ID A0A2K5XUZ9_MANLE Unreviewed; 90 AA.
AC A0A2K5XUZ9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein S100 {ECO:0000256|RuleBase:RU361184};
DE AltName: Full=S100 calcium-binding protein {ECO:0000256|RuleBase:RU361184};
GN Name=S100A6 {ECO:0000313|Ensembl:ENSMLEP00000007139.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000007139.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000007139.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May function as calcium sensor and modulator, contributing to
CC cellular calcium signaling. May function by interacting with other
CC proteins, such as TPR-containing proteins, and indirectly play a role
CC in many physiological processes such as the reorganization of the actin
CC cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium
CC binding is cooperative. {ECO:0000256|ARBA:ARBA00025385}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC {ECO:0000256|ARBA:ARBA00007323, ECO:0000256|RuleBase:RU361184}.
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DR RefSeq; XP_011823567.1; XM_011968177.1.
DR RefSeq; XP_011823569.1; XM_011968179.1.
DR RefSeq; XP_011823570.1; XM_011968180.1.
DR RefSeq; XP_011823571.1; XM_011968181.1.
DR RefSeq; XP_011823572.1; XM_011968182.1.
DR RefSeq; XP_011823573.1; XM_011968183.1.
DR RefSeq; XP_011823574.1; XM_011968184.1.
DR AlphaFoldDB; A0A2K5XUZ9; -.
DR SMR; A0A2K5XUZ9; -.
DR STRING; 9568.ENSMLEP00000007139; -.
DR Ensembl; ENSMLET00000030428.1; ENSMLEP00000007139.1; ENSMLEG00000027535.1.
DR GeneID; 105530585; -.
DR KEGG; mleu:105530585; -.
DR CTD; 6277; -.
DR GeneTree; ENSGT00940000161896; -.
DR OMA; LVVICHK; -.
DR OrthoDB; 4638795at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
DR GO; GO:0005523; F:tropomyosin binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR CDD; cd05029; S-100A6; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034118; S-100A6.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF80; PROTEIN S100-A6; 1.
DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361184};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361184};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 48..83
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 90 AA; 10180 MW; 860CBB1416ACBCA1 CRC64;
MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL
DRNKDQEVNF QEYVTFLGAL ALIYNEALKG
//
