ALBU_CHICK
ID ALBU_CHICK Reviewed; 615 AA.
AC P19121;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Albumin;
DE AltName: Full=Alpha-livetin;
DE AltName: Allergen=Gal d 5;
DE Flags: Precursor;
GN Name=ALB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Cassady A.I., Salklld C.K., Baverstock P., Wallace J.C.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=6187737; DOI=10.1016/s0021-9258(18)32659-0;
RA Hache R.J.G., Wiskocil R., Vasa M., Roy R.N., Lau P.C.K., Deeley R.G.;
RT "The 5' noncoding and flanking regions of the avian very low density
RT apolipoprotein II and serum albumin genes. Homologies with the egg white
RT protein genes.";
RL J. Biol. Chem. 258:4556-4564(1983).
RN [3]
RP PROTEIN SEQUENCE OF 19-30.
RX PubMed=911327; DOI=10.1016/0006-291x(77)90528-9;
RA Rosen A.M., Geller D.M.;
RT "Chicken microsomal albumin: amino terminal sequence of chicken
RT proalbumin.";
RL Biochem. Biophys. Res. Commun. 78:1060-1066(1977).
RN [4]
RP ALLERGEN.
RX PubMed=11488669; DOI=10.1034/j.1398-9995.2001.056008754.x;
RA Quirce S., Maranon F., Umpierrez A., de las Heras M., Fernandez-Caldas E.,
RA Sastre J.;
RT "Chicken serum albumin (Gal d 5*) is a partially heat-labile inhalant and
RT food allergen implicated in the bird-egg syndrome.";
RL Allergy 56:754-762(2001).
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. {ECO:0000250|UniProtKB:P02768}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- ALLERGEN: Can cause allergic reactions in humans. Binds to IgE.
CC Partially heat-labile allergen that may cause both respiratory and
CC food-allergy symptoms in patients with the bird-egg syndrome.
CC {ECO:0000269|PubMed:11488669}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; X60688; CAA43098.1; -; mRNA.
DR EMBL; V00381; CAA23680.1; -; Genomic_DNA.
DR PIR; S15571; ABCHS.
DR AlphaFoldDB; P19121; -.
DR SMR; P19121; -.
DR BioGRID; 676457; 1.
DR IntAct; P19121; 1.
DR STRING; 9031.ENSGALP00000019031; -.
DR Allergome; 3295; Gal d 5.0101.
DR Allergome; 363; Gal d 5.
DR PaxDb; P19121; -.
DR VEuPathDB; HostDB:geneid_396197; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P19121; -.
DR PhylomeDB; P19121; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0060417; C:yolk; IDA:AgBase.
DR GO; GO:0003677; F:DNA 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:0036094; F:small molecule binding; IPI:AgBase.
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 GO; GO:0009615; P:response to virus; IDA:AgBase.
DR GO; GO:0033189; P:response to vitamin A; IDA:AgBase.
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 Allergen; Calcium; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lipid-binding; Metal-binding; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:911327"
FT PROPEP 19..23
FT /id="PRO_0000001083"
FT CHAIN 24..615
FT /note="Albumin"
FT /id="PRO_0000001084"
FT DOMAIN 22..214
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 215..407
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 408..605
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 30
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
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 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 102..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 117..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 152..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 196..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 228..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 273..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 293..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 306..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 344..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 388..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 420..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 465..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 489..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 504..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 542..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 586..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 24
FT /note="F -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 69918 MW; E59E4BBCAEC066C6 CRC64;
MKWVTLISFI FLFSSATSRN LQRFARDAEH KSEIAHRYND LKEETFKAVA MITFAQYLQR
CSYEGLSKLV KDVVDLAQKC VANEDAPECS KPLPSIILDE ICQVEKLRDS YGAMADCCSK
ADPERNECFL SFKVSQPDFV QPYQRPASDV ICQEYQDNRV SFLGHFIYSV ARRHPFLYAP
AILSFAVDFE HALQSCCKES DVGACLDTKE IVMREKAKGV SVKQQYFCGI LKQFGDRVFQ
ARQLIYLSQK YPKAPFSEVS KFVHDSIGVH KECCEGDMVE CMDDMARMMS NLCSQQDVFS
GKIKDCCEKP IVERSQCIME AEFDEKPADL PSLVEKYIED KEVCKSFEAG HDAFMAEFVY
EYSRRHPEFS IQLIMRIAKG YESLLEKCCK TDNPAECYAN AQEQLNQHIK ETQDVVKTNC
DLLHDHGEAD FLKSILIRYT KKMPQVPTDL LLETGKKMTT IGTKCCQLGE DRRMACSEGY
LSIVIHDTCR KQETTPINDN VSQCCSQLYA NRRPCFTAMG VDTKYVPPPF NPDMFSFDEK
LCSAPAEERE VGQMKLLINL IKRKPQMTEE QIKTIADGFT AMVDKCCKQS DINTCFGEEG
ANLIVQSRAT LGIGA
