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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
 
 
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