Full text data of S100A3
S100A3
(S100E)
[Confidence: low (only semi-automatic identification from reviews)]
Protein S100-A3 (Protein S-100E; S100 calcium-binding protein A3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein S100-A3 (Protein S-100E; S100 calcium-binding protein A3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P33764
ID S10A3_HUMAN Reviewed; 101 AA.
AC P33764; D3DV51; Q6FGE4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Protein S100-A3;
DE AltName: Full=Protein S-100E;
DE AltName: Full=S100 calcium-binding protein A3;
GN Name=S100A3; Synonyms=S100E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8341667; DOI=10.1073/pnas.90.14.6547;
RA Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.;
RT "Six S100 genes are clustered on human chromosome 1q21: identification
RT of two genes coding for the two previously unreported calcium-binding
RT proteins S100D and S100E.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9920417; DOI=10.1016/S0167-4889(98)00138-4;
RA Fritz G., Heizmann C.W., Kroneck P.M.H.;
RT "Probing the structure of the human Ca2+- and Zn2+-binding protein
RT S100A3: spectroscopic investigations of its transition metal ion
RT complexes, and three-dimensional structural model.";
RL Biochim. Biophys. Acta 1448:264-276(1998).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND TISSUE
RP SPECIFICITY.
RX PubMed=12470658; DOI=10.1016/S0006-291X(02)02744-4;
RA Kizawa K., Troxler H., Kleinert P., Inoue T., Toyoda M., Morohashi M.,
RA Heizmann C.W.;
RT "Characterization of the cysteine-rich calcium-binding S100A3 protein
RT from human hair cuticles.";
RL Biochem. Biophys. Res. Commun. 299:857-862(2002).
RN [9]
RP FUNCTION, SUBUNIT, CITRULLINATION AT ARG-51, AND SUBCELLULAR LOCATION.
RX PubMed=18083705; DOI=10.1074/jbc.M709357200;
RA Kizawa K., Takahara H., Troxler H., Kleinert P., Mochida U.,
RA Heizmann C.W.;
RT "Specific citrullination causes assembly of a globular S100A3
RT homotetramer: a putative Ca2+ modulator matures human hair cuticle.";
RL J. Biol. Chem. 283:5004-5013(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=12136135; DOI=10.1107/S0907444902008430;
RA Mittl P.R., Fritz G., Sargent D.F., Richmond T.J., Heizmann C.W.,
RA Grutter M.G.;
RT "Metal-free MIRAS phasing: structure of apo-S100A3.";
RL Acta Crystallogr. D 58:1255-1261(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), DISULFIDE BONDS, ZINC-BINDING
RP SITES, AND MUTAGENESIS OF CYS-30; CYS-68; CSY-81 AND CYS-99.
RX PubMed=21377473; DOI=10.1016/j.jmb.2011.02.055;
RA Unno M., Kawasaki T., Takahara H., Heizmann C.W., Kizawa K.;
RT "Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3
RT protein characterized by two disulfide bridges.";
RL J. Mol. Biol. 408:477-490(2011).
CC -!- FUNCTION: Binds both calcium and zinc. May be involved in calcium-
CC dependent cuticle cell differentiation, hair shaft and hair
CC cuticular barrier formation.
CC -!- SUBUNIT: Homodimer and homotetramer for the citrullinated form.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Skin specific, specifically expressed at the
CC inner endocuticle of hair fibers.
CC -!- PTM: More than half of the arginine residues undergo
CC citrullination by PAD1 and PAD2. Arg-51 is specifically
CC citrullinated by PAD3 and promotes tetramerization.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z18948; CAA79471.1; -; mRNA.
DR EMBL; Z18950; CAA79473.1; -; Genomic_DNA.
DR EMBL; BT006955; AAP35601.1; -; mRNA.
DR EMBL; CR542163; CAG46960.1; -; mRNA.
DR EMBL; CR542185; CAG46982.1; -; mRNA.
DR EMBL; BX470102; CAI14755.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53306.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53307.1; -; Genomic_DNA.
DR EMBL; BC012893; AAH12893.1; -; mRNA.
DR PIR; C48219; C48219.
DR PIR; S70326; S70326.
DR RefSeq; NP_002951.1; NM_002960.1.
DR RefSeq; XP_005245483.1; XM_005245426.1.
DR UniGene; Hs.557609; -.
DR PDB; 1KSO; X-ray; 1.70 A; A/B=1-101.
DR PDB; 3NSI; X-ray; 2.15 A; A/B=1-101.
DR PDB; 3NSK; X-ray; 1.55 A; A/B=1-101.
DR PDB; 3NSL; X-ray; 1.50 A; A/B/C/D/E/F=2-101.
DR PDB; 3NSO; X-ray; 1.45 A; A/B=1-101.
DR PDBsum; 1KSO; -.
DR PDBsum; 3NSI; -.
DR PDBsum; 3NSK; -.
DR PDBsum; 3NSL; -.
DR PDBsum; 3NSO; -.
DR ProteinModelPortal; P33764; -.
DR SMR; P33764; 2-94.
DR MINT; MINT-4714713; -.
DR STRING; 9606.ENSP00000357701; -.
DR DMDM; 464729; -.
DR PaxDb; P33764; -.
DR PeptideAtlas; P33764; -.
DR PRIDE; P33764; -.
DR DNASU; 6274; -.
DR Ensembl; ENST00000368712; ENSP00000357701; ENSG00000188015.
DR Ensembl; ENST00000368713; ENSP00000357702; ENSG00000188015.
DR GeneID; 6274; -.
DR KEGG; hsa:6274; -.
DR UCSC; uc001fca.1; human.
DR CTD; 6274; -.
DR GeneCards; GC01M153519; -.
DR H-InvDB; HIX0116376; -.
DR HGNC; HGNC:10493; S100A3.
DR HPA; HPA042674; -.
DR MIM; 176992; gene.
DR neXtProt; NX_P33764; -.
DR PharmGKB; PA34905; -.
DR eggNOG; NOG40471; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P33764; -.
DR OMA; CEVDFAE; -.
DR OrthoDB; EOG779P19; -.
DR PhylomeDB; P33764; -.
DR EvolutionaryTrace; P33764; -.
DR GeneWiki; S100A3; -.
DR GenomeRNAi; 6274; -.
DR NextBio; 24351; -.
DR PRO; PR:P33764; -.
DR Bgee; P33764; -.
DR CleanEx; HS_S100A3; -.
DR Genevestigator; P33764; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028488; S100A3.
DR PANTHER; PTHR11639:SF12; PTHR11639:SF12; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Citrullination; Complete proteome;
KW Cytoplasm; Disulfide bond; Metal-binding; Polymorphism;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 101 Protein S100-A3.
FT /FTId=PRO_0000143972.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 50 85 EF-hand 2.
FT CA_BIND 20 33 1; low affinity (Potential).
FT CA_BIND 63 74 2; high affinity (Potential).
FT METAL 83 83 Zinc.
FT METAL 86 86 Zinc.
FT METAL 87 87 Zinc.
FT METAL 93 93 Zinc.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 51 51 Citrulline; by PAD3.
FT DISULFID 30 68
FT DISULFID 81 99
FT VARIANT 3 3 R -> K (in dbSNP:rs36022742).
FT /FTId=VAR_061047.
FT MUTAGEN 30 30 C->A: Abolishes calcium binding; when
FT associated with Ala-68.
FT MUTAGEN 68 68 C->A: Abolishes calcium binding; when
FT associated with Ala-30.
FT MUTAGEN 81 81 C->A: Increases affinity for calcium;
FT when associated with Ala-99.
FT MUTAGEN 99 99 C->A: Increases affinity for calcium;
FT when associated with Ala-81.
FT HELIX 4 20
FT STRAND 22 24
FT STRAND 28 30
FT HELIX 31 41
FT TURN 42 44
FT TURN 49 51
FT HELIX 52 64
FT TURN 65 67
FT STRAND 68 71
FT HELIX 72 86
FT HELIX 88 90
SQ SEQUENCE 101 AA; 11713 MW; ABCAF4B7E5F2E0A1 CRC64;
MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS
VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS Q
//
ID S10A3_HUMAN Reviewed; 101 AA.
AC P33764; D3DV51; Q6FGE4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1994, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Protein S100-A3;
DE AltName: Full=Protein S-100E;
DE AltName: Full=S100 calcium-binding protein A3;
GN Name=S100A3; Synonyms=S100E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8341667; DOI=10.1073/pnas.90.14.6547;
RA Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.;
RT "Six S100 genes are clustered on human chromosome 1q21: identification
RT of two genes coding for the two previously unreported calcium-binding
RT proteins S100D and S100E.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9920417; DOI=10.1016/S0167-4889(98)00138-4;
RA Fritz G., Heizmann C.W., Kroneck P.M.H.;
RT "Probing the structure of the human Ca2+- and Zn2+-binding protein
RT S100A3: spectroscopic investigations of its transition metal ion
RT complexes, and three-dimensional structural model.";
RL Biochim. Biophys. Acta 1448:264-276(1998).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND TISSUE
RP SPECIFICITY.
RX PubMed=12470658; DOI=10.1016/S0006-291X(02)02744-4;
RA Kizawa K., Troxler H., Kleinert P., Inoue T., Toyoda M., Morohashi M.,
RA Heizmann C.W.;
RT "Characterization of the cysteine-rich calcium-binding S100A3 protein
RT from human hair cuticles.";
RL Biochem. Biophys. Res. Commun. 299:857-862(2002).
RN [9]
RP FUNCTION, SUBUNIT, CITRULLINATION AT ARG-51, AND SUBCELLULAR LOCATION.
RX PubMed=18083705; DOI=10.1074/jbc.M709357200;
RA Kizawa K., Takahara H., Troxler H., Kleinert P., Mochida U.,
RA Heizmann C.W.;
RT "Specific citrullination causes assembly of a globular S100A3
RT homotetramer: a putative Ca2+ modulator matures human hair cuticle.";
RL J. Biol. Chem. 283:5004-5013(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=12136135; DOI=10.1107/S0907444902008430;
RA Mittl P.R., Fritz G., Sargent D.F., Richmond T.J., Heizmann C.W.,
RA Grutter M.G.;
RT "Metal-free MIRAS phasing: structure of apo-S100A3.";
RL Acta Crystallogr. D 58:1255-1261(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), DISULFIDE BONDS, ZINC-BINDING
RP SITES, AND MUTAGENESIS OF CYS-30; CYS-68; CSY-81 AND CYS-99.
RX PubMed=21377473; DOI=10.1016/j.jmb.2011.02.055;
RA Unno M., Kawasaki T., Takahara H., Heizmann C.W., Kizawa K.;
RT "Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3
RT protein characterized by two disulfide bridges.";
RL J. Mol. Biol. 408:477-490(2011).
CC -!- FUNCTION: Binds both calcium and zinc. May be involved in calcium-
CC dependent cuticle cell differentiation, hair shaft and hair
CC cuticular barrier formation.
CC -!- SUBUNIT: Homodimer and homotetramer for the citrullinated form.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Skin specific, specifically expressed at the
CC inner endocuticle of hair fibers.
CC -!- PTM: More than half of the arginine residues undergo
CC citrullination by PAD1 and PAD2. Arg-51 is specifically
CC citrullinated by PAD3 and promotes tetramerization.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z18948; CAA79471.1; -; mRNA.
DR EMBL; Z18950; CAA79473.1; -; Genomic_DNA.
DR EMBL; BT006955; AAP35601.1; -; mRNA.
DR EMBL; CR542163; CAG46960.1; -; mRNA.
DR EMBL; CR542185; CAG46982.1; -; mRNA.
DR EMBL; BX470102; CAI14755.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53306.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53307.1; -; Genomic_DNA.
DR EMBL; BC012893; AAH12893.1; -; mRNA.
DR PIR; C48219; C48219.
DR PIR; S70326; S70326.
DR RefSeq; NP_002951.1; NM_002960.1.
DR RefSeq; XP_005245483.1; XM_005245426.1.
DR UniGene; Hs.557609; -.
DR PDB; 1KSO; X-ray; 1.70 A; A/B=1-101.
DR PDB; 3NSI; X-ray; 2.15 A; A/B=1-101.
DR PDB; 3NSK; X-ray; 1.55 A; A/B=1-101.
DR PDB; 3NSL; X-ray; 1.50 A; A/B/C/D/E/F=2-101.
DR PDB; 3NSO; X-ray; 1.45 A; A/B=1-101.
DR PDBsum; 1KSO; -.
DR PDBsum; 3NSI; -.
DR PDBsum; 3NSK; -.
DR PDBsum; 3NSL; -.
DR PDBsum; 3NSO; -.
DR ProteinModelPortal; P33764; -.
DR SMR; P33764; 2-94.
DR MINT; MINT-4714713; -.
DR STRING; 9606.ENSP00000357701; -.
DR DMDM; 464729; -.
DR PaxDb; P33764; -.
DR PeptideAtlas; P33764; -.
DR PRIDE; P33764; -.
DR DNASU; 6274; -.
DR Ensembl; ENST00000368712; ENSP00000357701; ENSG00000188015.
DR Ensembl; ENST00000368713; ENSP00000357702; ENSG00000188015.
DR GeneID; 6274; -.
DR KEGG; hsa:6274; -.
DR UCSC; uc001fca.1; human.
DR CTD; 6274; -.
DR GeneCards; GC01M153519; -.
DR H-InvDB; HIX0116376; -.
DR HGNC; HGNC:10493; S100A3.
DR HPA; HPA042674; -.
DR MIM; 176992; gene.
DR neXtProt; NX_P33764; -.
DR PharmGKB; PA34905; -.
DR eggNOG; NOG40471; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P33764; -.
DR OMA; CEVDFAE; -.
DR OrthoDB; EOG779P19; -.
DR PhylomeDB; P33764; -.
DR EvolutionaryTrace; P33764; -.
DR GeneWiki; S100A3; -.
DR GenomeRNAi; 6274; -.
DR NextBio; 24351; -.
DR PRO; PR:P33764; -.
DR Bgee; P33764; -.
DR CleanEx; HS_S100A3; -.
DR Genevestigator; P33764; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028488; S100A3.
DR PANTHER; PTHR11639:SF12; PTHR11639:SF12; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Citrullination; Complete proteome;
KW Cytoplasm; Disulfide bond; Metal-binding; Polymorphism;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 101 Protein S100-A3.
FT /FTId=PRO_0000143972.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 50 85 EF-hand 2.
FT CA_BIND 20 33 1; low affinity (Potential).
FT CA_BIND 63 74 2; high affinity (Potential).
FT METAL 83 83 Zinc.
FT METAL 86 86 Zinc.
FT METAL 87 87 Zinc.
FT METAL 93 93 Zinc.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 51 51 Citrulline; by PAD3.
FT DISULFID 30 68
FT DISULFID 81 99
FT VARIANT 3 3 R -> K (in dbSNP:rs36022742).
FT /FTId=VAR_061047.
FT MUTAGEN 30 30 C->A: Abolishes calcium binding; when
FT associated with Ala-68.
FT MUTAGEN 68 68 C->A: Abolishes calcium binding; when
FT associated with Ala-30.
FT MUTAGEN 81 81 C->A: Increases affinity for calcium;
FT when associated with Ala-99.
FT MUTAGEN 99 99 C->A: Increases affinity for calcium;
FT when associated with Ala-81.
FT HELIX 4 20
FT STRAND 22 24
FT STRAND 28 30
FT HELIX 31 41
FT TURN 42 44
FT TURN 49 51
FT HELIX 52 64
FT TURN 65 67
FT STRAND 68 71
FT HELIX 72 86
FT HELIX 88 90
SQ SEQUENCE 101 AA; 11713 MW; ABCAF4B7E5F2E0A1 CRC64;
MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS
VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS Q
//
MIM
176992
*RECORD*
*FIELD* NO
176992
*FIELD* TI
*176992 S100 CALCIUM-BINDING PROTEIN A3; S100A3
;;S100E
*FIELD* TX
Engelkamp et al. (1993) demonstrated that the S100E protein is encoded
read moreby a gene located in a tight cluster of genes of similar structure in a
15-kb region of 1q21. The order of the genes from 5-prime to 3-prime was
found to be S100E, CAPL (S100A4; 114210), S100D (S100A5; 176991), CACY
(S100A6; 114110). The product of the S100E gene is cysteine-rich. The 4
genes were arranged in head-to-tail order. Despite the tight clustering,
each of the genes was expressed in different human tissues and probably
even at different times. Disruption of the cluster may occur in
neoplasia since the region 1q21 often shows structural alterations.
Schafer et al. (1995) isolated a YAC clone from 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. Clustered organization allowed introduction of a new logical
nomenclature for these genes, based on their physical arrangement on the
chromosome. S100E became S100A3 in the new nomenclature. The 9 genes are
in sequence with S100A1 (176940) being closest to the telomere and
S100A9 (123886) being closest to the centromere.
*FIELD* RF
1. Engelkamp, D.; Schafer, 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. Nat. Acad. Sci. 90: 6547-6551, 1993.
2. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
*FIELD* CD
Victor A. McKusick: 8/25/1993
*FIELD* ED
alopez: 10/12/1998
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 8/25/1993
*RECORD*
*FIELD* NO
176992
*FIELD* TI
*176992 S100 CALCIUM-BINDING PROTEIN A3; S100A3
;;S100E
*FIELD* TX
Engelkamp et al. (1993) demonstrated that the S100E protein is encoded
read moreby a gene located in a tight cluster of genes of similar structure in a
15-kb region of 1q21. The order of the genes from 5-prime to 3-prime was
found to be S100E, CAPL (S100A4; 114210), S100D (S100A5; 176991), CACY
(S100A6; 114110). The product of the S100E gene is cysteine-rich. The 4
genes were arranged in head-to-tail order. Despite the tight clustering,
each of the genes was expressed in different human tissues and probably
even at different times. Disruption of the cluster may occur in
neoplasia since the region 1q21 often shows structural alterations.
Schafer et al. (1995) isolated a YAC clone from 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. Clustered organization allowed introduction of a new logical
nomenclature for these genes, based on their physical arrangement on the
chromosome. S100E became S100A3 in the new nomenclature. The 9 genes are
in sequence with S100A1 (176940) being closest to the telomere and
S100A9 (123886) being closest to the centromere.
*FIELD* RF
1. Engelkamp, D.; Schafer, 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. Nat. Acad. Sci. 90: 6547-6551, 1993.
2. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
*FIELD* CD
Victor A. McKusick: 8/25/1993
*FIELD* ED
alopez: 10/12/1998
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 8/25/1993