HBB2_RAT
ID HBB2_RAT Reviewed; 147 AA.
AC P11517;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Hemoglobin beta chain, minor-form;
DE AltName: Full=Hemoglobin beta-2 chain;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3453111; DOI=10.1093/nar/15.3.1336;
RA Ohshita Y., Hozumi T.;
RT "Sequence of the rat beta-globin mRNA.";
RL Nucleic Acids Res. 15:1336-1336(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2748344; DOI=10.1093/nar/17.12.4878;
RA Stevanovic M., Crkvenjakov R.;
RT "Genomic sequence of rat beta-globin minor gene.";
RL Nucleic Acids Res. 17:4878-4878(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=3357786; DOI=10.1093/nar/16.5.2342;
RA Wong W.M., Lam V.M.S., Cheng L.Y.L., Tam J.W.O.;
RT "Genomic sequence of a Sprague-Dawley rat beta-globin gene.";
RL Nucleic Acids Res. 16:2342-2342(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2587229; DOI=10.1093/nar/17.21.8870;
RA Woo C., Lam V.M.S., Tam J.W.O.;
RT "cDNA sequences of two beta-globin genes in a Sprague-Dawley rat.";
RL Nucleic Acids Res. 17:8870-8870(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RA Inokuchi N., Iwahara S., Satoh H., Nagoe Y., Okazaki T.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-18; 32-41; 46-62; 67-145; 84-96 AND 106-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-53 AND THR-124,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 (VARIANT SER-126),
RP VARIANT [LARGE SCALE ANALYSIS] SER-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: In rats there are two non-allelic alpha chains and two
CC non-allelic beta chains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X67616; CAA47876.1; -; Genomic_DNA.
DR EMBL; X15160; CAA33250.1; -; Genomic_DNA.
DR EMBL; X05080; CAA28738.1; -; mRNA.
DR EMBL; X06701; CAA29887.1; -; Genomic_DNA.
DR EMBL; X16418; CAA34440.1; -; mRNA.
DR EMBL; X67615; CAA47875.1; -; Genomic_DNA.
DR EMBL; X67614; CAA47874.1; -; Genomic_DNA.
DR PIR; A25747; A25747.
DR PIR; S00840; S00840.
DR RefSeq; NP_001104739.1; NM_001111269.1.
DR RefSeq; NP_001106694.1; NM_001113223.1.
DR RefSeq; XP_008772023.1; XM_008773801.1.
DR RefSeq; XP_017458001.1; XM_017602512.1.
DR AlphaFoldDB; P11517; -.
DR SMR; P11517; -.
DR BioGRID; 603888; 1.
DR ComplexPortal; CPX-2926; Hemoglobin HbA complex, variant HBB2.
DR IntAct; P11517; 1.
DR MINT; P11517; -.
DR STRING; 10116.ENSRNOP00000048546; -.
DR iPTMnet; P11517; -.
DR PhosphoSitePlus; P11517; -.
DR SwissPalm; P11517; -.
DR jPOST; P11517; -.
DR PaxDb; P11517; -.
DR PRIDE; P11517; -.
DR Ensembl; ENSRNOT00000019913; ENSRNOP00000019914; ENSRNOG00000047098.
DR Ensembl; ENSRNOT00000090745; ENSRNOP00000071528; ENSRNOG00000047098.
DR GeneID; 100134871; -.
DR GeneID; 689064; -.
DR KEGG; rno:100134871; -.
DR KEGG; rno:689064; -.
DR CTD; 100503605; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000156216; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P11517; -.
DR OMA; TPDAVMN; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR PRO; PR:P11517; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000047098; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; P11517; baseline and differential.
DR Genevisible; P11517; RN.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha 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; IBA:GO_Central.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Methylation; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086, ECO:0000269|Ref.6"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-2"
FT /id="PRO_0000053091"
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 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 MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 126
FT /note="Phosphoserine; in variant Ser-126"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VARIANT 21
FT /note="A -> P (in strain: Sprague-Dawley)"
FT VARIANT 126
FT /note="C -> S (in strain: Sprague-Dawley)"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 147 AA; 15982 MW; 909061A0AD4E7BB8 CRC64;
MVHLTDAEKA TVSGLWGKVN ADNVGAEALG RLLVVYPWTQ RYFSKFGDLS SASAIMGNPQ
VKAHGKKVIN AFNDGLKHLD NLKGTFAHLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
KEFTPCAQAA FQKVVAGVAS ALAHKYH
