ALBU_SHEEP
ID ALBU_SHEEP Reviewed; 607 AA.
AC P14639;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Albumin;
DE Flags: Precursor;
GN Name=ALB;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2602160; DOI=10.1093/nar/17.24.10495;
RA Brown W.M., Dziegielewska K.M., Foreman R.C., Saunders N.R.;
RT "Nucleotide and deduced amino acid sequence of sheep serum albumin.";
RL Nucleic Acids Res. 17:10495-10495(1989).
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-272
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; X17055; CAA34903.1; -; mRNA.
DR PIR; S06936; ABSHS.
DR RefSeq; NP_001009376.1; NM_001009376.1.
DR PDB; 4LUF; X-ray; 2.30 A; A=25-607.
DR PDB; 4LUH; X-ray; 2.20 A; A=25-607.
DR PDB; 5ORF; X-ray; 2.54 A; A/B/C/D=25-607.
DR PDB; 6HN0; X-ray; 2.12 A; A=25-607.
DR PDBsum; 4LUF; -.
DR PDBsum; 4LUH; -.
DR PDBsum; 5ORF; -.
DR PDBsum; 6HN0; -.
DR AlphaFoldDB; P14639; -.
DR SMR; P14639; -.
DR STRING; 9940.ENSOARP00000014782; -.
DR Allergome; 758; Ovi a 6.
DR PRIDE; P14639; -.
DR GeneID; 443393; -.
DR KEGG; oas:443393; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000002356; 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; 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_0000001081"
FT CHAIN 25..607
FT /note="Albumin"
FT /id="PRO_0000001082"
FT DOMAIN 19..209
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 210..402
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 403..600
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 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 272
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 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 282
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 228
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 459
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 557
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT MOD_RES 587
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 147..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 191..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 223..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 268..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 288..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 301..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 339..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 383..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 415..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 460..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 484..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 499..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 537..582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 581..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4LUH"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:6HN0"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:6HN0"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 197..229
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 251..269
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 366..385
FT /evidence="ECO:0007829|PDB:6HN0"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 402..437
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 443..460
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 465..489
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 494..502
FT /evidence="ECO:0007829|PDB:6HN0"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:5ORF"
FT HELIX 507..513
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 541..558
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 564..582
FT /evidence="ECO:0007829|PDB:6HN0"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6HN0"
FT HELIX 587..605
FT /evidence="ECO:0007829|PDB:6HN0"
SQ SEQUENCE 607 AA; 69188 MW; 84979A87F8B86596 CRC64;
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFNDLGE ENFQGLVLIA FSQYLQQCPF
DEHVKLVKEL TEFAKTCVAD ESHAGCDKSL HTLFGDELCK VATLRETYGD MADCCEKQEP
ERNECFLNHK DDSPDLPKLK PEPDTLCAEF KADEKKFWGK YLYEVARRHP YFYAPELLYY
ANKYNGVFQE CCQAEDKGAC LLPKIDAMRE KVLASSARQR LRCASIQKFG ERALKAWSVA
RLSQKFPKAD FTDVTKIVTD LTKVHKECCH GDLLECADDR ADLAKYICDH QDALSSKLKE
CCDKPVLEKS HCIAEVDKDA VPENLPPLTA DFAEDKEVCK NYQEAKDVFL GSFLYEYSRR
HPEYAVSVLL RLAKEYEATL EDCCAKEDPH ACYATVFDKL KHLVDEPQNL IKKNCELFEK
HGEYGFQNAL IVRYTRKAPQ VSTPTLVEIS RSLGKVGTKC CAKPESERMP CTEDYLSLIL
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSDLTLDETY VPKPFDEKFF TFHADICTLP
DTEKQIKKQT ALVELLKHKP KATDEQLKTV MENFVAFVDK CCAADDKEGC FVLEGPKLVA
STQAALA
