S10AD_BOVIN
ID S10AD_BOVIN Reviewed; 98 AA.
AC P79342; Q3ZBJ2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein S100-A13;
DE AltName: Full=8 kDa amlexanox-binding protein;
DE AltName: Full=S100 calcium-binding protein A13;
GN Name=S100A13;
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].
RA Oyama Y., Shishibori T., Matsutomo M., Yamashita K., Maeta H.,
RA Kobayashi R.;
RT "Molecular cloning of a new 8KDa protein, isolated with Amlexanox coupled
RT column chromatography.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the export of proteins that lack a signal
CC peptide and are secreted by an alternative pathway. Binds two calcium
CC ions per subunit. Binds one copper ion. Binding of one copper ion does
CC not interfere with calcium binding. Required for the copper-dependent
CC stress-induced export of IL1A and FGF1. The calcium-free protein binds
CC to lipid vesicles containing phosphatidylserine, but not to vesicles
CC containing phosphatidylcholine (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Part of a copper-dependent multiprotein complex
CC containing S100A13, FGF1 and SYT1. Interacts with FGF1 and SYT1 (By
CC similarity). Interacts with IL1A (By similarity).
CC {ECO:0000250|UniProtKB:P97352, ECO:0000250|UniProtKB:Q99584}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}.
CC Note=Secretion is mediated by exposure to stress and requires copper
CC ions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB001567; BAA19411.1; -; mRNA.
DR EMBL; BC103266; AAI03267.1; -; mRNA.
DR RefSeq; NP_991369.1; NM_205800.1.
DR RefSeq; XP_005203680.1; XM_005203623.1.
DR RefSeq; XP_005203681.1; XM_005203624.3.
DR AlphaFoldDB; P79342; -.
DR SMR; P79342; -.
DR STRING; 9913.ENSBTAP00000028499; -.
DR PaxDb; P79342; -.
DR PRIDE; P79342; -.
DR Ensembl; ENSBTAT00000028499; ENSBTAP00000028499; ENSBTAG00000021378.
DR Ensembl; ENSBTAT00000067611; ENSBTAP00000058627; ENSBTAG00000021378.
DR GeneID; 404146; -.
DR KEGG; bta:404146; -.
DR CTD; 6284; -.
DR VEuPathDB; HostDB:ENSBTAG00000021378; -.
DR VGNC; VGNC:34239; S100A13.
DR eggNOG; ENOG502S3RT; Eukaryota.
DR GeneTree; ENSGT00940000161854; -.
DR HOGENOM; CLU_138624_3_0_1; -.
DR InParanoid; P79342; -.
DR OrthoDB; 1506806at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021378; Expressed in pons and 106 other tissues.
DR ExpressionAtlas; P79342; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0050786; F:RAGE receptor binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028487; S100A13.
DR PANTHER; PTHR11639:SF57; PTHR11639:SF57; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 3: Inferred from homology;
KW Calcium; Copper; Cytoplasm; Lipid-binding; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Secreted; Transport.
FT CHAIN 1..98
FT /note="Protein S100-A13"
FT /id="PRO_0000144018"
FT DOMAIN 18..53
FT /note="EF-hand"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97352"
FT CONFLICT 63
FT /note="L -> F (in Ref. 1; BAA19411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 11199 MW; 778584280CBE843B CRC64;
MAAEPLTELE AAIETVVTTF FTFAGREGRK GSLSVNEFKE LVTQQLPHLL KDVGSLDEKM
KSLDVNQDSE LKFSEYWRLI GELAKEIRKE KALEIRKK
