S10AG_BOVIN
ID S10AG_BOVIN Reviewed; 103 AA.
AC Q0VCM0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein S100-A16;
DE AltName: Full=S100 calcium-binding protein A16;
GN Name=S100A16;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-binding protein. Binds one calcium ion per monomer
CC (By similarity). Can promote differentiation of adipocytes (in vitro)
CC (By similarity). Overexpression in preadipocytes increases their
CC proliferation, enhances adipogenesis and reduces insulin-stimulated
CC glucose uptake (By similarity). {ECO:0000250|UniProtKB:Q96FQ6,
CC ECO:0000250|UniProtKB:Q9D708}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with TP53 (By
CC similarity). {ECO:0000250|UniProtKB:Q96FQ6,
CC ECO:0000250|UniProtKB:Q9D708}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96FQ6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96FQ6}. Note=Primarily nucleolar. A high
CC intracellular calcium level induces nucleolar exit and
CC nucleocytoplasmic transport, whereas a low intracellular calcium level
CC leads to nuclear translocation and accumulation within specific region
CC of nucleoli. {ECO:0000250|UniProtKB:Q96FQ6}.
CC -!- DOMAIN: S100A16 proteins, but not other S100 proteins, have only one
CC functional Ca(2+) binding site per monomer. Upon Ca(2+) binding,
CC undergoes conformational changes leading to the exposure of hydrophobic
CC patches which could be implicated in the Ca(2+)-dependent nuclear
CC export. Binds Zn(2+). Ca(2+) and Zn(2+) do not bind to the same site.
CC Does not bind Cu(2+). {ECO:0000250|UniProtKB:Q96FQ6,
CC ECO:0000250|UniProtKB:Q9D708}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; BC120103; AAI20104.1; -; mRNA.
DR RefSeq; NP_001068686.1; NM_001075218.1.
DR RefSeq; XP_005203713.1; XM_005203656.2.
DR RefSeq; XP_005203714.1; XM_005203657.2.
DR RefSeq; XP_005203715.1; XM_005203658.3.
DR AlphaFoldDB; Q0VCM0; -.
DR SMR; Q0VCM0; -.
DR STRING; 9913.ENSBTAP00000018877; -.
DR PaxDb; Q0VCM0; -.
DR PeptideAtlas; Q0VCM0; -.
DR Ensembl; ENSBTAT00000018877; ENSBTAP00000018877; ENSBTAG00000014204.
DR Ensembl; ENSBTAT00000082933; ENSBTAP00000071528; ENSBTAG00000014204.
DR Ensembl; ENSBTAT00000087147; ENSBTAP00000064089; ENSBTAG00000014204.
DR GeneID; 505679; -.
DR KEGG; bta:505679; -.
DR CTD; 140576; -.
DR VEuPathDB; HostDB:ENSBTAG00000014204; -.
DR VGNC; VGNC:34241; S100A16.
DR eggNOG; ENOG502S6F9; Eukaryota.
DR GeneTree; ENSGT00390000000920; -.
DR HOGENOM; CLU_138624_3_1_1; -.
DR InParanoid; Q0VCM0; -.
DR OMA; DCYTDLE; -.
DR OrthoDB; 1555271at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000014204; Expressed in esophagus and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028485; S100-A16.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF76; PTHR11639:SF76; 1.
DR Pfam; PF01023; S_100; 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 3: Inferred from homology;
KW Calcium; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..103
FT /note="Protein S100-A16"
FT /id="PRO_0000273720"
FT DOMAIN 12..47
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q96FQ6"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 103 AA; 11776 MW; C428F7873EDEDAB2 CRC64;
MADSYTELEK AVVVLVENFY KYVSKHSLVK NKISKSSFRK MLQKELNHML TDTGNRKAAD
KLIQNLDANH DGRISFDEYW TLIGGITSPI ANLIRQQEQQ SSS
