ALBU_PIG
ID ALBU_PIG Reviewed; 607 AA.
AC P08835; Q29018; Q68NH7;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Albumin;
DE Flags: Precursor;
GN Name=ALB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Sun S., Deng J., Zhou Y., Lu J., Wu X.;
RT "Porcine serum albumin gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-607.
RC TISSUE=Liver;
RX PubMed=3174440; DOI=10.1093/nar/16.18.9045;
RA Baldwin G.S., Weinstock J.;
RT "Nucleotide sequence of porcine liver albumin.";
RL Nucleic Acids Res. 16:9045-9045(1988).
RN [3]
RP PROTEIN SEQUENCE OF 25-57 AND 144-157.
RX PubMed=2728927; DOI=10.1002/jbmr.5650040216;
RA Limeback H., Sakarya H., Chu W., MacKinnon M.;
RT "Serum albumin and its acid hydrolysis peptides dominate preparations of
RT mineral-bound enamel proteins.";
RL J. Bone Miner. Res. 4:235-241(1989).
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-272
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 -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; AY663543; AAT98610.1; -; Genomic_DNA.
DR EMBL; X12422; CAA30970.1; -; mRNA.
DR EMBL; M36787; AAA30988.1; -; mRNA.
DR PIR; S01382; ABPGS.
DR RefSeq; NP_001005208.1; NM_001005208.1.
DR AlphaFoldDB; P08835; -.
DR SMR; P08835; -.
DR STRING; 9823.ENSSSCP00000009549; -.
DR Allergome; 11911; Sus s 1.0101.
DR Allergome; 757; Sus s 1.
DR PaxDb; P08835; -.
DR PeptideAtlas; P08835; -.
DR PRIDE; P08835; -.
DR GeneID; 396960; -.
DR KEGG; ssc:396960; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P08835; -.
DR OrthoDB; 906547at2759; -.
DR ChiTaRS; ALB; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0036094; F:small molecule binding; IPI:AgBase.
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 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Copper;
KW Direct protein sequencing; Disulfide bond; Lipid-binding; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT /id="PRO_0000001075"
FT CHAIN 25..607
FT /note="Albumin"
FT /id="PRO_0000001076"
FT DOMAIN 19..209
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 210..402
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 403..600
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 33
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 228
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 557
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 147..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 191..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 223..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 268..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 288..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 301..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 339..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 383..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 415..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 460..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 484..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 499..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 537..582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 581..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 146..151
FT /note="LCADFQ -> GYAEFE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="QK -> VN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="H -> D (in Ref. 2; CAA30970/AAA30988)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="E -> D (in Ref. 2; AAA30988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 69692 MW; 7B8DA13543CA99D8 CRC64;
MKWVTFISLL FLFSSAYSRG VFRRDTYKSE IAHRFKDLGE QYFKGLVLIA FSQHLQQCPY
EEHVKLVREV TEFAKTCVAD ESAENCDKSI HTLFGDKLCA IPSLREHYGD LADCCEKEEP
ERNECFLQHK NDNPDIPKLK PDPVALCADF QEDEQKFWGK YLYEIARRHP YFYAPELLYY
AIIYKDVFSE CCQAADKAAC LLPKIEHLRE KVLTSAAKQR LKCASIQKFG ERAFKAWSLA
RLSQRFPKAD FTEISKIVTD LAKVHKECCH GDLLECADDR ADLAKYICEN QDTISTKLKE
CCDKPLLEKS HCIAEAKRDE LPADLNPLEH DFVEDKEVCK NYKEAKHVFL GTFLYEYSRR
HPDYSVSLLL RIAKIYEATL EDCCAKEDPP ACYATVFDKF QPLVDEPKNL IKQNCELFEK
LGEYGFQNAL IVRYTKKVPQ VSTPTLVEVA RKLGLVGSRC CKRPEEERLS CAEDYLSLVL
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY KPKEFVEGTF TFHADLCTLP
EDEKQIKKQT ALVELLKHKP HATEEQLRTV LGNFAAFVQK CCAAPDHEAC FAVEGPKFVI
EIRGILA
