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Serum albumin (Fragment)

 ALBU_MACMU              Reviewed;         600 AA.
Q28522;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 108.
RecName: Full=Serum albumin;
Flags: Precursor; Fragment;
Name=ALB;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8460152; DOI=10.1073/pnas.90.6.2409;
Watkins S.A., Sakamoto Y., Madison J.M., Davis E.M., Smith D.G.,
Dwulet J., Putnam F.W.;
"cDNA and protein sequence of polymorphic macaque albumins that differ
in bilirubin binding.";
Proc. Natl. Acad. Sci. U.S.A. 90:2409-2413(1993).
-!- 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; M90463; AAA36906.1; -; mRNA.
PIR; A47391; A47391.
RefSeq; NP_001182578.1; NM_001195649.1.
UniGene; Mmu.2987; -.
ProteinModelPortal; Q28522; -.
SMR; Q28522; -.
STRING; 9544.ENSMMUP00000005100; -.
PRIDE; Q28522; -.
GeneID; 704892; -.
KEGG; mcc:704892; -.
CTD; 213; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; Q28522; -.
KO; K16141; -.
Proteomes; UP000006718; Unplaced.
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.
2: Evidence at transcript level;
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 10 {ECO:0000250|UniProtKB:P02770}.
PROPEP 11 16 {ECO:0000250|UniProtKB:P02770}.
/FTId=PRO_0000001069.
CHAIN 17 600 Serum albumin.
/FTId=PRO_0000001070.
DOMAIN 11 202 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 203 395 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 396 593 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 19 19 Copper. {ECO:0000250}.
METAL 83 83 Zinc. {ECO:0000250}.
METAL 115 115 Zinc. {ECO:0000250}.
METAL 263 263 Zinc. {ECO:0000250}.
METAL 265 265 Zinc. {ECO:0000250}.
BINDING 256 256 Bilirubin. {ECO:0000250}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 99 99 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 221 221 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 438 438 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 452 452 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 535 535 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 550 550 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 580 580 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
DISULFID 69 78 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 91 107 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 106 117 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 140 185 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 184 193 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 216 262 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 261 269 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 281 295 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 294 305 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 332 377 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 376 385 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 408 454 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 453 464 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 477 493 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 492 503 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 530 575 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 574 583 {ECO:0000255|PROSITE-ProRule:PRU00769}.
NON_TER 1 1
SEQUENCE 600 AA; 67881 MW; E45C871A670E740B CRC64;
LLFLFSSAYS RGVFRRDTHK SEVAHRFKDL GEEHFKGLVL VAFSQYLQQC PFEEHVKLVN
EVTEFAKTCV ADESAENCDK SLHTLFGDKL CTVATLRETY GEMADCCAKQ EPERNECFLQ
HKDDNPNLPP LVRPEVDVMC TAFHDNEATF LKKYLYEVAR RHPYFYAPEL LFFAARYKAA
FAECCQAADK AACLLPKLDE LRDEGKASSA KQRLKCASLQ KFGDRAFKAW AVARLSQKFP
KAEFAEVSKL VTDLTKVHTE CCHGDLLECA DDRADLAKYM CENQDSISSK LKECCDKPLL
EKSHCLAEVE NDEMPADLPS LAADYVESKD VCKNYAEAKD VFLGMFLYEY ARRHPDYSVM
LLLRLAKAYE ATLEKCCAAA DPHECYAKVF DEFQPLVEEP QNLVKQNCEL FEQLGEYKFQ
NALLVRYTKK VPQVSTPTLV EVSRNLGKVG AKCCKLPEAK RMPCAEDYLS VVLNRLCVLH
EKTPVSEKVT KCCTESLVNR RPCFSALELD EAYVPKAFNA ETFTFHADMC TLSEKEKQVK
KQTALVELVK HKPKATKEQL KGVMDNFAAF VEKCCKADDK EACFAEEGPK FVAASQAALA


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