HBAZ_NOTEU
ID HBAZ_NOTEU Reviewed; 79 AA.
AC P81044;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Hemoglobin subunit zeta;
DE AltName: Full=Hemoglobin zeta chain;
DE AltName: Full=Zeta-globin;
DE Flags: Fragments;
OS Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT SER-1, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Blood;
RX PubMed=9342240; DOI=10.1111/j.1432-1033.1997.00864.x;
RA Holland R.A.B., Gooley A.A.;
RT "Characterization of the embryonic globin chains of the marsupial Tammar
RT wallaby, Macropus eugenii.";
RL Eur. J. Biochem. 248:864-871(1997).
CC -!- FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic
CC hemoglobin.
CC -!- SUBUNIT: Heterotetramer of two zeta chains and two epsilon chains.
CC {ECO:0000269|PubMed:9342240}.
CC -!- DEVELOPMENTAL STAGE: Detected in blood from prenatal and neonatal
CC animals. {ECO:0000269|PubMed:9342240}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR iPTMnet; P81044; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.10; -; 2.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR Pfam; PF00042; Globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Phosphoprotein; Transport.
FT CHAIN 1..>79
FT /note="Hemoglobin subunit zeta"
FT /id="PRO_0000052854"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9342240"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02008"
FT UNSURE 16
FT /note="K or R"
FT UNSURE 17
FT /note="R or K"
FT UNSURE 26
FT /note="K or R"
FT UNSURE 43
FT /note="K or R"
FT UNSURE 54
FT /note="K or R"
FT UNSURE 71
FT /note="K or R"
FT NON_CONS 16..17
FT /evidence="ECO:0000305"
FT NON_CONS 42..43
FT /evidence="ECO:0000305"
FT NON_TER 79
SQ SEQUENCE 79 AA; 9185 MW; 5E61C3193F79C4B8 CRC64;
SLTKTXXTII XAMWAKRLFT SYPQTKTYFP HFDLHPDSAQ LRKNIDNIHS ALSKLSELHA
YILRVDPVNF KLLSHXFLV