HBB1_RAT
ID HBB1_RAT Reviewed; 147 AA.
AC P02091; P33584;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Hemoglobin beta chain, major-form;
DE AltName: Full=Hemoglobin beta-1 chain;
GN Name=Hbb;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2740220; DOI=10.1093/nar/17.11.4368;
RA Radosavlevic D., Crkvenjakov R.;
RT "Genomic sequence of rat beta-globin major gene.";
RL Nucleic Acids Res. 17:4368-4368(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3619896; DOI=10.1016/0006-291x(87)90573-0;
RA Satoh H., Fujii H., Okazaki T.;
RT "Molecular cloning and sequence analysis of two rat major globin cDNAs.";
RL Biochem. Biophys. Res. Commun. 146:618-624(1987).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [6]
RP PROTEIN SEQUENCE OF 2-147.
RA Garrick L.M., Klonowski T.J., Sloan R.L., Ryan T.W., Garrick M.D.;
RT "Primary structure of the major beta chain of rat hemoglobin.";
RL Fed. Proc. 36:758-758(1977).
RN [7]
RP PROTEIN SEQUENCE OF 2-36.
RC TISSUE=Brown adipose tissue;
RX PubMed=8334153; DOI=10.1016/0005-2760(93)90084-m;
RA Dutta-Roy A.K., Huang Y., Dunbar B., Trayhurn P.;
RT "Purification and characterization of fatty acid-binding proteins from
RT brown adipose tissue of the rat.";
RL Biochim. Biophys. Acta 1169:73-79(1993).
RN [8]
RP PROTEIN SEQUENCE OF 2-60; 67-145; 84-104 AND 106-145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-51 AND SER-53, AND
RP IDENTIFICATION BY MASS 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}.
CC -!- CAUTION: PubMed:8334153 incorrectly assigned their sequence fragment as
CC a fatty acid-binding protein. {ECO:0000305}.
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DR EMBL; X16417; CAA34439.1; -; mRNA.
DR EMBL; X15009; CAA33114.1; -; Genomic_DNA.
DR EMBL; M17084; AAA41309.1; -; mRNA.
DR EMBL; X67613; CAA47873.1; -; Genomic_DNA.
DR EMBL; BC058448; AAH58448.1; -; mRNA.
DR PIR; S04588; S04588.
DR PIR; S06748; HBRT.
DR RefSeq; NP_150237.1; NM_033234.1.
DR PDB; 3DHT; X-ray; 2.98 A; B=2-147.
DR PDB; 3HF4; X-ray; 2.70 A; B/F=2-147.
DR PDBsum; 3DHT; -.
DR PDBsum; 3HF4; -.
DR AlphaFoldDB; P02091; -.
DR SMR; P02091; -.
DR BioGRID; 246605; 4.
DR ComplexPortal; CPX-2925; Hemoglobin HbA complex, variant HBB1.
DR IntAct; P02091; 1.
DR STRING; 10116.ENSRNOP00000048250; -.
DR CarbonylDB; P02091; -.
DR iPTMnet; P02091; -.
DR PhosphoSitePlus; P02091; -.
DR jPOST; P02091; -.
DR PaxDb; P02091; -.
DR PRIDE; P02091; -.
DR Ensembl; ENSRNOT00000114441; ENSRNOP00000085307; ENSRNOG00000047098.
DR GeneID; 24440; -.
DR KEGG; rno:24440; -.
DR UCSC; RGD:2783; rat.
DR CTD; 3043; -.
DR RGD; 2783; Hbb.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000156216; -.
DR InParanoid; P02091; -.
DR OrthoDB; 1370439at2759; -.
DR PhylomeDB; P02091; -.
DR TreeFam; TF333268; -.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR Reactome; R-RNO-9707616; Heme signaling.
DR EvolutionaryTrace; P02091; -.
DR PRO; PR:P02091; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:RGD.
DR GO; GO:0005833; C:hemoglobin complex; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IDA:RGD.
DR GO; GO:0031722; F:hemoglobin beta binding; IDA:RGD.
DR GO; GO:0030492; F:hemoglobin binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005344; F:oxygen carrier activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0030185; P:nitric oxide transport; ISO:RGD.
DR GO; GO:0015671; P:oxygen transport; IDA:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0010999; P:regulation of eIF2 alpha phosphorylation by heme; ISO:RGD.
DR GO; GO:0070293; P:renal absorption; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Methylation; Oxygen transport; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:8334153, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.8"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000053090"
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 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02088"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11517"
FT VARIANT 59
FT /note="P -> A"
FT VARIANT 88
FT /note="H -> N"
FT VARIANT 90
FT /note="S -> T"
FT VARIANT 124
FT /note="T -> S"
FT CONFLICT 14
FT /note="G -> A (in Ref. 3; AAA41309)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:3HF4"
SQ SEQUENCE 147 AA; 15979 MW; 77A715901BC44D26 CRC64;
MVHLTDAEKA AVNGLWGKVN PDDVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNPK
VKAHGKKVIN AFNDGLKHLD NLKGTFAHLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
KEFTPCAQAA FQKVVAGVAS ALAHKYH
