HBB1_DANRE
ID HBB1_DANRE Reviewed; 148 AA.
AC Q90486; Q0P4G3; Q3B7Q0; Q90488;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Beta-A1-globin;
DE AltName: Full=Hemoglobin beta-1 chain;
GN Name=ba1; ORFNames=si:by187g17.2, zgc:123164;
GN and
GN Name=ba1l; ORFNames=si:by187g17.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB05403.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (BA1), PARTIAL PROTEIN SEQUENCE,
RP AND MASS SPECTROMETRY.
RC TISSUE=Kidney {ECO:0000269|PubMed:9002973};
RX PubMed=9002973;
RA Chan F.-Y., Robinson J., Brownlie A., Shivdasani R.A., Donovan A.,
RA Brugnara C., Kim J., Lau B.-C., Witkowska H.E., Zon L.I.;
RT "Characterization of adult alpha- and beta-globin genes in the zebrafish.";
RL Blood 89:688-700(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (BA1 AND BA1L).
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAE48983.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (BA1 AND BA1L).
RC STRAIN=AB; TISSUE=Gill, and Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=16257.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9002973};
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; U50380; AAB05403.1; -; mRNA.
DR EMBL; U50382; AAB05405.1; -; Genomic_DNA.
DR EMBL; AL929176; CAE48983.1; -; Genomic_DNA.
DR EMBL; AL929176; CAE48988.1; -; Genomic_DNA.
DR EMBL; BC107513; AAI07514.1; -; mRNA.
DR EMBL; BC122092; AAI22093.1; -; mRNA.
DR RefSeq; NP_001013045.1; NM_001013027.1.
DR RefSeq; NP_571095.1; NM_131020.2.
DR AlphaFoldDB; Q90486; -.
DR SMR; Q90486; -.
DR STRING; 7955.ENSDARP00000092488; -.
DR PaxDb; Q90486; -.
DR Ensembl; ENSDART00000101713; ENSDARP00000092488; ENSDARG00000089087.
DR Ensembl; ENSDART00000130869; ENSDARP00000109518; ENSDARG00000097238.
DR GeneID; 30216; -.
DR GeneID; 504174; -.
DR KEGG; dre:30216; -.
DR KEGG; dre:504174; -.
DR CTD; 30216; -.
DR CTD; 504174; -.
DR ZFIN; ZDB-GENE-990415-18; hbba1.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000157809; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; Q90486; -.
DR OrthoDB; 1370439at2759; -.
DR PhylomeDB; Q90486; -.
DR TreeFam; TF333268; -.
DR Reactome; R-DRE-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-DRE-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-DRE-2168880; Scavenging of heme from plasma.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-9707564; Cytoprotection by HMOX1.
DR Reactome; R-DRE-9707616; Heme signaling.
DR PRO; PR:Q90486; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000089087; Expressed in spleen and 16 other tissues.
DR ExpressionAtlas; Q90486; baseline and differential.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; ISS:UniProtKB.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:ZFIN.
DR CDD; cd08925; Hb-beta-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..148
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000052895"
FT BINDING 64
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 148 AA; 16389 MW; BC359ACF623C7ED4 CRC64;
MVEWTDAERT AILGLWGKLN IDEIGPQALS RCLIVYPWTQ RYFATFGNLS SPAAIMGNPK
VAAHGRTVMG GLERAIKNMD NVKNTYAALS VMHSEKLHVD PDNFRLLADC ITVCAAMKFG
QAGFNADVQE AWQKFLAVVV SALCRQYH
