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Serum albumin

 ALBU_RABIT              Reviewed;         608 AA.
P49065;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
15-MAR-2017, entry version 105.
RecName: Full=Serum albumin;
Flags: Precursor;
Name=ALB;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=9129029;
Syed S., Schuyler P.D., Kulczycky M., Sheffield W.P.;
"Potent antithrombin activity and delayed clearance from the
circulation characterize recombinant hirudin genetically fused to
albumin.";
Blood 89:3243-3252(1997).
[2]
SEQUENCE REVISION TO 322-323 AND 506-507.
Sheffield W.P.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
-!- 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; U18344; AAB58347.2; -; mRNA.
RefSeq; NP_001075813.1; NM_001082344.1.
UniGene; Ocu.3074; -.
PDB; 3V09; X-ray; 2.27 A; A=25-608.
PDBsum; 3V09; -.
ProteinModelPortal; P49065; -.
SMR; P49065; -.
STRING; 9986.ENSOCUP00000014006; -.
ChEMBL; CHEMBL6104; -.
Allergome; 759; Ory c 6.
PRIDE; P49065; -.
GeneID; 100009195; -.
KEGG; ocu:100009195; -.
CTD; 213; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; P49065; -.
KO; K16141; -.
PRO; PR:P49065; -.
Proteomes; UP000001811; 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; 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_0000001077.
CHAIN 25 608 Serum albumin.
/FTId=PRO_0000001078.
DOMAIN 19 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 403 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 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 229 229 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
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 558 558 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 570 570 Phosphothreonine.
{ECO:0000250|UniProtKB:P02770}.
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}.
HELIX 30 54 {ECO:0000244|PDB:3V09}.
HELIX 60 79 {ECO:0000244|PDB:3V09}.
TURN 84 87 {ECO:0000244|PDB:3V09}.
HELIX 90 99 {ECO:0000244|PDB:3V09}.
TURN 105 107 {ECO:0000244|PDB:3V09}.
HELIX 110 114 {ECO:0000244|PDB:3V09}.
HELIX 121 128 {ECO:0000244|PDB:3V09}.
HELIX 144 153 {ECO:0000244|PDB:3V09}.
HELIX 155 169 {ECO:0000244|PDB:3V09}.
HELIX 175 192 {ECO:0000244|PDB:3V09}.
STRAND 195 197 {ECO:0000244|PDB:3V09}.
HELIX 198 230 {ECO:0000244|PDB:3V09}.
HELIX 232 246 {ECO:0000244|PDB:3V09}.
HELIX 252 270 {ECO:0000244|PDB:3V09}.
HELIX 274 290 {ECO:0000244|PDB:3V09}.
HELIX 292 294 {ECO:0000244|PDB:3V09}.
HELIX 297 301 {ECO:0000244|PDB:3V09}.
TURN 302 304 {ECO:0000244|PDB:3V09}.
HELIX 307 316 {ECO:0000244|PDB:3V09}.
HELIX 330 333 {ECO:0000244|PDB:3V09}.
HELIX 339 345 {ECO:0000244|PDB:3V09}.
HELIX 347 360 {ECO:0000244|PDB:3V09}.
HELIX 367 385 {ECO:0000244|PDB:3V09}.
STRAND 387 389 {ECO:0000244|PDB:3V09}.
HELIX 390 394 {ECO:0000244|PDB:3V09}.
TURN 395 398 {ECO:0000244|PDB:3V09}.
HELIX 399 401 {ECO:0000244|PDB:3V09}.
HELIX 402 438 {ECO:0000244|PDB:3V09}.
HELIX 444 461 {ECO:0000244|PDB:3V09}.
HELIX 466 490 {ECO:0000244|PDB:3V09}.
HELIX 495 503 {ECO:0000244|PDB:3V09}.
HELIX 508 513 {ECO:0000244|PDB:3V09}.
HELIX 528 530 {ECO:0000244|PDB:3V09}.
HELIX 536 539 {ECO:0000244|PDB:3V09}.
HELIX 542 559 {ECO:0000244|PDB:3V09}.
HELIX 565 582 {ECO:0000244|PDB:3V09}.
STRAND 585 587 {ECO:0000244|PDB:3V09}.
HELIX 588 606 {ECO:0000244|PDB:3V09}.
SEQUENCE 608 AA; 68910 MW; 9EECAFDA86B1EF09 CRC64;
MKWVTFISLL FLFSSAYSRG VFRREAHKSE IAHRFNDVGE EHFIGLVLIT FSQYLQKCPY
EEHAKLVKEV TDLAKACVAD ESAANCDKSL HDIFGDKICA LPSLRDTYGD VADCCEKKEP
ERNECFLHHK DDKPDLPPFA RPEADVLCKA FHDDEKAFFG HYLYEVARRH PYFYAPELLY
YAQKYKAILT ECCEAADKGA CLTPKLDALE GKSLISAAQE RLRCASIQKF GDRAYKAWAL
VRLSQRFPKA DFTDISKIVT DLTKVHKECC HGDLLECADD RADLAKYMCE HQETISSHLK
ECCDKPILEK AHCIYGLHND ETPAGLPAVA EEFVEDKDVC KNYEEAKDLF LGKFLYEYSR
RHPDYSVVLL LRLGKAYEAT LKKCCATDDP HACYAKVLDE FQPLVDEPKN LVKQNCELYE
QLGDYNFQNA LLVRYTKKVP QVSTPTLVEI SRSLGKVGSK CCKHPEAERL PCVEDYLSVV
LNRLCVLHEK TPVSEKVTKC CSESLVDRRP CFSALGPDET YVPKEFNAET FTFHADICTL
PETERKIKKQ TALVELVKHK PHATNDQLKT VVGEFTALLD KCCSAEDKEA CFAVEGPKLV
ESSKATLG


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