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Protein S100-A3 (Protein S-100E) (S100 calcium-binding protein A3)

 S10A3_HUMAN             Reviewed;         101 AA.
P33764; D3DV51; Q6FGE4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
18-JUL-2018, entry version 168.
RecName: Full=Protein S100-A3;
AltName: Full=Protein S-100E;
AltName: Full=S100 calcium-binding protein A3;
Name=S100A3; Synonyms=S100E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8341667; DOI=10.1073/pnas.90.14.6547;
Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.;
"Six S100 genes are clustered on human chromosome 1q21: identification
of two genes coding for the two previously unreported calcium-binding
proteins S100D and S100E.";
Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION.
PubMed=9920417; DOI=10.1016/S0167-4889(98)00138-4;
Fritz G., Heizmann C.W., Kroneck P.M.H.;
"Probing the structure of the human Ca2+- and Zn2+-binding protein
S100A3: spectroscopic investigations of its transition metal ion
complexes, and three-dimensional structural model.";
Biochim. Biophys. Acta 1448:264-276(1998).
[8]
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND TISSUE
SPECIFICITY.
PubMed=12470658; DOI=10.1016/S0006-291X(02)02744-4;
Kizawa K., Troxler H., Kleinert P., Inoue T., Toyoda M., Morohashi M.,
Heizmann C.W.;
"Characterization of the cysteine-rich calcium-binding S100A3 protein
from human hair cuticles.";
Biochem. Biophys. Res. Commun. 299:857-862(2002).
[9]
FUNCTION, SUBUNIT, CITRULLINATION AT ARG-51, AND SUBCELLULAR LOCATION.
PubMed=18083705; DOI=10.1074/jbc.M709357200;
Kizawa K., Takahara H., Troxler H., Kleinert P., Mochida U.,
Heizmann C.W.;
"Specific citrullination causes assembly of a globular S100A3
homotetramer: a putative Ca2+ modulator matures human hair cuticle.";
J. Biol. Chem. 283:5004-5013(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=12136135; DOI=10.1107/S0907444902008430;
Mittl P.R., Fritz G., Sargent D.F., Richmond T.J., Heizmann C.W.,
Grutter M.G.;
"Metal-free MIRAS phasing: structure of apo-S100A3.";
Acta Crystallogr. D 58:1255-1261(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), DISULFIDE BONDS, ZINC-BINDING
SITES, AND MUTAGENESIS OF CYS-30; CYS-68; CYS-81 AND CYS-99.
PubMed=21377473; DOI=10.1016/j.jmb.2011.02.055;
Unno M., Kawasaki T., Takahara H., Heizmann C.W., Kizawa K.;
"Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3
protein characterized by two disulfide bridges.";
J. Mol. Biol. 408:477-490(2011).
-!- FUNCTION: Binds both calcium and zinc. May be involved in calcium-
dependent cuticle cell differentiation, hair shaft and hair
cuticular barrier formation. {ECO:0000269|PubMed:18083705}.
-!- SUBUNIT: Homodimer and homotetramer for the citrullinated form.
{ECO:0000269|PubMed:18083705}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18083705}.
-!- TISSUE SPECIFICITY: Skin specific, specifically expressed at the
inner endocuticle of hair fibers. {ECO:0000269|PubMed:12470658}.
-!- PTM: More than half of the arginine residues undergo
citrullination by PAD1 and PAD2. Arg-51 is specifically
citrullinated by PAD3 and promotes tetramerization.
{ECO:0000269|PubMed:18083705}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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EMBL; Z18948; CAA79471.1; -; mRNA.
EMBL; Z18950; CAA79473.1; -; Genomic_DNA.
EMBL; BT006955; AAP35601.1; -; mRNA.
EMBL; CR542163; CAG46960.1; -; mRNA.
EMBL; CR542185; CAG46982.1; -; mRNA.
EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53306.1; -; Genomic_DNA.
EMBL; CH471121; EAW53307.1; -; Genomic_DNA.
EMBL; BC012893; AAH12893.1; -; mRNA.
CCDS; CCDS1043.1; -.
PIR; C48219; C48219.
PIR; S70326; S70326.
RefSeq; NP_002951.1; NM_002960.1.
UniGene; Hs.557609; -.
PDB; 1KSO; X-ray; 1.70 A; A/B=1-101.
PDB; 3NSI; X-ray; 2.15 A; A/B=1-101.
PDB; 3NSK; X-ray; 1.55 A; A/B=1-101.
PDB; 3NSL; X-ray; 1.50 A; A/B/C/D/E/F=2-101.
PDB; 3NSO; X-ray; 1.45 A; A/B=1-101.
PDBsum; 1KSO; -.
PDBsum; 3NSI; -.
PDBsum; 3NSK; -.
PDBsum; 3NSL; -.
PDBsum; 3NSO; -.
ProteinModelPortal; P33764; -.
SMR; P33764; -.
BioGrid; 112182; 21.
IntAct; P33764; 7.
STRING; 9606.ENSP00000357701; -.
iPTMnet; P33764; -.
BioMuta; S100A3; -.
DMDM; 464729; -.
EPD; P33764; -.
MaxQB; P33764; -.
PaxDb; P33764; -.
PeptideAtlas; P33764; -.
PRIDE; P33764; -.
ProteomicsDB; 54924; -.
DNASU; 6274; -.
Ensembl; ENST00000368712; ENSP00000357701; ENSG00000188015.
Ensembl; ENST00000368713; ENSP00000357702; ENSG00000188015.
GeneID; 6274; -.
KEGG; hsa:6274; -.
UCSC; uc001fca.2; human.
CTD; 6274; -.
DisGeNET; 6274; -.
EuPathDB; HostDB:ENSG00000188015.9; -.
GeneCards; S100A3; -.
H-InvDB; HIX0116376; -.
HGNC; HGNC:10493; S100A3.
HPA; HPA042674; -.
HPA; HPA056140; -.
MIM; 176992; gene.
neXtProt; NX_P33764; -.
OpenTargets; ENSG00000188015; -.
PharmGKB; PA34905; -.
eggNOG; ENOG410J3DW; Eukaryota.
eggNOG; ENOG411196G; LUCA.
GeneTree; ENSGT00760000119034; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P33764; -.
OMA; YFKDCPP; -.
OrthoDB; EOG091G10JX; -.
PhylomeDB; P33764; -.
TreeFam; TF332727; -.
EvolutionaryTrace; P33764; -.
GeneWiki; S100A3; -.
GenomeRNAi; 6274; -.
PRO; PR:P33764; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000188015; -.
CleanEx; HS_S100A3; -.
Genevisible; P33764; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
CDD; cd00213; S-100; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR034325; S-100_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028488; S100A3.
PANTHER; PTHR11639:SF12; PTHR11639:SF12; 1.
Pfam; PF01023; S_100; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Citrullination; Complete proteome;
Cytoplasm; Disulfide bond; Metal-binding; Polymorphism;
Reference proteome; Repeat; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12470658}.
CHAIN 2 101 Protein S100-A3.
/FTId=PRO_0000143972.
DOMAIN 12 47 EF-hand 1.
DOMAIN 50 85 EF-hand 2.
CA_BIND 20 33 1; low affinity. {ECO:0000255}.
CA_BIND 63 74 2; high affinity. {ECO:0000255}.
METAL 83 83 Zinc.
METAL 86 86 Zinc.
METAL 87 87 Zinc.
METAL 93 93 Zinc.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:12470658}.
MOD_RES 51 51 Citrulline; by PAD3.
{ECO:0000269|PubMed:18083705}.
DISULFID 30 68 {ECO:0000269|PubMed:21377473}.
DISULFID 81 99 {ECO:0000269|PubMed:21377473}.
VARIANT 3 3 R -> K (in dbSNP:rs36022742).
/FTId=VAR_061047.
MUTAGEN 30 30 C->A: Abolishes calcium binding; when
associated with Ala-68.
{ECO:0000269|PubMed:21377473}.
MUTAGEN 68 68 C->A: Abolishes calcium binding; when
associated with Ala-30.
{ECO:0000269|PubMed:21377473}.
MUTAGEN 81 81 C->A: Increases affinity for calcium;
when associated with Ala-99.
{ECO:0000269|PubMed:21377473}.
MUTAGEN 99 99 C->A: Increases affinity for calcium;
when associated with Ala-81.
{ECO:0000269|PubMed:21377473}.
HELIX 4 20 {ECO:0000244|PDB:3NSO}.
STRAND 22 24 {ECO:0000244|PDB:1KSO}.
STRAND 28 30 {ECO:0000244|PDB:3NSL}.
HELIX 31 41 {ECO:0000244|PDB:3NSO}.
TURN 42 44 {ECO:0000244|PDB:3NSO}.
TURN 49 51 {ECO:0000244|PDB:3NSK}.
HELIX 52 64 {ECO:0000244|PDB:3NSO}.
TURN 65 67 {ECO:0000244|PDB:3NSL}.
STRAND 68 71 {ECO:0000244|PDB:3NSL}.
HELIX 72 86 {ECO:0000244|PDB:3NSO}.
HELIX 88 90 {ECO:0000244|PDB:3NSO}.
SEQUENCE 101 AA; 11713 MW; ABCAF4B7E5F2E0A1 CRC64;
MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS
VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS Q


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