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Serum albumin

 ALBU_SHEEP              Reviewed;         607 AA.
P14639;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
16-JAN-2019, entry version 100.
RecName: Full=Serum albumin;
Flags: Precursor;
Name=ALB;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2602160; DOI=10.1093/nar/17.24.10495;
Brown W.M., Dziegielewska K.M., Foreman R.C., Saunders N.R.;
"Nucleotide and deduced amino acid sequence of sheep serum albumin.";
Nucleic Acids Res. 17:10495-10495(1989).
-!- 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}.
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EMBL; X17055; CAA34903.1; -; mRNA.
PIR; S06936; ABSHS.
RefSeq; NP_001009376.1; NM_001009376.1.
UniGene; Oar.449; -.
PDB; 4LUF; X-ray; 2.30 A; A=25-607.
PDB; 4LUH; X-ray; 2.20 A; A=25-607.
PDB; 5ORF; X-ray; 2.54 A; A/B/C/D=25-607.
PDBsum; 4LUF; -.
PDBsum; 4LUH; -.
PDBsum; 5ORF; -.
ProteinModelPortal; P14639; -.
SMR; P14639; -.
Allergome; 758; Ovi a 6.
PRIDE; P14639; -.
GeneID; 443393; -.
KEGG; oas:443393; -.
CTD; 213; -.
HOVERGEN; HBG004207; -.
KO; K16141; -.
OrthoDB; 906547at2759; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PR00803; AFETOPROTEIN.
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;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Copper; Disulfide bond; Lipid-binding; Metal-binding; Methylation;
Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000250|UniProtKB:P02770}.
/FTId=PRO_0000001081.
CHAIN 25 607 Serum albumin.
/FTId=PRO_0000001082.
DOMAIN 19 209 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 210 402 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 403 600 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 27 27 Copper. {ECO:0000250}.
METAL 91 91 Zinc. {ECO:0000250}.
METAL 123 123 Zinc. {ECO:0000250}.
METAL 270 270 Zinc. {ECO:0000250}.
METAL 272 272 Zinc. {ECO:0000250}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 107 107 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 228 228 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 443 443 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 445 445 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 459 459 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 557 557 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 569 569 Phosphothreonine.
{ECO:0000250|UniProtKB:P02770}.
MOD_RES 587 587 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 147 192 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 191 200 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 223 269 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 268 276 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 288 302 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 301 312 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 339 384 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 383 392 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 415 461 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 460 471 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 484 500 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 499 510 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 537 582 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 581 590 {ECO:0000255|PROSITE-ProRule:PRU00769}.
HELIX 26 28 {ECO:0000244|PDB:4LUH}.
HELIX 30 38 {ECO:0000244|PDB:4LUH}.
HELIX 40 54 {ECO:0000244|PDB:4LUH}.
HELIX 60 79 {ECO:0000244|PDB:4LUH}.
TURN 84 87 {ECO:0000244|PDB:4LUH}.
HELIX 90 99 {ECO:0000244|PDB:4LUH}.
HELIX 104 108 {ECO:0000244|PDB:4LUH}.
HELIX 109 116 {ECO:0000244|PDB:4LUH}.
HELIX 121 128 {ECO:0000244|PDB:4LUH}.
HELIX 143 152 {ECO:0000244|PDB:4LUH}.
HELIX 154 168 {ECO:0000244|PDB:4LUH}.
HELIX 174 183 {ECO:0000244|PDB:4LUH}.
HELIX 185 191 {ECO:0000244|PDB:4LUH}.
STRAND 194 196 {ECO:0000244|PDB:4LUH}.
HELIX 197 229 {ECO:0000244|PDB:4LUH}.
HELIX 231 245 {ECO:0000244|PDB:4LUH}.
HELIX 251 269 {ECO:0000244|PDB:4LUH}.
HELIX 273 289 {ECO:0000244|PDB:4LUH}.
HELIX 291 293 {ECO:0000244|PDB:4LUH}.
HELIX 296 300 {ECO:0000244|PDB:4LUH}.
TURN 301 303 {ECO:0000244|PDB:4LUH}.
HELIX 306 314 {ECO:0000244|PDB:4LUH}.
HELIX 329 332 {ECO:0000244|PDB:4LUH}.
HELIX 338 344 {ECO:0000244|PDB:4LUH}.
HELIX 346 360 {ECO:0000244|PDB:4LUH}.
HELIX 366 385 {ECO:0000244|PDB:4LUH}.
STRAND 386 388 {ECO:0000244|PDB:4LUH}.
HELIX 389 393 {ECO:0000244|PDB:4LUH}.
HELIX 396 437 {ECO:0000244|PDB:4LUH}.
HELIX 443 460 {ECO:0000244|PDB:4LUH}.
HELIX 465 489 {ECO:0000244|PDB:4LUH}.
HELIX 494 501 {ECO:0000244|PDB:4LUH}.
TURN 504 506 {ECO:0000244|PDB:5ORF}.
HELIX 507 513 {ECO:0000244|PDB:4LUH}.
HELIX 527 530 {ECO:0000244|PDB:4LUH}.
HELIX 534 538 {ECO:0000244|PDB:4LUH}.
HELIX 541 558 {ECO:0000244|PDB:4LUH}.
HELIX 564 583 {ECO:0000244|PDB:4LUH}.
STRAND 584 586 {ECO:0000244|PDB:4LUH}.
HELIX 587 606 {ECO:0000244|PDB:4LUH}.
SEQUENCE 607 AA; 69188 MW; 84979A87F8B86596 CRC64;
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFNDLGE ENFQGLVLIA FSQYLQQCPF
DEHVKLVKEL TEFAKTCVAD ESHAGCDKSL HTLFGDELCK VATLRETYGD MADCCEKQEP
ERNECFLNHK DDSPDLPKLK PEPDTLCAEF KADEKKFWGK YLYEVARRHP YFYAPELLYY
ANKYNGVFQE CCQAEDKGAC LLPKIDAMRE KVLASSARQR LRCASIQKFG ERALKAWSVA
RLSQKFPKAD FTDVTKIVTD LTKVHKECCH GDLLECADDR ADLAKYICDH QDALSSKLKE
CCDKPVLEKS HCIAEVDKDA VPENLPPLTA DFAEDKEVCK NYQEAKDVFL GSFLYEYSRR
HPEYAVSVLL RLAKEYEATL EDCCAKEDPH ACYATVFDKL KHLVDEPQNL IKKNCELFEK
HGEYGFQNAL IVRYTRKAPQ VSTPTLVEIS RSLGKVGTKC CAKPESERMP CTEDYLSLIL
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSDLTLDETY VPKPFDEKFF TFHADICTLP
DTEKQIKKQT ALVELLKHKP KATDEQLKTV MENFVAFVDK CCAADDKEGC FVLEGPKLVA
STQAALA


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[SGK3 CISK SGKL] Serine/threonine-protein kinase Sgk3 (EC 2.7.11.1) (Cytokine-independent survival kinase) (Serum/glucocorticoid-regulated kinase 3) (Serum/glucocorticoid-regulated kinase-like)
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Bibliography :
[30901161] Apelin peptides linked to anti-serum albumin domain antibodies retain affinity in vitro and are efficacious receptor agonists in vivo.
[30900908] Prognostic Significance of Low Body Mass Index and Betel-Quid Use in the 5-Year Survival Rates of Esophageal Squamous Cell Carcinoma Patients.
[30900856] [Preparation of novel phenyl boronic acid functionalized silica gel using triazo-cyanide click chemistry and its application in glycoprotein/glycopeptide selective enrichment].
[30900783] Recombinant expression, purification and characterization of acetylated LysargiNase from Escherichia coli with high activity and stability.
[30900390] d-Amino Acid Modification Protects N-Acetyl-seryl-aspartyl-lysyl-proline from Physiological Hydroxylation and Increases Its Antifibrotic Effects on Hepatic Fibrosis.
[30899814] Involvement of Quebracho tannins in dietĀ alters productive and reproductive efficiency of postpartum buffalo cows.
[30899809] Productive performance, egg quality, hematological parameters and serum chemistry of laying hens fed diets supplemented with certain fat-soluble vitamins, individually or combined, during summer season.
[30899532] Risk Factors for Unplanned Dialysis Initiation: A Systematic Review of the Literature.
[30897897] Portal pressure gradient and serum albumin: A simple combined parameter associated with the appearance of ascites in decompensated cirrhosis treated with transjugular intrahepatic portosystemic shunt.
[30897829] Assessing the Sensitizing and Allergenic Potential of the Albumin and Globulin Fractions from Amaranth () Grains before and after an Extrusion Process.
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