S10A6_MOUSE
ID S10A6_MOUSE Reviewed; 89 AA.
AC P14069;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=5B10;
DE AltName: Full=Calcyclin;
DE AltName: Full=Prolactin receptor-associated protein;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100a6; Synonyms=Cacy;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RX PubMed=8449996; DOI=10.1242/jcs.104.1.187;
RA Timmons P.M., Chan C.T.J., Rigby P.W.J., Poirier F.;
RT "The gene encoding the calcium binding protein calcyclin is expressed at
RT sites of exocytosis in the mouse.";
RL J. Cell Sci. 104:187-196(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2177633;
RA Guo X., Chambers A.F., Parfett C.L., Waterhouse P., Murphy L.C., Reid R.E.,
RA Craig A.M., Edwards D.R., Denhardt D.T.;
RT "Identification of a serum-inducible messenger RNA (5B10) as the mouse
RT homologue of calcyclin: tissue distribution and expression in metastatic,
RT ras-transformed NIH 3T3 cells.";
RL Cell Growth Differ. 1:333-338(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TUC CF1;
RX PubMed=2002257; DOI=10.1111/1523-1747.ep12466230;
RA Wood L., Carter D., Mills M., Hatzenbuhler N., Vogeli G.;
RT "Expression of calcyclin, a calcium-binding protein, in the keratogenous
RT region of growing hair follicles.";
RL J. Invest. Dermatol. 96:383-387(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Mammary tumor;
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 PROTEIN SEQUENCE OF 56-69.
RX PubMed=2597136; DOI=10.1042/bj2630951;
RA Kuznicki J., Filipek A., Hunziker P.E., Huber S., Heizmann C.W.;
RT "Calcium-binding protein from mouse Ehrlich ascites-tumour cells is
RT homologous to human calcyclin.";
RL Biochem. J. 263:951-956(1989).
RN [6]
RP PROTEIN SEQUENCE OF 6-89, AND INTERACTION WITH OTHER PROTEINS.
RX PubMed=1999197; DOI=10.1111/j.1432-1033.1991.tb15768.x;
RA Filipek A., Gerke V., Weber K., Kuznicki J.;
RT "Characterization of the cell-cycle-regulated protein calcyclin from
RT Ehrlich ascites tumor cells. Identification of two binding proteins
RT obtained by Ca2(+)-dependent affinity chromatography.";
RL Eur. J. Biochem. 195:795-800(1991).
RN [7]
RP PROTEIN SEQUENCE OF 24-33 AND 37-89.
RX PubMed=1874170; DOI=10.1210/endo-129-3-1257;
RA Thordarson G., Southard J.N., Talamantes F.;
RT "Purification and characterization of mouse decidual calcyclin: a novel
RT stimulator of mouse placental lactogen-II secretion.";
RL Endocrinology 129:1257-1265(1991).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-47, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts with
CC CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11
CC (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher
CC affinity for TP53 that is phosphorylated on its N-terminal domain, and
CC lower affinity for TP53 that is phosphorylated on its C-terminal
CC domain. Interacts with tropomyosin. Interacts with FKBP4. 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). {ECO:0000250}.
CC -!- INTERACTION:
CC P14069; Q9CXW3: Cacybp; NbExp=4; IntAct=EBI-6478740, EBI-767146;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; M37761; AAA37358.1; -; mRNA.
DR EMBL; X66449; CAA47065.1; -; mRNA.
DR EMBL; X52278; CAA36521.1; -; mRNA.
DR EMBL; BC003832; AAH03832.1; -; mRNA.
DR EMBL; BC010774; AAH10774.1; -; mRNA.
DR CCDS; CCDS38506.1; -.
DR PIR; A54314; A54314.
DR RefSeq; NP_035443.1; NM_011313.2.
DR PDB; 4P2Y; X-ray; 2.30 A; B=1-89.
DR PDBsum; 4P2Y; -.
DR AlphaFoldDB; P14069; -.
DR SMR; P14069; -.
DR BioGRID; 203055; 12.
DR IntAct; P14069; 4.
DR MINT; P14069; -.
DR STRING; 10090.ENSMUSP00000001051; -.
DR iPTMnet; P14069; -.
DR PhosphoSitePlus; P14069; -.
DR SwissPalm; P14069; -.
DR DOSAC-COBS-2DPAGE; P14069; -.
DR EPD; P14069; -.
DR jPOST; P14069; -.
DR PaxDb; P14069; -.
DR PeptideAtlas; P14069; -.
DR PRIDE; P14069; -.
DR ProteomicsDB; 255434; -.
DR Antibodypedia; 1680; 536 antibodies from 40 providers.
DR DNASU; 20200; -.
DR Ensembl; ENSMUST00000001051; ENSMUSP00000001051; ENSMUSG00000001025.
DR Ensembl; ENSMUST00000198128; ENSMUSP00000143111; ENSMUSG00000001025.
DR Ensembl; ENSMUST00000200289; ENSMUSP00000143720; ENSMUSG00000001025.
DR GeneID; 20200; -.
DR KEGG; mmu:20200; -.
DR UCSC; uc008qdb.1; mouse.
DR CTD; 6277; -.
DR MGI; MGI:1339467; S100a6.
DR VEuPathDB; HostDB:ENSMUSG00000001025; -.
DR eggNOG; ENOG502S6IN; Eukaryota.
DR GeneTree; ENSGT00940000161896; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P14069; -.
DR OMA; MVYNEAL; -.
DR OrthoDB; 1581517at2759; -.
DR PhylomeDB; P14069; -.
DR TreeFam; TF332727; -.
DR BioGRID-ORCS; 20200; 1 hit in 73 CRISPR screens.
DR ChiTaRS; S100a6; mouse.
DR PRO; PR:P14069; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P14069; protein.
DR Bgee; ENSMUSG00000001025; Expressed in substantia propria of cornea and 256 other tissues.
DR ExpressionAtlas; P14069; baseline and differential.
DR Genevisible; P14069; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0015075; F:ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0005523; F:tropomyosin binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR CDD; cd05029; S-100A6; 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 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; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..89
FT /note="Protein S100-A6"
FT /id="PRO_0000143985"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 48..83
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06703"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06703"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 47
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 51
FT /note="A -> R (in Ref. 2; CAA36521)"
FT /evidence="ECO:0000305"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4P2Y"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4P2Y"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4P2Y"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4P2Y"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:4P2Y"
SQ SEQUENCE 89 AA; 10051 MW; 2AA1A4018B8CA687 CRC64;
MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMDDL
DRNKDQEVNF QEYVAFLGAL ALIYNEALK
