ALBU_CAPHI
ID ALBU_CAPHI Reviewed; 90 AA.
AC P85295;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Albumin;
DE Flags: Fragments;
GN Name=ALB {ECO:0000250|UniProtKB:P02769};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP PROTEIN SEQUENCE OF 1-15, AND INDUCTION.
RA Wanigasekera A., Hiraga K.;
RT "Goat milk proteins induced by some feeding conditions.";
RL Submitted (OCT-2007) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE OF 16-90.
RA Koenig S., Mehlich A.M., Ackermann D.;
RT "Access to lower abundant bovine and caprine whey proteins: the impact of
RT caseins and beta-lactoglobulin on proteome analysis.";
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC bilirubin and drugs. Its main function is the regulation of the
CC colloidal osmotic pressure of blood. Major zinc transporter in plasma,
CC typically binds about 80% of all plasma zinc (By similarity). Major
CC calcium and magnesium transporter in plasma, binds approximately 45% of
CC circulating calcium and magnesium in plasma (By similarity).
CC Potentially has more than two calcium-binding sites and might
CC additionally bind calcium in a non-specific manner (By similarity). The
CC shared binding site between zinc and calcium suggests a crosstalk
CC between zinc and calcium transport in the blood (By similarity). The
CC rank order of affinity is zinc > calcium > magnesium (By similarity).
CC Binds to the bacterial siderophore enterobactin and inhibits
CC enterobactin-mediated iron uptake of E.coli from ferric transferrin,
CC and may thereby limit the utilization of iron and growth of enteric
CC bacteria such as E.coli (By similarity). Does not prevent iron uptake
CC 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:0000305}.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by fat diet. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255}.
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DR Allergome; 1496; Cap h 6.
DR PRIDE; P85295; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR020858; Serum_albumin-like.
DR SUPFAM; SSF48552; SSF48552; 1.
PE 1: Evidence at protein level;
KW Calcium; Copper; Direct protein sequencing; Lipid-binding; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Secreted; Zinc.
FT CHAIN <1..>90
FT /note="Albumin"
FT /id="PRO_0000307919"
FT DOMAIN 25..>90
FT /note="Albumin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 6
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 80
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT UNSURE 25
FT /note="L or I"
FT UNSURE 26
FT /note="L or I"
FT UNSURE 29
FT /note="L or I"
FT UNSURE 34
FT /note="Q or K"
FT UNSURE 36
FT /note="L or I"
FT UNSURE 37
FT /note="I or L"
FT UNSURE 38
FT /note="K or Q"
FT UNSURE 39
FT /note="K or Q"
FT UNSURE 46
FT /note="Q or K"
FT UNSURE 49
FT /note="L or I"
FT UNSURE 50
FT /note="I or L"
FT UNSURE 56
FT /note="K or Q"
FT UNSURE 59
FT /note="Q or K"
FT UNSURE 65
FT /note="L or I"
FT UNSURE 68
FT /note="I or L"
FT UNSURE 71
FT /note="K or Q"
FT UNSURE 72
FT /note="Q or K"
FT UNSURE 75
FT /note="L or I"
FT UNSURE 78
FT /note="L or I"
FT UNSURE 79
FT /note="L or I"
FT UNSURE 80
FT /note="K or Q"
FT UNSURE 81
FT /note="L or I"
FT UNSURE 86
FT /note="Q or K"
FT UNSURE 89
FT /note="L or I"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_CONS 27..28
FT /evidence="ECO:0000305"
FT NON_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_CONS 70..71
FT /evidence="ECO:0000305"
FT NON_CONS 80..81
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 90
SQ SEQUENCE 90 AA; 10055 MW; 230CBB6A61921DB1 CRC64;
DTHKSEIAHR FNDLGRHPEY AVSVLLRHLV DEPQNLIKKH GEYGFQNALI VRXXXKAPQV
STPTLVEISR KQTALVELLK LVASTQAALA
