ALBUA_XENLA
ID ALBUA_XENLA Reviewed; 606 AA.
AC P08759;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Albumin A;
DE AltName: Full=68 kDa serum albumin;
DE Flags: Precursor;
GN Name=alb-a;
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].
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 458-556.
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: 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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18350; AAA49636.1; -; mRNA.
DR PIR; A41682; ABXL68.
DR RefSeq; NP_001081244.1; NM_001087775.1.
DR AlphaFoldDB; P08759; -.
DR SMR; P08759; -.
DR IntAct; P08759; 1.
DR GeneID; 397731; -.
DR CTD; 397731; -.
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_0000001089"
FT CHAIN 25..606
FT /note="Albumin A"
FT /id="PRO_0000001090"
FT DOMAIN 22..211
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 212..401
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 402..599
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..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 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..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 382..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 414..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 459..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 483..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 498..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 536..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 580..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 606 AA; 70500 MW; F8E72AA952C3A3E8 CRC64;
MKWITLICLL ISSTLIESRI IFKRDTDVDH HKHIADMYNL LTERTFKGLT LAIVSQNLQK
CSLEELSKLV NEINDFAKSC TGNDKTPECE KPIGTLFYDK LCADPKVGVN YEWSKECCSK
QDPERAQCFR AHRVFEHNPV RPKPEETCAL FKEHPDDLLS AFIHEEARNH PDLYPPAVLL
LTQQYGKLVE HCCEEEDKDK CFAEKMKELM KHSHSIEDKQ KHFCWIVNNY PERVIKALNL
ARVSHRYPKP DFKLAHKFTE ETTHFIKDCC HGDMFECMTE RLELSEHTCQ HKDELSTKLE
KCCNLPLLER TYCIVTLEND DVPAELSKPI TEFTEDPHVC EKYAENKSFL EISPWQSQET
PELSEQFLLQ SAKEYESLLN KCCFSDNPPE CYKDGADRFM NEAKERFAYL KQNCDILHEH
GEYLFENELL IRYTKKMPQV SDETLIGIAH QMADIGEHCC AVPENQRMPC AEGDLTILIG
KMCERQKKTF INNHVAHCCT DSYSGMRSCF TALGPDEDYV PPPVTDDTFH FDDKICTAND
KEKQHIKQKF LVKLIKVSPK LEKNHIDEWL LEFLKMVQKC CTADEHQPCF DTEKPVLIEH
CQKLHP
