HBPI_CHICK
ID HBPI_CHICK Reviewed; 142 AA.
AC P02007; Q78AK0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Hemoglobin subunit pi;
DE AltName: Full=Hemoglobin pi chain;
DE AltName: Full=Hemoglobin pi' chain;
DE AltName: Full=Pi-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 [GENOMIC DNA].
RX PubMed=6572397; DOI=10.1073/pnas.80.5.1392;
RA Engel J.D., Rusling D.J., McCune K.C., Dodgson J.B.;
RT "Unusual structure of the chicken embryonic alpha-globin gene, pi'.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:1392-1396(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11157800; DOI=10.1093/hmg/10.4.371;
RA Flint J., Tufarelli C., Peden J., Clark K., Daniels R.J., Hardison R.,
RA Miller W., Philipsen S., Tan-Un K.C., McMorrow T., Frampton J., Alter B.P.,
RA Frischauf A.-M., Higgs D.R.;
RT "Comparative genome analysis delimits a chromosomal domain and identifies
RT key regulatory elements in the alpha globin cluster.";
RL Hum. Mol. Genet. 10:371-382(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhao Z., Sjakste N., De Moura-Gallo C.V., Ioudinkova E.S., Razin S.V.,
RA Scherrer K.;
RT "Organization of the chicken domain of alpha-globin genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-142, AND VARIANT GLU-125.
RX PubMed=6157691; DOI=10.1016/s0021-9258(19)70526-2;
RA Chapman B.S., Tobin A.J., Hood L.E.;
RT "Complete amino acid sequences of the major early embryonic alpha-like
RT globins of the chicken.";
RL J. Biol. Chem. 255:9051-9059(1980).
CC -!- FUNCTION: The pi' chain is the counterpart of the alpha chain in the
CC major early embryonic hemoglobin P.
CC -!- MISCELLANEOUS: Only one chromosomal locus was found, suggesting that
CC the pi gene either does not exist or is an allele of the pi' gene.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; V00408; CAA23699.1; -; Genomic_DNA.
DR EMBL; AY016020; AAL35402.1; -; Genomic_DNA.
DR EMBL; AF098919; AAM09071.1; -; Genomic_DNA.
DR PIR; A93941; HACHPE.
DR RefSeq; NP_001004374.1; NM_001004374.2.
DR AlphaFoldDB; P02007; -.
DR SMR; P02007; -.
DR STRING; 9031.ENSGALP00000038921; -.
DR PaxDb; P02007; -.
DR Ensembl; ENSGALT00000012060; ENSGALP00000012046; ENSGALG00000023740.
DR GeneID; 416650; -.
DR KEGG; gga:416650; -.
DR CTD; 3050; -.
DR VEuPathDB; HostDB:geneid_416650; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000158623; -.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P02007; -.
DR OMA; VTIWAKV; -.
DR OrthoDB; 1398217at2759; -.
DR PhylomeDB; P02007; -.
DR TreeFam; TF332328; -.
DR PRO; PR:P02007; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000023740; Expressed in kidney and 4 other tissues.
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:0005506; F:iron ion binding; IEA:InterPro.
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; cd08927; Hb-alpha-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; IPR002338; Hemoglobin_a-typ.
DR InterPro; IPR002339; Hemoglobin_pi.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00815; PIHAEM.
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:6157691"
FT CHAIN 2..142
FT /note="Hemoglobin subunit pi"
FT /id="PRO_0000053272"
FT BINDING 59
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 88
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 VARIANT 125
FT /note="A -> E"
FT /evidence="ECO:0000269|PubMed:6157691"
SQ SEQUENCE 142 AA; 15709 MW; 4523C28E56E40415 CRC64;
MALTQAEKAA VTTIWAKVAT QIESIGLESL ERLFASYPQT KTYFPHFDVS QGSVQLRGHG
SKVLNAIGEA VKNIDDIRGA LAKLSELHAY ILRVDPVNFK LLSHCILCSV AARYPSDFTP
EVHAAWDKFL SSISSVLTEK YR
