ALBU_FELCA
ID ALBU_FELCA Reviewed; 608 AA.
AC P49064; Q7YSG3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Albumin;
DE AltName: Allergen=Fel d 2;
DE Flags: Precursor;
GN Name=ALB;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8647469; DOI=10.1016/0378-1119(95)00851-9;
RA Hilger C., Grigioni F., Kohnen M., Hentges F.;
RT "Sequence of the gene encoding cat (Felis domesticus) serum albumin.";
RL Gene 169:295-296(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-608.
RC TISSUE=Liver;
RA Reininger R., Swoboda I., Bohle B., Hauswirth A.W., Valent P., Rumpold H.,
RA Valenta R., Spitzauer S.;
RT "Escherichia coli expression and purification of recombinant cat
RT albumin:IgE recognition, induction of basophil activation and
RT lymphoproliferative responses in atopic patients.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- ALLERGEN: Can cause allergic reactions in humans.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; X84842; CAA59279.1; -; mRNA.
DR EMBL; AJ487677; CAD32275.1; -; mRNA.
DR PIR; JC4660; S57632.
DR RefSeq; NP_001009961.1; NM_001009961.1.
DR PDB; 5YXE; X-ray; 3.40 A; A=25-608.
DR PDBsum; 5YXE; -.
DR AlphaFoldDB; P49064; -.
DR SMR; P49064; -.
DR STRING; 9685.ENSFCAP00000011000; -.
DR Allergome; 3279; Fel d 2.0101.
DR Allergome; 346; Fel d 2.
DR PRIDE; P49064; -.
DR GeneID; 448843; -.
DR KEGG; fca:448843; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P49064; -.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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; 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; Allergen; Calcium; Cleavage on pair of basic residues;
KW Copper; Disulfide bond; Lipid-binding; Metal-binding; Methylation;
KW Phosphoprotein; 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_0000001063"
FT CHAIN 25..608
FT /note="Albumin"
FT /id="PRO_0000001064"
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 229
FT /note="N6-succinyllysine"
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 DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 75
FT /note="K -> N (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> F (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="K -> R (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="E -> D (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> E (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="V -> A (in Ref. 2; CAD32275)"
FT /evidence="ECO:0000305"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:5YXE"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:5YXE"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 198..229
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 252..270
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:5YXE"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:5YXE"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 397..438
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:5YXE"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 469..488
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 535..539
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 542..559
FT /evidence="ECO:0007829|PDB:5YXE"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 567..583
FT /evidence="ECO:0007829|PDB:5YXE"
FT HELIX 591..605
FT /evidence="ECO:0007829|PDB:5YXE"
SQ SEQUENCE 608 AA; 68659 MW; 07E629CAC5F60E5F CRC64;
MKWVTFISLL LLFSSAYSRG VTRREAHQSE IAHRFNDLGE EHFRGLVLVA FSQYLQQCPF
EDHVKLVNEV TEFAKGCVAD QSAANCEKSL HELLGDKLCT VASLRDKYGE MADCCEKKEP
ERNECFLQHK DDNPGFGQLV TPEADAMCTA FHENEQRFLG KYLYEIARRH PYFYAPELLY
YAEEYKGVFT ECCEAADKAA CLTPKVDALR EKVLASSAKE RLKCASLQKF GERAFKAWSV
ARLSQKFPKA EFAEISKLVT DLAKIHKECC HGDLLECADD RADLAKYICE NQDSISTKLK
ECCGKPVLEK SHCISEVERD ELPADLPPLA VDFVEDKEVC KNYQEAKDVF LGTFLYEYSR
RHPEYSVSLL LRLAKEYEAT LEKCCATDDP PACYAHVFDE FKPLVEEPHN LVKTNCELFE
KLGEYGFQNA LLVRYTKKVP QVSTPTLVEV SRSLGKVGSK CCTHPEAERL SCAEDYLSVV
LNRLCVLHEK TPVSERVTKC CTESLVNRRP CFSALQVDET YVPKEFSAET FTFHADLCTL
PEAEKQIKKQ SALVELLKHK PKATEEQLKT VMGDFGSFVD KCCAAEDKEA CFAEEGPKLV
AAAQAALA
