ALBUB_XENLA
ID ALBUB_XENLA Reviewed; 607 AA.
AC P14872;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Albumin B;
DE AltName: Full=74 kDa serum albumin;
DE Flags: Precursor;
GN Name=alb-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-607.
RX PubMed=2747653; DOI=10.1210/mend-3-3-464;
RA Moskaitis J.E., Sargent T.D., Smith L.H. Jr., Pastori R.L.,
RA Schoenberg D.R.;
RT "Xenopus laevis serum albumin: sequence of the complementary
RT deoxyribonucleic acids encoding the 68- and 74-kilodalton peptides and the
RT regulation of albumin gene expression by thyroid hormone during
RT development.";
RL Mol. Endocrinol. 3:464-473(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-48.
RX PubMed=2451026; DOI=10.1016/0022-2836(88)90380-4;
RA Schorpp M., Doebbeling U., Wagner U., Ryffel G.U.;
RT "5'-flanking and 5'-proximal exon regions of the two Xenopus albumin genes.
RT Deletion analysis of constitutive promoter function.";
RL J. Mol. Biol. 199:83-93(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 459-557.
RC TISSUE=Liver;
RX PubMed=3971963; DOI=10.1111/j.1432-1033.1985.tb08678.x;
RA Wolffe A.P., Glover J.F., Martin S.C., Tenniswood M.P.R., Williams J.L.,
RA Tata J.R.;
RT "Deinduction of transcription of Xenopus 74-kDa albumin genes and
RT destabilization of mRNA by estrogen in vivo and in hepatocyte cultures.";
RL Eur. J. Biochem. 146:489-496(1985).
CC -!- FUNCTION: Serum albumin, the main protein of plasma, has a good binding
CC capacity for 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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; M21442; AAA49637.1; -; mRNA.
DR EMBL; M28276; AAA49642.1; -; mRNA.
DR PIR; B41682; ABXL72.
DR AlphaFoldDB; P14872; -.
DR SMR; P14872; -.
DR IntAct; P14872; 1.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Copper; Disulfide bond; Lipid-binding;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000255"
FT /id="PRO_0000001091"
FT CHAIN 25..607
FT /note="Albumin B"
FT /id="PRO_0000001092"
FT DOMAIN 22..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 30
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT DISULFID 80..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 101..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 116..127
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 503
FT /note="S -> L (in Ref. 3; AAA49642)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="H -> D (in Ref. 3; AAA49642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 70382 MW; 592BA4177A36B66B CRC64;
MKWITLICLL ISSSFIESRI LFKRDTDADH HKHIADVYTA LTERTFKGLT LAIVSQNLQK
CSLEELSKLV NEINDFAKSC INDKTPECEK PVGTLFFDKL CADPAVGVNY EWSKECCAKQ
DPERAQCFKA HRDHEHTSIK PEPEETCKLL KEHPDDLLSA FIHEEARNHP DLYPPAVLAL
TKQYHKLAEH CCEEEDKEKC FSEKMKQLMK QSHSIEDKQH HFCWILDNFP EKVLKALNLA
RVSHRYPKAE FKLAHNFTEE VTHFIKDCCH DDMFECMTER LELTEHTCQH KDELSSKLEK
CCNIPLLERT YCIVTLENDD VPAELSQPIT EFTEDPHVCE KYAENNEVFL GRYLHAVSRK
HQELSEQFLL QSAKEYESLL NKCCKTDNPP ECYKDGADRF MNEAKERFAY LKQNCDILHE
HGEYLFENEL LIRYTKKMPQ VSDETLIGIA HQMADIGEHC CAVPENQRMP CAEGDLTILI
GKMCERQKKT FINNHVAHCC TDSYSGMRSC FTALGPDEDY VPPPVTDDTF HFDDKICTAN
DKEKQHIKQK FLVKLIKVSP KLEKNHIDEC SAEFLKMVQK CCTADEHQPC FDTEKPVLIE
HCQKLHP
