ID   ALBU_MOUSE              Reviewed;         608 AA.
AC   P07724; Q3TV03; Q61802; Q8C7C7; Q8C7H3; Q8CG74;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Albumin;
DE   Flags: Precursor;
GN   Name=Alb; Synonyms=Alb-1, Alb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
RC   STRAIN=129/SvEvTacfBr; TISSUE=Liver;
RA   Van Reeth T., Dreze P.L., Gabant P., Szpirer C., Szpirer J.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, Stomach, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-44.
RC   TISSUE=Liver;
RX   PubMed=1286668; DOI=10.1002/elps.11501301200;
RA   Giometti C.S., Taylor J., Tollaksen S.L.;
RT   "Mouse liver protein database: a catalog of proteins detected by two-
RT   dimensional gel electrophoresis.";
RL   Electrophoresis 13:970-991(1992).
RN   [5]
RP   PROTEIN SEQUENCE OF 35-57; 66-75; 89-105; 243-257; 299-309; 348-372;
RP   422-434; 439-452; 470-483; 509-524; 550-558 AND 570-602, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 99-516.
RX   PubMed=2452956; DOI=10.1093/oxfordjournals.molbev.a040350;
RA   Minghetti P.P., Law S.W., Dugaiczyk A.;
RT   "The rate of molecular evolution of alpha-fetoprotein approaches that of
RT   pseudogenes.";
RL   Mol. Biol. Evol. 2:347-358(1985).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-551.
RC   STRAIN=BALB/cJ;
RX   PubMed=1971802; DOI=10.1016/0378-1119(90)90030-u;
RA   Boccaccio C., Deschatrette J., Meunier-Rotival M.;
RT   "Empty and occupied insertion site of the truncated LINE-1 repeat located
RT   in the mouse serum albumin-encoding gene.";
RL   Gene 88:181-186(1990).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-443, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-229; LYS-460; LYS-543 AND
RP   LYS-588, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX   PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA   Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA   Prochazka J., Sedlacek R.;
RT   "Fam208a orchestrates interaction protein network essential for early
RT   embryonic development and cell division.";
RL   Exp. Cell Res. 382:111437-111437(2019).
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. Major zinc transporter in plasma,
CC       typically binds about 80% of all plasma zinc (By similarity). Major
CC       calcium and magnesium transporter in plasma, binds approximately 45% of
CC       circulating calcium and magnesium in plasma (By similarity).
CC       Potentially has more than two calcium-binding sites and might
CC       additionally bind calcium in a non-specific manner (By similarity). The
CC       shared binding site between zinc and calcium at residue Asp-273
CC       suggests a crosstalk between zinc and calcium transport in the blood
CC       (By similarity). The rank order of affinity is zinc > calcium >
CC       magnesium (By similarity). Binds to the bacterial siderophore
CC       enterobactin and inhibits enterobactin-mediated iron uptake of E.coli
CC       from ferric transferrin, and may thereby limit the utilization of iron
CC       and growth of enteric bacteria such as E.coli (By similarity). Does not
CC       prevent iron uptake by the bacterial siderophore aerobactin (By
CC       similarity). {ECO:0000250|UniProtKB:P02768,
CC       ECO:0000250|UniProtKB:P02769}.
CC   -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB
CC       homeostasis (By similarity). Interacts with TASOR (PubMed:31112734). In
CC       plasma, occurs in a covalently-linked complex with chromophore-bound
CC       alpha-1-microglobulin; this interaction does not prevent fatty acid
CC       binding to ALB. {ECO:0000250|UniProtKB:P02768,
CC       ECO:0000269|PubMed:31112734}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma. Expressed in the granular cells within the
CC       cerebellum (PubMed:31112734). {ECO:0000269|PubMed:31112734}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P02768}.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
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DR   EMBL; AJ011413; CAA09617.1; -; mRNA.
DR   EMBL; AJ277794; CAC81903.1; -; Genomic_DNA.
DR   EMBL; AK010025; BAB26650.1; -; mRNA.
DR   EMBL; AK050248; BAC34145.1; -; mRNA.
DR   EMBL; AK050644; BAC34360.1; -; mRNA.
DR   EMBL; AK160487; BAE35818.1; -; mRNA.
DR   EMBL; BC024643; AAH24643.1; -; mRNA.
DR   EMBL; BC049971; AAH49971.1; -; mRNA.
DR   EMBL; M16111; AAA37190.1; -; mRNA.
DR   EMBL; X13060; CAA31458.1; -; Genomic_DNA.
DR   CCDS; CCDS19412.1; -.
DR   PIR; A05139; A05139.
DR   RefSeq; NP_033784.2; NM_009654.4.
DR   AlphaFoldDB; P07724; -.
DR   SMR; P07724; -.
DR   BioGRID; 198060; 41.
DR   IntAct; P07724; 9.
DR   MINT; P07724; -.
DR   STRING; 10090.ENSMUSP00000031314; -.
DR   BindingDB; P07724; -.
DR   ChEMBL; CHEMBL1075271; -.
DR   Allergome; 755; Mus m 4.
DR   CarbonylDB; P07724; -.
DR   GlyGen; P07724; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P07724; -.
DR   PhosphoSitePlus; P07724; -.
DR   SwissPalm; P07724; -.
DR   REPRODUCTION-2DPAGE; IPI00131695; -.
DR   REPRODUCTION-2DPAGE; P07724; -.
DR   REPRODUCTION-2DPAGE; Q8CG74; -.
DR   CPTAC; non-CPTAC-3890; -.
DR   jPOST; P07724; -.
DR   PaxDb; 10090-ENSMUSP00000031314; -.
DR   PeptideAtlas; P07724; -.
DR   ProteomicsDB; 281964; -.
DR   ABCD; P07724; 88 sequenced antibodies.
DR   Antibodypedia; 3342; 3472 antibodies from 52 providers.
DR   DNASU; 11657; -.
DR   Ensembl; ENSMUST00000031314.10; ENSMUSP00000031314.9; ENSMUSG00000029368.11.
DR   GeneID; 11657; -.
DR   KEGG; mmu:11657; -.
DR   UCSC; uc008yaz.2; mouse.
DR   AGR; MGI:87991; -.
DR   CTD; 213; -.
DR   MGI; MGI:87991; Alb.
DR   VEuPathDB; HostDB:ENSMUSG00000029368; -.
DR   eggNOG; ENOG502R7EA; Eukaryota.
DR   GeneTree; ENSGT00390000000113; -.
DR   HOGENOM; CLU_030161_0_0_1; -.
DR   InParanoid; P07724; -.
DR   OMA; ADPHACY; -.
DR   OrthoDB; 5196468at2759; -.
DR   PhylomeDB; P07724; -.
DR   TreeFam; TF335561; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR   Reactome; R-MMU-189451; Heme biosynthesis.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-MMU-8964058; HDL remodeling.
DR   Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   Reactome; R-MMU-9757110; Prednisone ADME.
DR   Reactome; R-MMU-9793528; Ciprofloxacin ADME.
DR   SABIO-RK; P07724; -.
DR   BioGRID-ORCS; 11657; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Alb; mouse.
DR   PRO; PR:P07724; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P07724; Protein.
DR   Bgee; ENSMUSG00000029368; Expressed in gall bladder and 93 other cell types or tissues.
DR   ExpressionAtlas; P07724; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0140272; F:exogenous protein binding; ISO:MGI.
DR   GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0072341; F:modified amino acid binding; ISO:MGI.
DR   GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0072732; P:cellular response to calcium ion starvation; ISS:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR   GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; ISO:MGI.
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; PR00802; SERUMALBUMIN.
DR   SMART; SM00103; ALBUMIN; 3.
DR   SUPFAM; SSF48552; Serum albumin-like; 3.
DR   PROSITE; PS00212; ALBUMIN_1; 3.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
DR   SWISS-2DPAGE; P07724; -.
DR   UCD-2DPAGE; P07724; -.
DR   Genevisible; P07724; MM.
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   Methylation; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW   Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /id="PRO_0000001073"
FT   CHAIN           25..608
FT                   /note="Albumin"
FT                   /id="PRO_0000001074"
FT   DOMAIN          19..211
FT                   /note="Albumin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          212..403
FT                   /note="Albumin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          404..601
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         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         268
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02769"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         229
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         444
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         460
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         543
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         558
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         570
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02770"
FT   MOD_RES         588
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   DISULFID        77..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        114..125
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..385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        384..393
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        416..462
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        461..472
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        485..501
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        500..511
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        538..583
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        582..591
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   CONFLICT        27
FT                   /note="H -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="H -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="H -> N (in Ref. 2; BAC34360)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="Q -> I (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="P -> H (in Ref. 2; BAE35818)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="A -> T (in Ref. 2; BAC34145)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   608 AA;  68693 MW;  292F7C7EED3A61B4 CRC64;
     MKWVTFLLLL FVSGSAFSRG VFRREAHKSE IAHRYNDLGE QHFKGLVLIA FSQYLQKCSY
     DEHAKLVQEV TDFAKTCVAD ESAANCDKSL HTLFGDKLCA IPNLRENYGE LADCCTKQEP
     ERNECFLQHK DDNPSLPPFE RPEAEAMCTS FKENPTTFMG HYLHEVARRH PYFYAPELLY
     YAEQYNEILT QCCAEADKES CLTPKLDGVK EKALVSSVRQ RMKCSSMQKF GERAFKAWAV
     ARLSQTFPNA DFAEITKLAT DLTKVNKECC HGDLLECADD RAELAKYMCE NQATISSKLQ
     TCCDKPLLKK AHCLSEVEHD TMPADLPAIA ADFVEDQEVC KNYAEAKDVF LGTFLYEYSR
     RHPDYSVSLL LRLAKKYEAT LEKCCAEANP PACYGTVLAE FQPLVEEPKN LVKTNCDLYE
     KLGEYGFQNA ILVRYTQKAP QVSTPTLVEA ARNLGRVGTK CCTLPEDQRL PCVEDYLSAI
     LNRVCLLHEK TPVSEHVTKC CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL
     PEKEKQIKKQ TALAELVKHK PKATAEQLKT VMDDFAQFLD TCCKAADKDT CFSTEGPNLV
     TRCKDALA
//