ALBU_BOMMX
ID ALBU_BOMMX Reviewed; 607 AA.
AC Q3T478; Q3T479;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Serum albumin {ECO:0000250|UniProtKB:P02768};
DE AltName: Full=BmA-serum {ECO:0000303|PubMed:16081656};
DE AltName: Full=BmA-skin {ECO:0000303|PubMed:16081656};
DE Flags: Precursor;
OS Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Bombinatoridae; Bombina.
OX NCBI_TaxID=161274;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAX82486.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000269|PubMed:16081656},
RC Serum {ECO:0000312|EMBL:AAX82486.1}, and
RC Skin {ECO:0000312|EMBL:AAX82485.1};
RX PubMed=16081656; DOI=10.1110/ps.051551105;
RA Zhang Y.X., Lai R., Lee W.H., Zhang Y.;
RT "Frog albumin is expressed in skin and characterized as a novel potent
RT trypsin inhibitor.";
RL Protein Sci. 14:2469-2477(2005).
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 (By similarity). Potent inhibitor
CC of trypsin but has no inhibitory effect on thrombin, chymotrypsin,
CC elastase and subtilisin. {ECO:0000250|UniProtKB:P02768,
CC ECO:0000269|PubMed:16081656}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00769,
CC ECO:0000269|PubMed:16081656}.
CC -!- TISSUE SPECIFICITY: Plasma. In the skin, widely distributed around the
CC membranes of epithelial layer cells and within the stratum spongiosum
CC of the dermis (at protein level). {ECO:0000269|PubMed:16081656,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; AY885649; AAX82485.1; -; mRNA.
DR EMBL; AY885650; AAX82486.1; -; mRNA.
DR AlphaFoldDB; Q3T478; -.
DR SMR; Q3T478; -.
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 GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; 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; PR00803; AFETOPROTEIN.
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 Protease inhibitor; Repeat; Secreted; Serine protease inhibitor; Signal;
KW Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..20
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16081656"
FT /id="PRO_0000423001"
FT CHAIN 23..607
FT /note="Serum albumin"
FT /evidence="ECO:0000269|PubMed:16081656"
FT /id="PRO_0000423002"
FT DOMAIN 19..209
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 210..401
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 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 DISULFID 77..86
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 99..115
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 114..125
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 147..192
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 191..200
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 223..269
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 268..276
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 288..302
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 301..312
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 339..384
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 383..392
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 415..461
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 460..471
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 484..500
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 499..510
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 537..582
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 581..590
FT /evidence="ECO:0000250|UniProtKB:P02768,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 494
FT /note="E -> G (in Ref. 1; AAX82485)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="N -> S (in Ref. 1; AAX82485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 69554 MW; 9596EA2137A049A7 CRC64;
MKWTILTALL IISAESKNLY KRDSEPHIRF LGEVYKKVDT IDFRGLVLIT LAQHLQKCPF
EELAKQVEQI TTLAQACAAG ARHADCATPL ITLFLNRICA VPELSATYDW STECCAKSDP
ERHQCFRAHR NPAPGTHYKR PEPEELCESY KKNKEDVLAH YIYEVSRGHP VLYSPAVLGF
AYQFNGICSH CCEEEDKTTC FKDRMTQLKK ALHIVEVQQK ESCRILDNFG VRVLQALKLV
KISKKNPKAT FEVAQKLTSE VTHLNEDCCH GDMLECMIER MELTEHTCEH HEDISTKLKT
CCEKPLIERT HCIVNLENDD IPEDLPKKVT KFVEDPEVCK LFADKKDIFL AEFLYEYGRR
HPELSDQLLL RIAKGYEHQL EKCCELENFL ECLKDGEHVL ADAIKESTEL TEKDCAIQQK
LGDYLFQNVL LIRYTKKMPH VTTPSLIHIT KHMTEVGDKC CALPNTQKMP CAEGGLSLII
GEFCEMEKTH PINEHVKNCC WKSYSNRRNC FTNLGPDDSY VAPEITDDTF HFTEDLCTLP
EEELKNKKQG FIATLVKVKP HVTDELYGQI AVEFTKMREK CCAAEDHQAC FNAEEPILIE
HCKQLAA
