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Database: UniProt
Entry: HBB1_RAT
LinkDB: HBB1_RAT
Original site: 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   24-JAN-2024, entry version 180.
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; 2.
DR   STRING; 10116.ENSRNOP00000070324; -.
DR   CarbonylDB; P02091; -.
DR   GlyGen; P02091; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P02091; -.
DR   PhosphoSitePlus; P02091; -.
DR   jPOST; P02091; -.
DR   PaxDb; 10116-ENSRNOP00000048250; -.
DR   Ensembl; ENSRNOT00000114441.1; ENSRNOP00000085307.1; ENSRNOG00000047098.3.
DR   GeneID; 24440; -.
DR   KEGG; rno:24440; -.
DR   UCSC; RGD:2783; rat.
DR   AGR; RGD:2783; -.
DR   CTD; 3043; -.
DR   RGD; 2783; Hbb.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000156216; -.
DR   InParanoid; P02091; -.
DR   OrthoDB; 5356926at2759; -.
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; NAS: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: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; Globins; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002337; Hemoglobin_b.
DR   PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR11442:SF42; HEMOGLOBIN SUBUNIT BETA; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin-like; 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
//
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