ALBU_LITCT
ID ALBU_LITCT Reviewed; 382 AA.
AC P21847;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Albumin;
DE Flags: Fragment;
GN Name=ALB;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tadpole liver;
RX PubMed=1704484; DOI=10.1210/mend-4-10-1556;
RA Averyhart-Fullard V., Jaffe R.C.;
RT "Cloning and thyroid hormone regulation of albumin mRNA in Rana catesbeiana
RT tadpole liver.";
RL Mol. Endocrinol. 4:1556-1563(1990).
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. {ECO:0000250|UniProtKB:P02768}.
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; M38195; AAA63473.1; -; mRNA.
DR PIR; A37253; A37253.
DR AlphaFoldDB; P21847; -.
DR SMR; P21847; -.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036094; F:small molecule binding; IPI:AgBase.
DR GO; GO:0070324; F:thyroid hormone binding; TAS:AgBase.
DR CDD; cd00015; ALBUMIN; 2.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR Pfam; PF00273; Serum_albumin; 2.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 2.
DR SUPFAM; SSF48552; SSF48552; 2.
DR PROSITE; PS00212; ALBUMIN_1; 2.
DR PROSITE; PS51438; ALBUMIN_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Lipid-binding; Metal-binding; Repeat; Secreted;
KW Zinc.
FT CHAIN <1..382
FT /note="Albumin"
FT /id="PRO_0000135615"
FT DOMAIN <1..178
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 179..377
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02768"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT DISULFID 2..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 47..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 67..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 80..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 116..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 160..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 192..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 237..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 261..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 276..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 314..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 358..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT NON_TER 1
SQ SEQUENCE 382 AA; 43920 MW; 1BD981FE808AEA37 CRC64;
KCRIIREFPD IVFKGLTLVQ VSQKFGKAGF EDVKKVTEEI VHLNEDCCKG DAVECMMERM
EATDHICEAK DKLSSKLADC CAKSILERTP CLLALPNDES DLSKELKNYY EDERVCENYK
KDKLLFLAHF THDYARSHQE SSPQSCLRVS KGFEGLLEKC CASENHAECL KQAPILLEAA
LKEIEELRKQ NCGALQLLGF RDYNIQLLFR YFFKMPQVTA PTLVELAGRM TKVAVYCCGL
AENKQQTCAE EKLDILLGEM CEKEKHTFVN DNVRHCCVDS YANRRKCFTD LQRYPNYVAP
KWDESKLHFN EDLCKGSEDD QIKKKLEVLV EYMKMKPDCG PEKLKEVVEA FRKIDIKCCA
AEDHQKCFDD EKAGLLQIIE AH