631; -.
DR SMR; P04631; -.
DR BioGRID; 247770; 2.
DR IntAct; P04631; 3.
DR STRING; 10116.ENSRNOP00000001743; -.
DR BindingDB; P04631; -.
DR ChEMBL; CHEMBL3763006; -.
DR iPTMnet; P04631; -.
DR PhosphoSitePlus; P04631; -.
DR SwissPalm; P04631; -.
DR PaxDb; P04631; -.
DR PRIDE; P04631; -.
DR ABCD; P04631; 1 sequenced antibody.
DR GeneID; 25742; -.
DR KEGG; rno:25742; -.
DR UCSC; RGD:3615; rat.
DR CTD; 6285; -.
DR RGD; 3615; S100b.
DR VEuPathDB; HostDB:ENSRNOG00000001295; -.
DR eggNOG; ENOG502S4HJ; Eukaryota.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P04631; -.
DR OMA; VTMVTIC; -.
DR OrthoDB; 1574989at2759; -.
DR PhylomeDB; P04631; -.
DR TreeFam; TF332727; -.
DR Reactome; R-RNO-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-RNO-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-RNO-933542; TRAF6 mediated NF-kB activation.
DR EvolutionaryTrace; P04631; -.
DR PRO; PR:P04631; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001295; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P04631; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0050786; F:RAGE receptor binding; IPI:RGD.
DR GO; GO:0044548; F:S100 protein binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0048156; F:tau protein binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0048708; P:astrocyte differentiation; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR CDD; cd05027; S-100B; 1.
DR IDEAL; IID50019; -.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028481; S100-B.
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; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02638"
FT CHAIN 2..92
FT /note="Protein S100-B"
FT /id="PRO_0000143969"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 62
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 BINDING 64
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 BINDING 66
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 BINDING 68
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 BINDING 73
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02638"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1B4C"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1SYM"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1DT7"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1B4C"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1QLK"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1B4C"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:1B4C"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1B4C"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1B4C"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1B4C"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1XYD"
SQ SEQUENCE 92 AA; 10744 MW; 43815AC212BEC7D0 CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE
