ID   S100B_BOVIN             Reviewed;          92 AA.
AC   P02638; A4IFR6; Q3ZBY1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 202.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Burczynska B.B., Duda T., Venkataraman V., Sharma R.K.;
RT   "Cloning, molecular and biochemical characterization of S100B from bovine
RT   retina.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons, and Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-92.
RX   PubMed=710399; DOI=10.1111/j.1432-1033.1978.tb12539.x;
RA   Isobe T., Okuyama T.;
RT   "The amino-acid sequence of S-100 protein (PAP I-b protein) and its
RT   relation to the calcium-binding proteins.";
RL   Eur. J. Biochem. 89:379-388(1978).
RN   [4]
RP   SEQUENCE REVISION TO 1-5.
RX   PubMed=7250124; DOI=10.1111/j.1432-1033.1981.tb05303.x;
RA   Isobe T., Okuyama T.;
RT   "The amino-acid sequence of the alpha subunit in bovine brain S-100a
RT   protein.";
RL   Eur. J. Biochem. 116:79-86(1981).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-92, AND ACETYLATION AT SER-2.
RX   PubMed=4026304; DOI=10.1016/0003-9861(85)90086-4;
RA   Marshak D.R., Umekawa H., Watterson D.M., Hidaka H.;
RT   "Structural characterization of the calcium binding protein s100 from
RT   adipose tissue.";
RL   Arch. Biochem. Biophys. 240:777-780(1985).
RN   [6]
RP   FUNCTION, AND METAL ION-BINDING PROPERTIES.
RX   PubMed=6615778; DOI=10.1021/bi00283a009;
RA   Baudier J., Gerard D.;
RT   "Ions binding to S100 proteins: structural changes induced by calcium and
RT   zinc on S100a and S100b proteins.";
RL   Biochemistry 22:3360-3369(1983).
RN   [7]
RP   FUNCTION, AND METAL ION-BINDING PROPERTIES.
RX   PubMed=3722149; DOI=10.1016/s0021-9258(19)83895-4;
RA   Baudier J., Glasser N., Gerard D.;
RT   "Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of
RT   bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta)
RT   protein: Zn2+ regulates Ca2+ binding on S100b protein.";
RL   J. Biol. Chem. 261:8192-8203(1986).
RN   [8]
RP   CADMIUM-BINDING STUDIES.
RX   PubMed=2039467; DOI=10.1042/bj2760013;
RA   Donato H. Jr., Mani R.S., Kay C.M.;
RT   "Spectral studies on the cadmium-ion-binding properties of bovine brain S-
RT   100b protein.";
RL   Biochem. J. 276:13-18(1991).
RN   [9]
RP   STRUCTURE BY NMR.
RX   PubMed=8805590; DOI=10.1016/s0969-2126(96)00111-6;
RA   Kilby P.M., van Eldik L.J., Roberts G.C.K.;
RT   "The solution structure of the bovine S100B protein dimer in the calcium-
RT   free state.";
RL   Structure 4:1041-1052(1996).
RN   [10]
RP   STRUCTURE BY NMR, FUNCTION, AND INTERACTION WITH STK38.
RX   PubMed=14661952; DOI=10.1021/bi035089a;
RA   Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.;
RT   "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100
RT   target specificity and activation of the kinase.";
RL   Biochemistry 42:14416-14426(2003).
CC   -!- FUNCTION: Small zinc- and- and calcium-binding protein that is highly
CC       expressed in astrocytes and constitutes one of the most abundant
CC       soluble proteins in brain (PubMed:3722149, PubMed:6615778). Weakly
CC       binds calcium but binds zinc very tightly-distinct binding sites with
CC       different affinities exist for both ions on each monomer
CC       (PubMed:3722149, PubMed:6615778). Physiological concentrations of
CC       potassium ion antagonize the binding of both divalent cations,
CC       especially affecting high-affinity calcium-binding sites
CC       (PubMed:3722149). Acts as a neurotrophic factor that promotes
CC       astrocytosis and axonal proliferation (By similarity). Involved in
CC       innervation of thermogenic adipose tissue by acting as an adipocyte-
CC       derived neurotrophic factor that promotes sympathetic innervation of
CC       adipose tissue (By similarity). Binds to and initiates the activation
CC       of STK38 by releasing autoinhibitory intramolecular interactions within
CC       the kinase (PubMed:14661952). Interaction with AGER after myocardial
CC       infarction may play a role in myocyte apoptosis by activating ERK1/2
CC       and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic
CC       processing, preventing aggregation and favoring mitochondrial
CC       localization (By similarity). May mediate calcium-dependent regulation
CC       on many physiological processes by interacting with other proteins,
CC       such as TPR-containing proteins, and modulating their activity (By
CC       similarity). {ECO:0000250|UniProtKB:P04271,
CC       ECO:0000250|UniProtKB:P04631, ECO:0000250|UniProtKB:P50114,
CC       ECO:0000269|PubMed:14661952, ECO:0000269|PubMed:3722149,
CC       ECO:0000269|PubMed:6615778}.
CC   -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC       alpha and one beta chain (PubMed:14661952). The S100B dimer binds two
CC       molecules of STK38 (PubMed:14661952). Interacts with CACYBP in a
CC       calcium-dependent manner (By similarity). Interacts with ATAD3A; this
CC       interaction probably occurs in the cytosol prior to ATAD3A
CC       mitochondrial targeting (By similarity). Interacts with S100A6 (By
CC       similarity). The S100B dimer interacts with two molecules of CAPZA1 (By
CC       similarity). Interacts with AGER (By similarity). Interacts with PPP5C
CC       (via TPR repeats); the interaction is calcium-dependent and modulates
CC       PPP5C activity (By similarity). Interacts with TPPP; this interaction
CC       inhibits TPPP dimerization (By similarity). Interacts with isoform
CC       CLSTN3beta of CLSTN3; interaction promotes secretion (By similarity).
CC       {ECO:0000250|UniProtKB:P04271, ECO:0000250|UniProtKB:P04631,
CC       ECO:0000250|UniProtKB:P50114, ECO:0000269|PubMed:14661952}.
CC   -!- INTERACTION:
CC       P02638; Q9CXW3: Cacybp; Xeno; NbExp=4; IntAct=EBI-458452, EBI-767146;
CC       P02638; O95259-2: KCNH1; Xeno; NbExp=2; IntAct=EBI-458452, EBI-9836801;
CC       P02638; Q15208: STK38; Xeno; NbExp=3; IntAct=EBI-458452, EBI-458376;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04271}. Nucleus
CC       {ECO:0000250|UniProtKB:P04271}. Secreted
CC       {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is
CC       promoted by interaction with isoform CLSTN3beta of CLSTN3.
CC       {ECO:0000250|UniProtKB:P50114}.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; DQ195377; ABA39829.1; -; mRNA.
DR   EMBL; BC103041; AAI03042.1; -; mRNA.
DR   EMBL; BC134727; AAI34728.1; -; mRNA.
DR   PIR; A91254; BCBOIB.
DR   RefSeq; NP_001029727.1; NM_001034555.3.
DR   PDB; 1CFP; NMR; -; A/B=1-92.
DR   PDB; 1MHO; X-ray; 2.00 A; A=2-89.
DR   PDB; 1PSB; NMR; -; A/B=2-92.
DR   PDB; 3CR2; X-ray; 1.88 A; A=1-92.
DR   PDB; 3CR4; X-ray; 2.15 A; X=1-92.
DR   PDB; 3CR5; X-ray; 1.85 A; X=1-92.
DR   PDB; 3GK1; X-ray; 2.10 A; A=1-92.
DR   PDB; 3GK2; X-ray; 1.98 A; A=1-92.
DR   PDB; 3GK4; X-ray; 1.90 A; X=1-92.
DR   PDB; 3IQO; X-ray; 1.50 A; A/B=1-92.
DR   PDB; 3IQQ; X-ray; 2.01 A; A=1-92.
DR   PDB; 3LK0; X-ray; 2.04 A; A/B/C/D=1-90.
DR   PDB; 3LK1; X-ray; 1.79 A; A=1-90.
DR   PDB; 3LLE; X-ray; 1.85 A; A/B=1-92.
DR   PDB; 3RLZ; X-ray; 2.01 A; A/B=1-92.
DR   PDB; 3RM1; X-ray; 1.24 A; A=1-92.
DR   PDB; 4FQO; X-ray; 1.65 A; A=1-89.
DR   PDB; 4PDZ; X-ray; 1.73 A; A/B=1-92.
DR   PDB; 4PE0; X-ray; 1.08 A; A/X=1-92.
DR   PDB; 4PE1; X-ray; 1.58 A; A/B=1-92.
DR   PDB; 4PE4; X-ray; 2.18 A; A/X=1-92.
DR   PDB; 4PE7; X-ray; 1.65 A; A=1-92.
DR   PDB; 5DKN; X-ray; 1.53 A; A=1-92.
DR   PDB; 5DKQ; X-ray; 1.59 A; A=1-92.
DR   PDB; 5DKR; X-ray; 1.74 A; A/B=1-92.
DR   PDB; 5ER4; X-ray; 1.81 A; X=1-92.
DR   PDB; 5ER5; X-ray; 1.26 A; A=1-92.
DR   PDB; 8FJ8; X-ray; 2.17 A; A=1-90.
DR   AlphaFoldDB; P02638; -.
DR   BMRB; P02638; -.
DR   MDposit; P02638; -.
DR   MDRepo; P02638; -.
DR   SMR; P02638; -.
DR   BioGRID; 182329; 3.
DR   FunCoup; P02638; 324.
DR   IntAct; P02638; 3.
DR   STRING; 9913.ENSBTAP00000063447; -.
DR   iPTMnet; P02638; -.
DR   PaxDb; 9913-ENSBTAP00000063447; -.
DR   PeptideAtlas; P02638; -.
DR   Ensembl; ENSBTAT00000086647.1; ENSBTAP00000063447.1; ENSBTAG00000004777.8.
DR   Ensembl; ENSBTAT00085016378; ENSBTAP00085032325; ENSBTAG00085010762.
DR   Ensembl; ENSBTAT00090014148; ENSBTAP00090006703; ENSBTAG00090007564.
DR   GeneID; 525716; -.
DR   KEGG; bta:525716; -.
DR   CTD; 6285; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004777; -.
DR   VGNC; VGNC:34248; S100B.
DR   eggNOG; ENOG502S4HJ; Eukaryota.
DR   GeneTree; ENSGT00940000161997; -.
DR   HOGENOM; CLU_138624_2_0_1; -.
DR   InParanoid; P02638; -.
DR   OMA; ACCHEFF; -.
DR   OrthoDB; 9903855at2759; -.
DR   Reactome; R-BTA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR   Reactome; R-BTA-879415; Advanced glycosylation endproduct receptor signaling.
DR   Reactome; R-BTA-933542; TRAF6 mediated NF-kB activation.
DR   SABIO-RK; P02638; -.
DR   EvolutionaryTrace; P02638; -.
DR   PRO; PR:P02638; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000004777; Expressed in midbrain and 102 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0019210; F:kinase inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0050786; F:RAGE receptor binding; IBA:GO_Central.
DR   GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR   GO; GO:0048156; F:tau protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR   GO; GO:0048143; P:astrocyte activation; NAS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR   GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR   GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IGI:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0045917; P:positive regulation of complement activation; NAS:UniProtKB.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0006417; P:regulation of translation; NAS:UniProtKB.
DR   GO; GO:0097490; P:sympathetic neuron projection extension; ISS:UniProtKB.
DR   CDD; cd05027; S-100B; 1.
DR   FunFam; 1.10.238.10:FF:000044; Protein S100; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   IDEAL; IID50022; -.
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   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.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Cell adhesion; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Secreted; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4026304,
FT                   ECO:0000269|PubMed:710399"
FT   CHAIN           2..92
FT                   /note="Protein S100-B"
FT                   /id="PRO_0000143965"
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         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   BINDING         22
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   BINDING         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
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   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P04271"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:4026304"
FT   HELIX           3..19
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1PSB"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1CFP"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:4PE0"
FT   HELIX           71..88
FT                   /evidence="ECO:0007829|PDB:4PE0"
SQ   SEQUENCE   92 AA;  10668 MW;  589BF1DAA0AF6DA7 CRC64;
     MSELEKAVVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
     LDSDGDGECD FQEFMAFVAM ITTACHEFFE HE
//