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Serum albumin

 ALBU_RAT                Reviewed;         608 AA.
P02770; P11382; Q5U3X3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 160.
RecName: Full=Serum albumin;
Flags: Precursor;
Name=Alb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7017712; DOI=10.1073/pnas.78.1.243;
Sargent T.D., Yang M., Bonner J.;
"Nucleotide sequence of cloned rat serum albumin messenger RNA.";
Proc. Natl. Acad. Sci. U.S.A. 78:243-246(1981).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-262.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 1-38, PROTEOLYTIC PROCESSING, AND IDENTIFICATION
OF PROPEPTIDE CLEAVAGE SITE.
PubMed=893447;
Strauss A.W., Bennett C.D., Donohue A.M., Rodkey J.A., Alberts A.W.;
"Rat liver pre-proalbumin: complete amino acid sequence of the pre-
piece. Analysis of the direct translation product of albumin messenger
RNA.";
J. Biol. Chem. 252:6846-6855(1977).
[4]
PROTEIN SEQUENCE OF 19-27 AND 606-608.
TISSUE=Liver;
PubMed=7358734;
Peters T. Jr., Reed R.G.;
"The biosynthesis of rat serum albumin. Composition and properties of
the intracellular precursor, proalbumin.";
J. Biol. Chem. 255:3156-3163(1980).
[5]
PROTEIN SEQUENCE OF 25-222.
PubMed=564345;
Isemura S., Ikenaka T.;
"Amino acid sequences of fragments I and II obtained by cyanogen
bromide cleavage of rat serum albumin.";
J. Biochem. 83:35-48(1978).
[6]
PROTEIN SEQUENCE OF 166-174.
TISSUE=Plasma;
PubMed=2437111;
Carraway R.E., Mitra S.P., Cochrane D.E.;
"Structure of a biologically active neurotensin-related peptide
obtained from pepsin-treated albumin(s).";
J. Biol. Chem. 262:5968-5973(1987).
[7]
PROTEIN SEQUENCE OF 35-57; 66-75; 89-97; 168-181; 247-264; 287-298;
361-372; 376-383; 414-434; 439-452; 470-483; 509-524; 528-545; 570-581
AND 585-602, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 223-288 AND 572-608.
PubMed=956149;
Isemura S., Ikenaka T.;
"Fragmentation of rat serum albumin by cyanogen bromide cleavage and
the amino acid sequences of four fragments.";
J. Biochem. 79:1183-1196(1976).
[9]
COPPER-BINDING.
PubMed=80265;
Aoyagi Y., Ikenaka T., Ichida F.;
"Copper(II)-binding ability of human alpha-fetoprotein.";
Cancer Res. 38:3483-3486(1978).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND THR-570, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Serum albumin, the main protein of plasma, has a good
binding capacity for water, Ca(2+), Na(+), K(+), fatty acids,
hormones, bilirubin and drugs. Its main function is the regulation
of the colloidal osmotic pressure of blood. Major zinc transporter
in plasma, typically binds about 80% of all plasma zinc.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02768}.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
-!- CAUTION: A peptide arising from positions 166 to 174 was
originally termed neurotensin-related peptide (NRP) and was
thought to regulate fat digestion, lipid absorption, and blood
flow. {ECO:0000305|PubMed:2437111}.
-----------------------------------------------------------------------
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EMBL; V01222; CAA24532.1; -; mRNA.
EMBL; BC085359; AAH85359.1; -; mRNA.
PIR; A93872; ABRTS.
RefSeq; NP_599153.2; NM_134326.2.
UniGene; Rn.202968; -.
UniGene; Rn.49051; -.
ProteinModelPortal; P02770; -.
SMR; P02770; -.
CORUM; P02770; -.
IntAct; P02770; 2.
MINT; MINT-4542462; -.
STRING; 10116.ENSRNOP00000003921; -.
BindingDB; P02770; -.
ChEMBL; CHEMBL4817; -.
Allergome; 756; Rat n 4.
iPTMnet; P02770; -.
PhosphoSitePlus; P02770; -.
SwissPalm; P02770; -.
UCD-2DPAGE; P02770; -.
World-2DPAGE; 0004:P02770; -.
PaxDb; P02770; -.
PRIDE; P02770; -.
GeneID; 24186; -.
KEGG; rno:24186; -.
UCSC; RGD:2085; rat.
CTD; 213; -.
RGD; 2085; Alb.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; P02770; -.
KO; K16141; -.
PhylomeDB; P02770; -.
TreeFam; TF335561; -.
PRO; PR:P02770; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; IPI:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0005504; F:fatty acid binding; IDA:RGD.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:UniProtKB.
GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IDA:RGD.
GO; GO:0046689; P:response to mercury ion; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0070541; P:response to platinum ion; IEP:RGD.
GO; GO:0006810; P:transport; IEA:InterPro.
GO; GO:0042311; P:vasodilation; NAS:RGD.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 3.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Lipid-binding;
Metal-binding; Methylation; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 18 {ECO:0000269|PubMed:893447}.
PROPEP 19 24 {ECO:0000269|PubMed:893447}.
/FTId=PRO_0000001079.
CHAIN 25 608 Serum albumin.
/FTId=PRO_0000001080.
DOMAIN 19 211 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 212 403 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 404 601 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 27 27 Copper.
METAL 91 91 Zinc. {ECO:0000250}.
METAL 123 123 Zinc. {ECO:0000250}.
METAL 271 271 Zinc. {ECO:0000250}.
METAL 273 273 Zinc. {ECO:0000250}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 460 460 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 543 543 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 558 558 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 570 570 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 588 588 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 99 115 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 114 125 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 148 193 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 192 201 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 224 270 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 269 277 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 289 303 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 340 385 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 416 462 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 461 472 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 485 501 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 500 511 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 538 583 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 582 591 {ECO:0000255|PROSITE-ProRule:PRU00769}.
VARIANT 262 262 V -> L. {ECO:0000269|PubMed:15489334}.
CONFLICT 174 174 Y -> L (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 317 317 I -> T (in Ref. 1; CAA24532).
{ECO:0000305}.
CONFLICT 431 431 V -> I (in Ref. 2; AAH85359).
{ECO:0000305}.
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


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