ALBU_MERUN
ID ALBU_MERUN Reviewed; 609 AA.
AC O35090;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Albumin;
DE Flags: Precursor;
GN Name=ALB;
OS Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MGS IDR; TISSUE=Liver;
RX PubMed=9455485; DOI=10.1093/dnares/4.5.351;
RA Yoshida K., Seto-Ohshima A., Sinohara H.;
RT "Sequencing of cDNA encoding serum albumin and its extrahepatic synthesis
RT in the Mongolian gerbil, Meriones unguiculatus.";
RL DNA Res. 4:351-354(1997).
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-274
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; AB006197; BAA21765.1; -; mRNA.
DR PIR; JC5838; JC5838.
DR AlphaFoldDB; O35090; -.
DR SMR; O35090; -.
DR PRIDE; O35090; -.
DR OrthoDB; 906547at2759; -.
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 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Copper; Disulfide bond;
KW Lipid-binding; Metal-binding; Methylation; Phosphoprotein; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT /id="PRO_0000001071"
FT CHAIN 25..609
FT /note="Albumin"
FT /id="PRO_0000001072"
FT DOMAIN 20..212
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 213..404
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 405..602
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT MOD_RES 30
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 544
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 559
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 589
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT DISULFID 78..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 100..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 115..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 149..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 193..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 225..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 270..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 290..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 341..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 385..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 417..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 462..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 486..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 501..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 539..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 583..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 609 AA; 68941 MW; 9CA5F97F67EF1A48 CRC64;
MKWVTFLLLL FVSGSAFSRG VFRRDAAHKS EIAHRYKDLG EKYFKGLVLY TFSQYLQKCS
YEEHVKLVRE VTDFASNCAK DESAENCDKS LHTLFGDKLC SLPNFGEKYA EMADCCAKQE
PERNECFLQH KDDNPQLPPF KRAEPDAMCT AFQENAEAFM GHYLHEVARR HPYFYGPELL
YLADKYTAVL TECCAADDKG ACLTPKLDAL KEKALVSAVR QRLKCSSMKK FGERAFKAWA
VARMSQTFPN ADFAEITKLA TDLTKVTQEC CHGDLLECAD DRAELAKYMC ENQASISSKL
QACCDKEMLQ KSQCLAEVEH DDMPADLPAL TADFVEDKDV CKNYAEAKDV FLGTFLYEYS
RRHPEYSVSL LLRLAKKYEA TLEKCCAEAD PHACYGHVFD EFKPLVEEPQ NLVKSNCELY
EKLGEYGFQN AVLVRYTKKA PQVSTPTLVE AARSLGRVGT HCCALPEKKR LPCVEDYLSA
ILNRVCLLHE KTPVSEQVTK CCSGSLVERR PCFSALPVDE TYVPKEFKAE TFTFHANICT
LPEKEKQMEK QTALAELVKH KPQATEEQLK KVMGDFAEFL EKCCKQEDKE ACFSTEGPKL
VAESQKALA
