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Serum albumin

 ALBU_EQUAS              Reviewed;         607 AA.
Q5XLE4;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
10-MAY-2017, entry version 58.
RecName: Full=Serum albumin;
Flags: Precursor;
Name=ALB;
Equus asinus (Donkey) (Equus africanus asinus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9793;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Li H., Tang Y., Pingfan R.;
"Full-length cDNA sequence of serum albumin of donkey (Equus asinus)
and its structure analysis.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 31-41; 45-340; 344-565 AND 569-607.
STRAIN=Ragusana; TISSUE=Milk;
PubMed=17605147; DOI=10.1002/jms.1247;
Cunsolo V., Saletti R., Muccilli V., Foti S.;
"Characterization of the protein profile of donkey's milk whey
fraction.";
J. Mass Spectrom. 42:1162-1174(2007).
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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; AY754333; AAV28861.1; -; mRNA.
RefSeq; NP_001310707.1; NM_001323778.1.
ProteinModelPortal; Q5XLE4; -.
SMR; Q5XLE4; -.
Allergome; 1494; Equ as 6.
PRIDE; Q5XLE4; -.
GeneID; 106835108; -.
KEGG; eai:106835108; -.
CTD; 213; -.
HOVERGEN; HBG004207; -.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
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:0006810; P:transport; IEA:InterPro.
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; Copper; Direct protein sequencing;
Disulfide bond; Lipid-binding; Metal-binding; Methylation;
Phosphoprotein; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 18 {ECO:0000250|UniProtKB:P02770}.
PROPEP 19 24 {ECO:0000250|UniProtKB:P02770}.
/FTId=PRO_0000001061.
CHAIN 25 607 Serum albumin.
/FTId=PRO_0000001062.
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 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 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}.
CONFLICT 521 521 I -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 607 AA; 68539 MW; 7099E1E08E3C426A CRC64;
MKWVTFVSLL FLFSSAYFRG VLRRDTHKSE IAHRFNDLGE KHFKGLVLVA FSQYLQQCPF
EDHVKLVNEV TEFAKKCAAD ESAENCDKSL HTLFGDKLCT VATLRATYGE LADCCEKQEP
ERNECFLTHK DDHPNLPKLK PEPDAQCAAF QEDPDKFLGK YLYEVARRHP YFYGPELLFH
AEEYKADFTE CCPADDKAGC LIPKLDALKE RILLSSAKER LKCSSFQKFG ERAFKAWSVA
RLSQKFPKAD FAEVSKIVTD LTKVHKECCH GDLLECADDR ADLTKYICEH QDSISGKLKA
CCDKPLLQKS HCIAEVKEDD LPSDLPALAA DFAEDKEICK HYKDAKDVFL GTFLYEYSRR
HPDYSVSLLL RIAKTYEATL EKCCAEADPP ACYATVFDQF TPLVEEPKSL VKKNCDLFEE
VGEYDFQNAL IVRYTKKAPQ VSTPTLVEIG RTLGKVGSRC CKLPESERLP CSENHLALAL
NRLCVLHEKT PVSEKITKCC TDSLAERRPC FSALELDEGY IPKEFKAETF TFHADICTLP
EDEKQIKKQS ALAELVKHKP KATKEQLKTV LGNFSAFVAK CCGAEDKEAC FAEEGPKLVA
SSQLALA


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