ALBU_CANLF
ID ALBU_CANLF Reviewed; 608 AA.
AC P49822; O77705; Q9TSZ4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Albumin;
DE AltName: Allergen=Can f 3;
DE Flags: Precursor;
GN Name=ALB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Liver;
RA Hilger C.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Liver;
RX PubMed=10669848; DOI=10.1016/s0091-6749(00)90077-0;
RA Pandjaitan B., Swoboda I., Brandejsky-Pichler F., Rumpold H., Valenta R.,
RA Spitzauer S.;
RT "Escherichia coli expression and purification of recombinant dog albumin, a
RT cross-reactive animal allergen.";
RL J. Allergy Clin. Immunol. 105:279-285(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Liver;
RA Miyake M., Okazaki M., Iwabuchi S.;
RT "Isolation of a cDNA encoding canine serum albumin.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 25-48.
RX PubMed=4414013; DOI=10.1016/s0021-9258(20)79899-6;
RA Dixon J.W., Sarkar B.;
RT "Isolation, amino acid sequence and copper(II)-binding properties of
RT peptide (1-24) of dog serum albumin.";
RL J. Biol. Chem. 249:5872-5877(1974).
RN [5]
RP PROTEIN SEQUENCE OF 25-38.
RC TISSUE=Heart;
RX PubMed=9504812; DOI=10.1002/elps.1150181514;
RA Dunn M.J., Corbett J.M., Wheeler C.H.;
RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT heart proteins.";
RL Electrophoresis 18:2795-2802(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 215-478, AND ALLERGEN.
RC TISSUE=Salivary gland;
RX PubMed=7512102; DOI=10.1016/s0091-6749(94)70073-7;
RA Spitzauer S., Schweiger C., Sperr W.R., Pandjaitan B., Valent P., Muehl S.,
RA Ebner C., Scheiner O., Kraft D., Rumpold H.;
RT "Molecular characterization of dog albumin as a cross-reactive allergen.";
RL J. Allergy Clin. Immunol. 93:614-627(1994).
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 {ECO:0000269|PubMed:10669848, ECO:0000269|PubMed:7512102}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC -!- CAUTION: Contains a tyrosine at position 27 instead of the conserved
CC histidine found in mammalian homologs that is involved in copper
CC binding. {ECO:0000250|UniProtKB:P02770}.
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DR EMBL; AJ133489; CAB64867.1; -; mRNA.
DR EMBL; Y17737; CAA76841.1; -; mRNA.
DR EMBL; AB090854; BAC10663.1; -; mRNA.
DR EMBL; S72946; AAB30434.1; -; mRNA.
DR PIR; S29749; S29749.
DR RefSeq; NP_001003026.1; NM_001003026.1.
DR PDB; 5GHK; X-ray; 3.20 A; A=25-608.
DR PDBsum; 5GHK; -.
DR AlphaFoldDB; P49822; -.
DR BMRB; P49822; -.
DR SMR; P49822; -.
DR STRING; 9612.ENSCAFP00000004489; -.
DR Allergome; 176; Can f 3.
DR Allergome; 3171; Can f 3.0101.
DR UCD-2DPAGE; P49822; -.
DR PaxDb; P49822; -.
DR PRIDE; P49822; -.
DR GeneID; 403550; -.
DR CTD; 213; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P49822; -.
DR Proteomes; UP000002254; 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; 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; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /id="PRO_0000001059"
FT CHAIN 25..608
FT /note="Albumin"
FT /id="PRO_0000001060"
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 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 1..26
FT /note="MKWVTFISLFFLFSSAYSRGLVRREA -> MDT (in Ref. 2;
FT CAA76841)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> R (in Ref. 2; CAA76841)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="I -> T (in Ref. 2; CAA76841)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> A (in Ref. 2; CAA76841)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="A -> S (in Ref. 2; CAA76841 and 6; AAB30434)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="V -> VV (in Ref. 6; AAB30434)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="E -> D (in Ref. 2; CAA76841 and 6; AAB30434)"
FT /evidence="ECO:0000305"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:5GHK"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 199..229
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:5GHK"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:5GHK"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:5GHK"
FT TURN 391..395
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 401..438
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:5GHK"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 469..490
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 495..503
FT /evidence="ECO:0007829|PDB:5GHK"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:5GHK"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 565..583
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:5GHK"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:5GHK"
SQ SEQUENCE 608 AA; 68605 MW; 3DB012FF7C979CF3 CRC64;
MKWVTFISLF FLFSSAYSRG LVRREAYKSE IAHRYNDLGE EHFRGLVLVA FSQYLQQCPF
EDHVKLAKEV TEFAKACAAE ESGANCDKSL HTLFGDKLCT VASLRDKYGD MADCCEKQEP
DRNECFLAHK DDNPGFPPLV APEPDALCAA FQDNEQLFLG KYLYEIARRH PYFYAPELLY
YAQQYKGVFA ECCQAADKAA CLGPKIEALR EKVLLSSAKE RFKCASLQKF GDRAFKAWSV
ARLSQRFPKA DFAEISKVVT DLTKVHKECC HGDLLECADD RADLAKYMCE NQDSISTKLK
ECCDKPVLEK SQCLAEVERD ELPGDLPSLA ADFVEDKEVC KNYQEAKDVF LGTFLYEYAR
RHPEYSVSLL LRLAKEYEAT LEKCCATDDP PTCYAKVLDE FKPLVDEPQN LVKTNCELFE
KLGEYGFQNA LLVRYTKKAP QVSTPTLVEV SRKLGKVGTK CCKKPESERM SCAEDFLSVV
LNRLCVLHEK TPVSERVTKC CSESLVNRRP CFSGLEVDET YVPKEFNAET FTFHADLCTL
PEAEKQVKKQ TALVELLKHK PKATDEQLKT VMGDFGAFVE KCCAAENKEG CFSEEGPKLV
AAAQAALV
