ID   ALBU_DAMDA              Reviewed;          10 AA.
AC   C0HJD2;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Serum albumin {ECO:0000303|PubMed:24410890};
DE   Flags: Fragment;
OS   Dama dama (Fallow deer) (Cervus dama).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Dama.
OX   NCBI_TaxID=30532;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta {ECO:0000269|PubMed:24410890};
RX   PubMed=24410890; DOI=10.1186/1751-0147-56-4;
RA   Beriot M., Tchimbou A.F., Barbato O., Beckers J.F., de Sousa N.M.;
RT   "Identification of pregnancy-associated glycoproteins and alpha-fetoprotein
RT   in fallow deer (Dama dama) placenta.";
RL   Acta Vet. Scand. 56:4-4(2014).
CC   -!- FUNCTION: Serum albumin, the main protein of plasma, has a good binding
CC       capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC       bilirubin and drugs (By similarity). Its main function is the
CC       regulation of the colloidal osmotic pressure of blood (By similarity).
CC       Major zinc transporter in plasma, typically binds about 80% of all
CC       plasma zinc (By similarity). Major calcium and magnesium transporter in
CC       plasma, binds approximately 45% of circulating calcium and magnesium in
CC       plasma (By similarity). Potentially has more than two calcium-binding
CC       sites and might additionally bind calcium in a non-specific manner (By
CC       similarity). The shared binding site between zinc and calcium suggests
CC       a crosstalk between zinc and calcium transport in the blood (By
CC       similarity). The rank order of affinity is zinc > calcium > magnesium
CC       (By similarity). Binds to the bacterial siderophore enterobactin and
CC       inhibits enterobactin-mediated iron uptake of E.coli from ferric
CC       transferrin, and may thereby limit the utilization of iron and growth
CC       of enteric bacteria such as E.coli (By similarity). Does not prevent
CC       iron uptake by the bacterial siderophore aerobactin (By similarity).
CC       {ECO:0000250|UniProtKB:P02768, ECO:0000250|UniProtKB:P02769}.
CC   -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB
CC       homeostasis (By similarity). Interacts with TASOR (By similarity). In
CC       plasma, occurs in a covalently-linked complex with chromophore-bound
CC       alpha-1-microglobulin; this interaction does not prevent fatty acid
CC       binding to ALB. {ECO:0000250|UniProtKB:P02768,
CC       ECO:0000250|UniProtKB:P07724}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02769,
CC       ECO:0000255|PROSITE-ProRule:PRU00769}.
CC   -!- TISSUE SPECIFICITY: Expressed in placenta, specifically the maternal
CC       caruncula tissue (MCT) (at protein level).
CC       {ECO:0000269|PubMed:24410890}.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lipid-binding; Metal-binding;
KW   Phosphoprotein; Secreted; Zinc.
FT   CHAIN           1..>10
FT                   /note="Serum albumin"
FT                   /evidence="ECO:0000269|PubMed:24410890"
FT                   /id="PRO_0000423369"
FT   BINDING         6
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:24410890"
SQ   SEQUENCE   10 AA;  1193 MW;  EC51B9D05B05B331 CRC64;
     DTHKSEIAHR