ALBU_RABIT
ID ALBU_RABIT Reviewed; 608 AA.
AC P49065;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Albumin;
DE Flags: Precursor;
GN Name=ALB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=9129029;
RA Syed S., Schuyler P.D., Kulczycky M., Sheffield W.P.;
RT "Potent antithrombin activity and delayed clearance from the circulation
RT characterize recombinant hirudin genetically fused to albumin.";
RL Blood 89:3243-3252(1997).
RN [2]
RP SEQUENCE REVISION TO 322-323 AND 506-507.
RA Sheffield W.P.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:3V09}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 25-608, AND DISULFIDE BONDS.
RX PubMed=22677715; DOI=10.1016/j.molimm.2012.05.011;
RA Majorek K.A., Porebski P.J., Dayal A., Zimmerman M.D., Jablonska K.,
RA Stewart A.J., Chruszcz M., Minor W.;
RT "Structural and immunologic characterization of bovine, horse, and rabbit
RT serum albumins.";
RL Mol. Immunol. 52:174-182(2012).
CC -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC bilirubin and drugs. Its main function is the regulation of the
CC colloidal osmotic pressure of blood. Major zinc transporter in plasma,
CC typically binds about 80% of all plasma zinc (By similarity). Major
CC calcium and magnesium transporter in plasma, binds approximately 45% of
CC circulating calcium and magnesium in plasma (By similarity).
CC Potentially has more than two calcium-binding sites and might
CC additionally bind calcium in a non-specific manner (By similarity). The
CC shared binding site between zinc and calcium at residue Asp-273
CC suggests a crosstalk between zinc and calcium transport in the blood
CC (By similarity). The rank order of affinity is zinc > calcium >
CC magnesium (By similarity). Binds to the bacterial siderophore
CC enterobactin and inhibits enterobactin-mediated iron uptake of E.coli
CC from ferric transferrin, and may thereby limit the utilization of iron
CC and growth of enteric bacteria such as E.coli (By similarity). Does not
CC prevent iron uptake by the bacterial siderophore aerobactin (By
CC similarity). {ECO:0000250|UniProtKB:P02768,
CC ECO:0000250|UniProtKB:P02769}.
CC -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB
CC homeostasis (By similarity). Interacts with TASOR (By similarity). In
CC plasma, occurs in a covalently-linked complex with chromophore-bound
CC alpha-1-microglobulin; this interaction does not prevent fatty acid
CC binding to ALB. {ECO:0000250|UniProtKB:P02768,
CC ECO:0000250|UniProtKB:P07724}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02768}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; U18344; AAB58347.2; -; mRNA.
DR RefSeq; NP_001075813.1; NM_001082344.1.
DR PDB; 3V09; X-ray; 2.27 A; A=25-608.
DR PDB; 6OCK; X-ray; 1.90 A; A=25-608.
DR PDB; 6OCL; X-ray; 2.35 A; A=25-608.
DR PDBsum; 3V09; -.
DR PDBsum; 6OCK; -.
DR PDBsum; 6OCL; -.
DR AlphaFoldDB; P49065; -.
DR SMR; P49065; -.
DR STRING; 9986.ENSOCUP00000014006; -.
DR ChEMBL; CHEMBL6104; -.
DR Allergome; 759; Ory c 6.
DR PRIDE; P49065; -.
DR GeneID; 100009195; -.
DR KEGG; ocu:100009195; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P49065; -.
DR OrthoDB; 906547at2759; -.
DR PRO; PR:P49065; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR CDD; cd00015; ALBUMIN; 3.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR Pfam; PF00273; Serum_albumin; 3.
DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR PRINTS; PR00803; AFETOPROTEIN.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 3.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues; Copper;
KW Disulfide bond; Lipid-binding; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT /id="PRO_0000001077"
FT CHAIN 25..608
FT /note="Albumin"
FT /id="PRO_0000001078"
FT DOMAIN 19..210
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 211..403
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 404..601
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 27
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 229
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 460
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 558
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT MOD_RES 588
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V09"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:6OCK"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 199..230
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 252..270
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3V09"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:6OCK"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 402..438
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 444..461
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 466..490
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 495..503
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6OCL"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 542..559
FT /evidence="ECO:0007829|PDB:6OCK"
FT HELIX 565..582
FT /evidence="ECO:0007829|PDB:6OCK"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:3V09"
FT HELIX 588..607
FT /evidence="ECO:0007829|PDB:6OCK"
SQ 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
