HBRH_CHICK
ID HBRH_CHICK Reviewed; 147 AA.
AC P02127;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Hemoglobin subunit rho;
DE AltName: Full=Hemoglobin rho chain;
DE AltName: Full=Rho-globin;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6170981; DOI=10.1073/pnas.78.8.4782;
RA Roninson I.B., Ingram V.M.;
RT "cDNA sequence of a new chicken embryonic rho-globin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4782-4785(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6313671; DOI=10.1016/s0021-9258(17)44230-x;
RA Dodgson J.B., Stadt S.J., Choi O.-R., Dolan M., Fischer H.D., Engel J.D.;
RT "The nucleotide sequence of the embryonic chicken beta-type globin genes.";
RL J. Biol. Chem. 258:12685-12692(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8307571; DOI=10.1016/s0888-7543(05)80364-7;
RA Reitman M., Grasso J.A., Blumenthal R., Lewit P.;
RT "Primary sequence, evolution, and repetitive elements of the Gallus gallus
RT (chicken) beta-globin cluster.";
RL Genomics 18:616-626(1993).
RN [4]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=7240154; DOI=10.1016/s0021-9258(19)69232-x;
RA Chapman B.S., Tobin A.J., Hood L.E.;
RT "Complete amino acid sequence of the major early embryonic beta-like globin
RT in chickens.";
RL J. Biol. Chem. 256:5524-5531(1981).
CC -!- FUNCTION: The rho chain is the major early embryonic beta-type
CC hemoglobin chain.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; V00412; CAA23703.1; -; mRNA.
DR EMBL; K00823; AAA48806.1; -; Genomic_DNA.
DR EMBL; L17432; AAD03345.1; -; Genomic_DNA.
DR PIR; I50247; HFCHR.
DR RefSeq; NP_001004390.1; NM_001004390.1.
DR AlphaFoldDB; P02127; -.
DR SMR; P02127; -.
DR STRING; 9031.ENSGALP00000027974; -.
DR Ensembl; ENSGALT00000028027; ENSGALP00000027974; ENSGALG00000017347.
DR GeneID; 419079; -.
DR KEGG; gga:419079; -.
DR CTD; 419079; -.
DR VEuPathDB; HostDB:geneid_419079; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000157809; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR OMA; DFTPTCQ; -.
DR OrthoDB; 1370439at2759; -.
DR Reactome; R-GGA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-GGA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-GGA-2168880; Scavenging of heme from plasma.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-GGA-9707616; Heme signaling.
DR PRO; PR:P02127; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017347; Expressed in lung.
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: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: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 Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7240154"
FT CHAIN 2..147
FT /note="Hemoglobin subunit rho"
FT /id="PRO_0000053274"
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 CONFLICT 126
FT /note="T -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="H -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Y -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16589 MW; CD1798DB1215CEB8 CRC64;
MVHWSAEEKQ LITSVWSKVN VEECGAEALA RLLIVYPWTQ RFFDNFGNLS SPTAIIGNPK
VRAHGKKVLS SFGEAVKNLD NIKNTYAKLS ELHCEKLHVD PENFRLLGNI LIIVLAAHFT
KDFTPTCQAV WQKLVSVVAH ALAYKYH
