ALBU_RAT
ID ALBU_RAT Reviewed; 608 AA.
AC P02770; P11382; Q5U3X3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Albumin;
DE Flags: Precursor;
GN Name=Alb;
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 NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7017712; DOI=10.1073/pnas.78.1.243;
RA Sargent T.D., Yang M., Bonner J.;
RT "Nucleotide sequence of cloned rat serum albumin messenger RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:243-246(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-262.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 1-38 (PRECURSOR PROTEIN), PROTEOLYTIC PROCESSING, AND
RP IDENTIFICATION OF PROPEPTIDE CLEAVAGE SITE.
RX PubMed=893447; DOI=10.1016/s0021-9258(17)39927-1;
RA Strauss A.W., Bennett C.D., Donohue A.M., Rodkey J.A., Alberts A.W.;
RT "Rat liver pre-proalbumin: complete amino acid sequence of the pre-piece.
RT Analysis of the direct translation product of albumin messenger RNA.";
RL J. Biol. Chem. 252:6846-6855(1977).
RN [4]
RP PROTEIN SEQUENCE OF 19-27 AND 606-608.
RC TISSUE=Liver;
RX PubMed=7358734; DOI=10.1016/s0021-9258(19)85865-9;
RA Peters T. Jr., Reed R.G.;
RT "The biosynthesis of rat serum albumin. Composition and properties of the
RT intracellular precursor, proalbumin.";
RL J. Biol. Chem. 255:3156-3163(1980).
RN [5]
RP PROTEIN SEQUENCE OF 25-222.
RX PubMed=564345; DOI=10.1093/oxfordjournals.jbchem.a131910;
RA Isemura S., Ikenaka T.;
RT "Amino acid sequences of fragments I and II obtained by cyanogen bromide
RT cleavage of rat serum albumin.";
RL J. Biochem. 83:35-48(1978).
RN [6]
RP PROTEIN SEQUENCE OF 166-174.
RC TISSUE=Plasma;
RX PubMed=2437111; DOI=10.1016/s0021-9258(18)45523-8;
RA Carraway R.E., Mitra S.P., Cochrane D.E.;
RT "Structure of a biologically active neurotensin-related peptide obtained
RT from pepsin-treated albumin(s).";
RL J. Biol. Chem. 262:5968-5973(1987).
RN [7]
RP PROTEIN SEQUENCE OF 35-57; 66-75; 89-97; 168-181; 247-264; 287-298;
RP 361-372; 376-383; 414-434; 439-452; 470-483; 509-524; 528-545; 570-581 AND
RP 585-602, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 223-288 AND 572-608.
RX PubMed=956149; DOI=10.1093/oxfordjournals.jbchem.a131173;
RA Isemura S., Ikenaka T.;
RT "Fragmentation of rat serum albumin by cyanogen bromide cleavage and the
RT amino acid sequences of four fragments.";
RL J. Biochem. 79:1183-1196(1976).
RN [9]
RP COPPER-BINDING.
RX PubMed=80265;
RA Aoyagi Y., Ikenaka T., Ichida F.;
RT "Copper(II)-binding ability of human alpha-fetoprotein.";
RL Cancer Res. 38:3483-3486(1978).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND THR-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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-273
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}.
CC -!- CAUTION: A peptide arising from positions 166 to 174 was originally
CC termed neurotensin-related peptide (NRP) and was thought to regulate
CC fat digestion, lipid absorption, and blood flow.
CC {ECO:0000305|PubMed:2437111}.
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DR EMBL; V01222; CAA24532.1; -; mRNA.
DR EMBL; BC085359; AAH85359.1; -; mRNA.
DR PIR; A93872; ABRTS.
DR RefSeq; NP_599153.2; NM_134326.2.
DR AlphaFoldDB; P02770; -.
DR SMR; P02770; -.
DR BioGRID; 246376; 1.
DR CORUM; P02770; -.
DR IntAct; P02770; 3.
DR STRING; 10116.ENSRNOP00000003921; -.
DR BindingDB; P02770; -.
DR ChEMBL; CHEMBL4817; -.
DR Allergome; 756; Rat n 4.
DR CarbonylDB; P02770; -.
DR iPTMnet; P02770; -.
DR PhosphoSitePlus; P02770; -.
DR SwissPalm; P02770; -.
DR UCD-2DPAGE; P02770; -.
DR World-2DPAGE; 0004:P02770; -.
DR jPOST; P02770; -.
DR PaxDb; P02770; -.
DR PRIDE; P02770; -.
DR ABCD; P02770; 2 sequenced antibodies.
DR GeneID; 24186; -.
DR KEGG; rno:24186; -.
DR UCSC; RGD:2085; rat.
DR CTD; 213; -.
DR RGD; 2085; Alb.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P02770; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; P02770; -.
DR TreeFam; TF335561; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-189451; Heme biosynthesis.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR SABIO-RK; P02770; -.
DR PRO; PR:P02770; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0140272; F:exogenous protein binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0072341; F:modified amino acid binding; IPI:RGD.
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; IDA:RGD.
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 GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IDA:RGD.
DR GO; GO:0046689; P:response to mercury ion; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0070541; P:response to platinum ion; IEP:RGD.
DR GO; GO:0042311; P:vasodilation; NAS:RGD.
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:0000269|PubMed:893447"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:893447"
FT /id="PRO_0000001079"
FT CHAIN 25..608
FT /note="Albumin"
FT /id="PRO_0000001080"
FT DOMAIN 19..211
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 212..403
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 404..601
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 27
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:80265"
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 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 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="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 279
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 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 460
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 543
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 558
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 588
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
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 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT VARIANT 262
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 174
FT /note="Y -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="I -> T (in Ref. 1; CAA24532)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="V -> I (in Ref. 2; AAH85359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 68731 MW; 07475796EA94938C CRC64;
MKWVTFLLLL FISGSAFSRG VFRREAHKSE IAHRFKDLGE QHFKGLVLIA FSQYLQKCPY
EEHIKLVQEV TDFAKTCVAD ENAENCDKSI HTLFGDKLCA IPKLRDNYGE LADCCAKQEP
ERNECFLQHK DDNPNLPPFQ RPEAEAMCTS FQENPTSFLG HYLHEVARRH PYFYAPELLY
YAEKYNEVLT QCCTESDKAA CLTPKLDAVK EKALVAAVRQ RMKCSSMQRF GERAFKAWAV
ARMSQRFPNA EFAEITKLAT DVTKINKECC HGDLLECADD RAELAKYMCE NQATISSKLQ
ACCDKPVLQK SQCLAEIEHD NIPADLPSIA ADFVEDKEVC KNYAEAKDVF LGTFLYEYSR
RHPDYSVSLL LRLAKKYEAT LEKCCAEGDP PACYGTVLAE FQPLVEEPKN LVKTNCELYE
KLGEYGFQNA VLVRYTQKAP QVSTPTLVEA ARNLGRVGTK CCTLPEAQRL PCVEDYLSAI
LNRLCVLHEK TPVSEKVTKC CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL
PDKEKQIKKQ TALAELVKHK PKATEDQLKT VMGDFAQFVD KCCKAADKDN CFATEGPNLV
ARSKEALA
