ID   G1U9S2_RABIT            Unreviewed;       608 AA.
AC   G1U9S2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Albumin {ECO:0000256|ARBA:ARBA00039343};
GN   Name=ALB {ECO:0000313|Ensembl:ENSOCUP00000014006.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000014006.2, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000014006.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000014006.2,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0007829|PDB:4F5V}
RP   X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 25-608, AND DISULFIDE BONDS.
RX   PubMed=22993082; DOI=10.1107/S0907444912027047;
RA   Bujacz A.;
RT   "Structures of bovine, equine and leporine serum albumin.";
RL   Acta Crystallogr. D 68:1278-1289(2012).
RN   [3] {ECO:0007829|PDB:4PO0}
RP   X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 25-608, AND DISULFIDE BONDS.
RX   PubMed=24753230; DOI=10.1002/prot.24583;
RA   Bujacz A., Zielinski K., Sekula B.;
RT   "Structural studies of bovine, equine, and leporine serum albumin complexes
RT   with naproxen.";
RL   Proteins 82:2199-2208(2014).
RN   [4] {ECO:0000313|Ensembl:ENSOCUP00000014006.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000014006.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; AAGW02023015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 4F5V; X-ray; 2.27 A; A=25-608.
DR   PDB; 4PO0; X-ray; 2.73 A; A=25-608.
DR   PDBsum; 4F5V; -.
DR   PDBsum; 4PO0; -.
DR   PDBsum; 6OCK; -.
DR   PDBsum; 6OCL; -.
DR   AlphaFoldDB; G1U9S2; -.
DR   SMR; G1U9S2; -.
DR   Allergome; 759; Ory c 6.
DR   Ensembl; ENSOCUT00000016292.4; ENSOCUP00000014006.2; ENSOCUG00000016287.4.
DR   GeneTree; ENSGT00390000000113; -.
DR   HOGENOM; CLU_030161_0_0_1; -.
DR   InParanoid; G1U9S2; -.
DR   OMA; ADPHACY; -.
DR   TreeFam; TF335561; -.
DR   Proteomes; UP000001811; Chromosome 15.
DR   Bgee; ENSOCUG00000016287; Expressed in liver and 14 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:1903981; F:enterobactin binding; IEA:Ensembl.
DR   GO; GO:0140272; F:exogenous protein binding; IEA:Ensembl.
DR   GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR   GO; GO:0015643; F:toxic substance binding; IEA:Ensembl.
DR   GO; GO:0072732; P:cellular response to calcium ion starvation; IEA:Ensembl.
DR   GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IEA:Ensembl.
DR   CDD; cd00015; ALBUMIN; 3.
DR   Gene3D; 1.10.246.10; -; 6.
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:SF15; ALBUMIN; 1.
DR   PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 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; Serum albumin-like; 3.
DR   PROSITE; PS00212; ALBUMIN_1; 2.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4F5V, ECO:0007829|PDB:4PO0};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR002520-1};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR002520-1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR002520-2};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR002520-1};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR002520-1}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..608
FT                   /note="Albumin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003424139"
FT   DOMAIN          19..211
FT                   /note="Albumin"
FT                   /evidence="ECO:0000259|PROSITE:PS51438"
FT   DOMAIN          212..403
FT                   /note="Albumin"
FT                   /evidence="ECO:0000259|PROSITE:PS51438"
FT   DOMAIN          404..601
FT                   /note="Albumin"
FT                   /evidence="ECO:0000259|PROSITE:PS51438"
FT   BINDING         27
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         264
FT                   /ligand="bilirubin IXalpha"
FT                   /ligand_id="ChEBI:CHEBI:57977"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-3"
FT   BINDING         268
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-1"
FT   DISULFID        77..86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        114..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        148..193
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        192..201
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        224..270
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        269..277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        289..303
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        302..313
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        340..385
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        384..393
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        416..462
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        461..472
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        485..501
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        500..511
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        538..583
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
FT   DISULFID        582..591
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002520-2,
FT                   ECO:0007829|PDB:4F5V"
SQ   SEQUENCE   608 AA;  68965 MW;  C24CA502C1801BCE CRC64;
     MKWVTFISLL FLFSSAYSRG VFRREAHKSE IAHRFNDVGE EHFIGLVLIT FSQYLQKCPY
     EEHAKLVKEV TDLAKACVAD ESAANCDKSL HDIFGDKICA LPSLRDTYGD VADCCEKKEP
     ERNECFLHHK DDKPDLPPFA RPEADVLCKA FHDDEKAFFG HYLYEVARRH PYFYAPELLY
     YAQKYKAILT ECCEAADKGA CLTPKLDALK EKALISAAQE RLRCASIQKF GDRAYKAWAL
     VRLSQRFPKA DFTDISKIVT DLTKVHKECC HGDLLECADD RADLAKYMCE HQETISSHLK
     ECCDKPILEK AHCIYGLHND ETPAGLPAVA EEFVEDKDVC KNYEEAKDLF LGKFLYEYSR
     RHPDYSVVLL LRLGKAYEAT LKKCCATDDP HACYAKVLDE FQPLVDEPKN LVKQNCELYE
     QLGDYNFQNA LLVRYTKKVP QVSTPTLVEI SRSLGKVGSK CCKHPEAERL PCVEDYLSVV
     LNRLCVLHEK TPVSEKVTKC CSESLVDRRP CFSALGPDET YVPKEFNAET FTFHADICTL
     PETERKIKKQ TALVELVKHK PHATNDQLKT VVGEFTALLD KCCSAEDKEA CFAVEGPKLV
     ESSKATLG
//