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S10A5_RAT
ID   S10A5_RAT               Reviewed;          93 AA.
AC   P63083; O88945; P82540;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Protein S100-A5;
DE   AltName: Full=Protein S-100D;
DE   AltName: Full=S100 calcium-binding protein A5;
GN   Name=S100a5; Synonyms=S100d;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10882717; DOI=10.1074/jbc.m002260200;
RA   Schaefer B.W., Fritschy J.-M., Murmann P., Troxler H., Durussel I.,
RA   Heizmann C.W., Cox J.A.;
RT   "Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding protein of
RT   the EF-hand superfamily.";
RL   J. Biol. Chem. 275:30623-30630(2000).
CC   -!- FUNCTION: Binds calcium, zinc and copper. One subunit can
CC       simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion.
CC       Calcium and copper ions compete for the same binding sites.
CC       {ECO:0000269|PubMed:10882717}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10882717}.
CC   -!- MASS SPECTROMETRY: Mass=10878; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10882717};
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   RefSeq; NP_001099908.1; NM_001106438.1.
DR   RefSeq; XP_006232663.1; XM_006232601.3.
DR   RefSeq; XP_017446250.1; XM_017590761.1.
DR   RefSeq; XP_017446251.1; XM_017590762.1.
DR   RefSeq; XP_017446252.1; XM_017590763.1.
DR   AlphaFoldDB; P63083; -.
DR   SMR; P63083; -.
DR   STRING; 10116.ENSRNOP00000015712; -.
DR   PaxDb; P63083; -.
DR   PRIDE; P63083; -.
DR   ABCD; P63083; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000015712; ENSRNOP00000015712; ENSRNOG00000011748.
DR   GeneID; 295211; -.
DR   KEGG; rno:295211; -.
DR   UCSC; RGD:1308996; rat.
DR   CTD; 6276; -.
DR   RGD; 1308996; S100a5.
DR   eggNOG; ENOG502S40V; Eukaryota.
DR   GeneTree; ENSGT00940000161986; -.
DR   HOGENOM; CLU_138624_2_0_1; -.
DR   InParanoid; P63083; -.
DR   OMA; HAVMETP; -.
DR   OrthoDB; 1563974at2759; -.
DR   PhylomeDB; P63083; -.
DR   TreeFam; TF332727; -.
DR   PRO; PR:P63083; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000011748; Expressed in thymus and 15 other tissues.
DR   Genevisible; P63083; RN.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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; IPR028497; S100-A5.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF65; PTHR11639:SF65; 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; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   1: Evidence at protein level;
KW   Calcium; Copper; Direct protein sequencing; Metal-binding;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN           1..93
FT                   /note="Protein S100-A5"
FT                   /id="PRO_0000143982"
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                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         33
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
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                   /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_label="2"
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_label="2"
FT                   /ligand_note="high affinity"
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                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   93 AA;  10812 MW;  9A922E1898D202A4 CRC64;
     METPLEKALT TMVTTFHKYS GREGSKLTLS RKELKELIKT ELSLAEKMKE SSIDNLMKSL
     DKNSDQEIDF KEYSVFLTTL CMAYNDFFLE DNK
 
 
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