ALBU_MESAU
ID ALBU_MESAU Reviewed; 608 AA.
AC A6YF56;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Albumin {ECO:0000250|UniProtKB:P02768, ECO:0000312|EMBL:ABR68005.1};
DE Flags: Precursor;
GN Name=ALB {ECO:0000250|UniProtKB:P02768};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABR68005.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver {ECO:0000269|PubMed:17475267};
RX PubMed=17475267; DOI=10.1016/j.ijpara.2007.03.004;
RA DeMarco R., Mathieson W., Dillon G.P., Wilson R.A.;
RT "Schistosome albumin is of host, not parasite, origin.";
RL Int. J. Parasitol. 37:1201-1208(2007).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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, ECO:0000305}.
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 {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF488484; ABR68005.1; -; mRNA.
DR RefSeq; NP_001268578.1; NM_001281649.1.
DR AlphaFoldDB; A6YF56; -.
DR SMR; A6YF56; -.
DR PRIDE; A6YF56; -.
DR GeneID; 101837229; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 2.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Copper; Disulfide bond;
KW 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_0000394754"
FT CHAIN 25..608
FT /note="Albumin"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT /id="PRO_0000394755"
FT DOMAIN 19..211
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 212..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 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 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 543
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
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:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 99..115
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 114..125
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 148..193
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..201
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 224..270
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 269..277
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 289..303
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 302..313
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 340..385
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..472
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..583
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 582..591
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 608 AA; 68225 MW; E5EABB28E1C66E54 CRC64;
MKWVTFLLLL FVSDSAFSRG LFRRDAHKSE IAHRFKDLGE QHFKGLVLIA FSQFLQKCPY
EEHVKLVNEV TDFAKTCVAD ESAENCDKSL HTLFGDKLCA IPTLRDSYGE LADCCAKKEP
ERNECFLKHK DDHPNLPPFV RPDAEAMCTS FQENAVTFMG HYLHEVARRH PYFYAPELLY
YAEKYSAIMT ECCGEADKAA CITPKLDALK EKALASSVNQ RLKCSSLQRF GQRAFKAWAV
ARMSQKFPKA DFAEITKLAT DLTKLTEECC HGDLLECADD RAELAKYMCE NQASISSKLQ
ACCDKPVLKK SHCLSEVEND DLPADLPSLA ADFVEDKEVC KNYAEAKDVF LGTFLYEYAR
RHPDYSVALL LRLAKKYEAT LEKCCAEADP SACYGKVLDE FQPLVEEPKN LVKANCELFE
KLGEYGFQNA LIVRYTQKAP QVSTPTLVEA ARNLGKVGSK CCVLPEAQRL PCVEDYISAI
LNRVCVLHEK TPVSEQVTKC CTGSVVERRP CFSALPVDET YVPKEFKAET FTFHADICSL
PEKEKQMKKQ AALVELVKHK PKATGPQLRT VLGEFTAFLD KCCKAEDKEA CFSEDGPKLV
ASSQAALA
