ID   HBAZ_PANTR              Reviewed;         142 AA.
AC   P06347;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Hemoglobin subunit zeta;
DE   AltName: Full=Hemoglobin zeta chain;
DE   AltName: Full=Zeta-globin;
GN   Name=HBZ1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3003369; DOI=10.1007/bf02115686;
RA   Willard C., Wong E., Hess J.F., Shen C.-K.J., Chapman B., Wilson A.C.,
RA   Schmid C.W.;
RT   "Comparison of human and chimpanzee zeta 1 globin genes.";
RL   J. Mol. Evol. 22:309-315(1985).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X03234; CAA26980.1; -; Genomic_DNA.
DR   PIR; A02337; HZCZ.
DR   RefSeq; XP_016784461.1; XM_016928972.1.
DR   AlphaFoldDB; P06347; -.
DR   SMR; P06347; -.
DR   STRING; 9598.ENSPTRP00000012857; -.
DR   PaxDb; P06347; -.
DR   Ensembl; ENSPTRT00000013880; ENSPTRP00000012857; ENSPTRG00000031328.
DR   VGNC; VGNC:51580; HBZ.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000158623; -.
DR   InParanoid; P06347; -.
DR   OMA; VTIWAKV; -.
DR   OrthoDB; 1398217at2759; -.
DR   Proteomes; UP000002277; Chromosome 16.
DR   Bgee; ENSPTRG00000031328; Expressed in bone marrow and 3 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; 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_0000052853"
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;  15537 MW;  A62B956CA74C43C4 CRC64;
     MSLTKTEGTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH PGSAQLRAHG
     SKVVAAVGDA VKSIDNIGGA LSKLSELHAY ILRVDPVNFK LLSHCLLVTL AARFPADFTA
     EAHAAWDKFL SVVSSVLTEK YR