HBB2_DANRE
ID HBB2_DANRE Reviewed; 148 AA.
AC Q90485; Q7SZW0; Q7T3C2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Beta-A2-globin;
DE AltName: Full=Hemoglobin beta-2 chain;
GN Name=ba2; ORFNames=si:dz118j2.3;
GN and
GN Name=ba2l; ORFNames=si:dz118j2.1, zgc:92900;
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:AAB05402.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (BA2), PARTIAL PROTEIN SEQUENCE, AND MASS
RP SPECTROMETRY.
RC TISSUE=Spleen {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] (BA2 AND BA2L).
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:CAE30441.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (BA2 AND BA2L).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH76356.1},
RC Kidney {ECO:0000312|EMBL:AAH53176.1}, and
RC Retina {ECO:0000312|EMBL:AAH59624.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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=16258.2; 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; U50379; AAB05402.1; -; mRNA.
DR EMBL; BX004811; CAE30441.1; -; Genomic_DNA.
DR EMBL; BX004811; CAE30439.1; -; Genomic_DNA.
DR EMBL; BC053176; AAH53176.1; -; mRNA.
DR EMBL; BC059624; AAH59624.1; -; mRNA.
DR EMBL; BC076356; AAH76356.1; -; mRNA.
DR RefSeq; NP_001005403.1; NM_001005403.1.
DR AlphaFoldDB; Q90485; -.
DR SMR; Q90485; -.
DR IntAct; Q90485; 1.
DR MINT; Q90485; -.
DR InParanoid; Q90485; -.
DR PhylomeDB; Q90485; -.
DR PRO; PR:Q90485; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 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-2"
FT /id="PRO_0000052896"
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"
FT CONFLICT 25
FT /note="G -> A (in Ref. 3; AAH53176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16389 MW; BC3588532B7EC144 CRC64;
MVEWTDAERT AILGLWGKLN IDEIGPQALS RCLIVYPWTQ RYFATFGNLS SPAAIMGNPK
VAAHGRTVMG GLERAIKNMD NIKNTYAALS VMHSEKLHVD PDNFKLLADC ITVCAAMKFG
QAGFNADIQE AWQKFLAVVV SALCRQYH
