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ALBU_EQUAS
ID   ALBU_EQUAS              Reviewed;         607 AA.
AC   Q5XLE4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Albumin;
DE   Flags: Precursor;
GN   Name=ALB;
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Li H., Tang Y., Pingfan R.;
RT   "Full-length cDNA sequence of serum albumin of donkey (Equus asinus) and
RT   its structure analysis.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 31-41; 45-340; 344-565 AND 569-607.
RC   STRAIN=Ragusana; TISSUE=Milk;
RX   PubMed=17605147; DOI=10.1002/jms.1247;
RA   Cunsolo V., Saletti R., Muccilli V., Foti S.;
RT   "Characterization of the protein profile of donkey's milk whey fraction.";
RL   J. Mass Spectrom. 42:1162-1174(2007).
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; AY754333; AAV28861.1; -; mRNA.
DR   RefSeq; NP_001310707.1; NM_001323778.1.
DR   AlphaFoldDB; Q5XLE4; -.
DR   SMR; Q5XLE4; -.
DR   Allergome; 1494; Equ as 3.
DR   PRIDE; Q5XLE4; -.
DR   GeneID; 106835108; -.
DR   KEGG; eai:106835108; -.
DR   CTD; 213; -.
DR   OrthoDB; 906547at2759; -.
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   Calcium; Cleavage on pair of basic residues; Copper;
KW   Direct protein sequencing; Disulfide bond; Lipid-binding; Metal-binding;
KW   Methylation; Phosphoprotein; Repeat; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250|UniProtKB:P02770"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250|UniProtKB:P02770"
FT                   /id="PRO_0000001061"
FT   CHAIN           25..607
FT                   /note="Albumin"
FT                   /id="PRO_0000001062"
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         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         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   CONFLICT        521
FT                   /note="I -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   607 AA;  68539 MW;  7099E1E08E3C426A CRC64;
     MKWVTFVSLL FLFSSAYFRG VLRRDTHKSE IAHRFNDLGE KHFKGLVLVA FSQYLQQCPF
     EDHVKLVNEV TEFAKKCAAD ESAENCDKSL HTLFGDKLCT VATLRATYGE LADCCEKQEP
     ERNECFLTHK DDHPNLPKLK PEPDAQCAAF QEDPDKFLGK YLYEVARRHP YFYGPELLFH
     AEEYKADFTE CCPADDKAGC LIPKLDALKE RILLSSAKER LKCSSFQKFG ERAFKAWSVA
     RLSQKFPKAD FAEVSKIVTD LTKVHKECCH GDLLECADDR ADLTKYICEH QDSISGKLKA
     CCDKPLLQKS HCIAEVKEDD LPSDLPALAA DFAEDKEICK HYKDAKDVFL GTFLYEYSRR
     HPDYSVSLLL RIAKTYEATL EKCCAEADPP ACYATVFDQF TPLVEEPKSL VKKNCDLFEE
     VGEYDFQNAL IVRYTKKAPQ VSTPTLVEIG RTLGKVGSRC CKLPESERLP CSENHLALAL
     NRLCVLHEKT PVSEKITKCC TDSLAERRPC FSALELDEGY IPKEFKAETF TFHADICTLP
     EDEKQIKKQS ALAELVKHKP KATKEQLKTV LGNFSAFVAK CCGAEDKEAC FAEEGPKLVA
     SSQLALA
 
 
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