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Serum albumin (allergen Fel d 2)

 ALBU_FELCA              Reviewed;         608 AA.
P49064; Q7YSG3;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
15-MAR-2017, entry version 99.
RecName: Full=Serum albumin;
AltName: Allergen=Fel d 2;
Flags: Precursor;
Name=ALB;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8647469; DOI=10.1016/0378-1119(95)00851-9;
Hilger C., Grigioni F., Kohnen M., Hentges F.;
"Sequence of the gene encoding cat (Felis domesticus) serum albumin.";
Gene 169:295-296(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-608.
TISSUE=Liver;
Reininger R., Swoboda I., Bohle B., Hauswirth A.W., Valent P.,
Rumpold H., Valenta R., Spitzauer S.;
"Escherichia coli expression and purification of recombinant cat
albumin:IgE recognition, induction of basophil activation and
lymphoproliferative responses in atopic patients.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Serum albumin, the main protein of plasma, has a good
binding capacity for water, Ca(2+), Na(+), K(+), fatty acids,
hormones, bilirubin and drugs. Its main function is the regulation
of the colloidal osmotic pressure of blood. Major zinc transporter
in plasma, typically binds about 80% of all plasma zinc.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02768}.
-!- ALLERGEN: Causes an allergic reaction in human.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
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EMBL; X84842; CAA59279.1; -; mRNA.
EMBL; AJ487677; CAD32275.1; -; mRNA.
PIR; JC4660; S57632.
RefSeq; NP_001009961.1; NM_001009961.1.
ProteinModelPortal; P49064; -.
SMR; P49064; -.
STRING; 9685.ENSFCAP00000011000; -.
Allergome; 3279; Fel d 2.0101.
Allergome; 346; Fel d 2.
PRIDE; P49064; -.
GeneID; 448843; -.
KEGG; fca:448843; -.
CTD; 213; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
HOVERGEN; HBG004207; -.
InParanoid; P49064; -.
KO; K16141; -.
Proteomes; UP000011712; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:UniProtKB.
GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0006810; P:transport; IEA:InterPro.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 3.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
Allergen; Cleavage on pair of basic residues; Complete proteome;
Copper; Disulfide bond; Lipid-binding; Metal-binding; Methylation;
Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000250|UniProtKB:P02770}.
/FTId=PRO_0000001063.
CHAIN 25 608 Serum albumin.
/FTId=PRO_0000001064.
DOMAIN 19 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 403 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 404 601 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 27 27 Copper.
METAL 91 91 Zinc. {ECO:0000250}.
METAL 123 123 Zinc. {ECO:0000250}.
METAL 271 271 Zinc. {ECO:0000250}.
METAL 273 273 Zinc. {ECO:0000250}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 229 229 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 460 460 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 558 558 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 570 570 Phosphothreonine.
{ECO:0000250|UniProtKB:P02770}.
MOD_RES 588 588 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 99 115 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 114 125 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 148 193 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 192 201 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 224 270 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 269 277 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 289 303 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 340 385 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 416 462 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 461 472 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 485 501 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 500 511 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 538 583 {ECO:0000255|PROSITE-ProRule:PRU00769}.
DISULFID 582 591 {ECO:0000255|PROSITE-ProRule:PRU00769}.
CONFLICT 75 75 K -> N (in Ref. 2; CAD32275).
{ECO:0000305}.
CONFLICT 94 94 L -> F (in Ref. 2; CAD32275).
{ECO:0000305}.
CONFLICT 186 186 K -> R (in Ref. 2; CAD32275).
{ECO:0000305}.
CONFLICT 251 251 E -> D (in Ref. 2; CAD32275).
{ECO:0000305}.
CONFLICT 282 282 A -> E (in Ref. 2; CAD32275).
{ECO:0000305}.
CONFLICT 331 331 V -> A (in Ref. 2; CAD32275).
{ECO:0000305}.
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


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