HBAZ_CAPHI
ID HBAZ_CAPHI Reviewed; 142 AA.
AC P13786;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Hemoglobin subunit zeta;
DE AltName: Full=Hemoglobin zeta chain;
DE AltName: Full=Zeta-globin;
GN Name=HBZ1;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3560223; DOI=10.1016/0022-2836(86)90269-x;
RA Wernke S.M., Lingrel J.B.;
RT "Nucleotide sequence of the goat embryonic alpha globin gene (zeta) and
RT linkage and evolutionary analysis of the complete alpha globin cluster.";
RL J. Mol. Biol. 192:457-471(1986).
CC -!- FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic
CC hemoglobin. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two zeta chains and beta-type chains.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X04726; CAA28435.1; -; Genomic_DNA.
DR EMBL; X04862; CAA28435.1; JOINED; Genomic_DNA.
DR PIR; A25555; A25555.
DR RefSeq; XP_017895578.1; XM_018040089.1.
DR AlphaFoldDB; P13786; -.
DR SMR; P13786; -.
DR STRING; 9925.ENSCHIP00000019992; -.
DR Ensembl; ENSCHIT00000027816; ENSCHIP00000019992; ENSCHIG00000018800.
DR GeneID; 108633874; -.
DR KEGG; chx:108633874; -.
DR GeneTree; ENSGT00940000158623; -.
DR OMA; AAMFPND; -.
DR OrthoDB; 1398217at2759; -.
DR Proteomes; UP000291000; Chromosome 25.
DR Bgee; ENSCHIG00000018800; Expressed in uterus and 2 other tissues.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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; IPR002340; Hemoglobin_zeta.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00816; ZETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 3: Inferred from homology;
KW Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT CHAIN 2..142
FT /note="Hemoglobin subunit zeta"
FT /id="PRO_0000052849"
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
SQ SEQUENCE 142 AA; 15697 MW; C7538DF9047018E8 CRC64;
MSLTRTERTI ILSLWSKIST QADVIGTETL ERLFSCYPQA KTYFPHFDLH SGSAQLRAHG
SKVVAAVGDA VKSIDNVTSA LSKLSELHAY VLRVDPVNFK FLSHCLLVTL ASHFPADFTA
DAHAAWDKFL SIVSGVLTEK YR