ALBU_MACMU
ID ALBU_MACMU Reviewed; 600 AA.
AC Q28522;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Albumin;
DE Flags: Precursor; Fragment;
GN Name=ALB;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8460152; DOI=10.1073/pnas.90.6.2409;
RA Watkins S.A., Sakamoto Y., Madison J.M., Davis E.M., Smith D.G., Dwulet J.,
RA Putnam F.W.;
RT "cDNA and protein sequence of polymorphic macaque albumins that differ in
RT bilirubin binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2409-2413(1993).
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 at residue Asp-265
CC suggests a crosstalk between zinc and calcium transport in the blood
CC (By similarity). The rank order of affinity is zinc > calcium >
CC magnesium (By similarity). Binds to the bacterial siderophore
CC enterobactin and inhibits enterobactin-mediated iron uptake of E.coli
CC from ferric transferrin, and may thereby limit the utilization of iron
CC and growth of enteric bacteria such as E.coli (By similarity). Does not
CC prevent iron uptake by the bacterial siderophore aerobactin (By
CC similarity). {ECO:0000250|UniProtKB:P02768,
CC 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.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02768}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; M90463; AAA36906.1; -; mRNA.
DR PIR; A47391; A47391.
DR RefSeq; NP_001182578.1; NM_001195649.1.
DR AlphaFoldDB; Q28522; -.
DR SMR; Q28522; -.
DR STRING; 9544.ENSMMUP00000005100; -.
DR GeneID; 704892; -.
DR KEGG; mcc:704892; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; Q28522; -.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR CDD; cd00015; ALBUMIN; 3.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR Pfam; PF00273; Serum_albumin; 3.
DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 3.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Copper; Disulfide bond;
KW Lipid-binding; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL <1..10
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT PROPEP 11..16
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT /id="PRO_0000001069"
FT CHAIN 17..600
FT /note="Albumin"
FT /id="PRO_0000001070"
FT DOMAIN 11..202
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 203..395
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 396..593
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 19
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 256
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 221
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 452
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 535
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 550
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 580
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT DISULFID 69..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 91..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 106..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 140..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 184..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 216..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 261..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 281..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 294..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 332..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 376..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 408..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 453..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 477..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 492..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 530..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 574..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT NON_TER 1
SQ SEQUENCE 600 AA; 67881 MW; E45C871A670E740B CRC64;
LLFLFSSAYS RGVFRRDTHK SEVAHRFKDL GEEHFKGLVL VAFSQYLQQC PFEEHVKLVN
EVTEFAKTCV ADESAENCDK SLHTLFGDKL CTVATLRETY GEMADCCAKQ EPERNECFLQ
HKDDNPNLPP LVRPEVDVMC TAFHDNEATF LKKYLYEVAR RHPYFYAPEL LFFAARYKAA
FAECCQAADK AACLLPKLDE LRDEGKASSA KQRLKCASLQ KFGDRAFKAW AVARLSQKFP
KAEFAEVSKL VTDLTKVHTE CCHGDLLECA DDRADLAKYM CENQDSISSK LKECCDKPLL
EKSHCLAEVE NDEMPADLPS LAADYVESKD VCKNYAEAKD VFLGMFLYEY ARRHPDYSVM
LLLRLAKAYE ATLEKCCAAA DPHECYAKVF DEFQPLVEEP QNLVKQNCEL FEQLGEYKFQ
NALLVRYTKK VPQVSTPTLV EVSRNLGKVG AKCCKLPEAK RMPCAEDYLS VVLNRLCVLH
EKTPVSEKVT KCCTESLVNR RPCFSALELD EAYVPKAFNA ETFTFHADMC TLSEKEKQVK
KQTALVELVK HKPKATKEQL KGVMDNFAAF VEKCCKADDK EACFAEEGPK FVAASQAALA
