S10A7_BOVIN
ID S10A7_BOVIN Reviewed; 101 AA.
AC Q28050; A5PJH5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein S100-A7;
DE AltName: Full=Calcium-binding protein in amniotic fluid 2;
DE Short=CAAF2;
DE AltName: Full=Dander minor allergen BDA11;
DE AltName: Full=Dermal allergen BDA11;
DE AltName: Full=S100 calcium-binding protein A7;
DE AltName: Allergen=Bos d 3;
GN Name=S100A7; Synonyms=CAAF2;
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], AND PROTEIN SEQUENCE OF 20-33; 38-49 AND
RP 70-101.
RC TISSUE=Skin;
RX PubMed=7594639; DOI=10.1111/1523-1747.ep12324309;
RA Rautiainen J., Rytkoenen M., Parkkinen S., Pentikaeinen J.,
RA Linnala-Kankkunen A., Virtanen T., Pelkonen J., Maentyjaervi R.;
RT "cDNA cloning and protein analysis of a bovine dermal allergen with
RT homology to psoriasin.";
RL J. Invest. Dermatol. 105:660-663(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=8941350; DOI=10.1006/bbrc.1996.1728;
RA Hitomi J., Maruyama K., Kikuchi Y., Nagasaki K., Yamaguchi K.;
RT "Characterization of a new calcium-binding protein abundant in amniotic
RT fluid, CAAF2, which is produced by fetal epidermal keratinocytes during
RT embryogenesis.";
RL Biochem. Biophys. Res. Commun. 228:757-763(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with RANBP9. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}.
CC Note=Secreted by a non-classical secretory pathway. {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Minor allergen of
CC bovine dander.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; L39834; AAA91101.1; -; mRNA.
DR EMBL; D49550; BAA08498.1; -; mRNA.
DR EMBL; BC142114; AAI42115.1; -; mRNA.
DR RefSeq; NP_777021.1; NM_174596.2.
DR AlphaFoldDB; Q28050; -.
DR SMR; Q28050; -.
DR STRING; 9913.ENSBTAP00000010838; -.
DR Allergome; 162; Bos d 3.
DR Allergome; 3164; Bos d 3.0101.
DR PaxDb; Q28050; -.
DR PeptideAtlas; Q28050; -.
DR Ensembl; ENSBTAT00000010838; ENSBTAP00000010838; ENSBTAG00000008238.
DR GeneID; 282344; -.
DR KEGG; bta:282344; -.
DR CTD; 6278; -.
DR VEuPathDB; HostDB:ENSBTAG00000008238; -.
DR eggNOG; ENOG502SZJ5; Eukaryota.
DR GeneTree; ENSGT00940000163629; -.
DR HOGENOM; CLU_138624_5_0_1; -.
DR InParanoid; Q28050; -.
DR OMA; VELFHRY; -.
DR OrthoDB; 1486203at2759; -.
DR TreeFam; TF341148; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-6799990; Metal sequestration by antimicrobial proteins.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000008238; Expressed in zone of skin and 59 other tissues.
DR ExpressionAtlas; Q28050; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028477; S100A7.
DR PANTHER; PTHR11639:SF67; PTHR11639:SF67; 1.
DR Pfam; PF00036; EF-hand_1; 1.
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; 2.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allergen; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat; Secreted; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P31151"
FT CHAIN 2..101
FT /note="Protein S100-A7"
FT /id="PRO_0000143989"
FT DOMAIN 8..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P31151"
FT CONFLICT 38
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 101 AA; 11544 MW; 1D8E4E5D56661AFA CRC64;
MSSSQLEQAI TDLINLFHKY SGSDDTIEKE DLLRLMKDNF PNFLGACEKR GRDYLSNIFE
KQDKNKDRKI DFSEFLSLLA DIATDYHNHS HGAQLCSGGN Q