HBAZ_MOUSE
ID HBAZ_MOUSE Reviewed; 142 AA.
AC P06467; Q61654;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Hemoglobin subunit zeta;
DE AltName: Full=Alpha-like embryonic globin chain x;
DE AltName: Full=Hemoglobin zeta chain;
DE AltName: Full=Zeta-globin;
GN Name=Hbz; Synonyms=Hba-x, Hbz1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4000117; DOI=10.1128/mcb.5.5.1025-1033.1985;
RA Leder A., Weir L., Leder P.;
RT "Characterization, expression, and evolution of the mouse embryonic zeta-
RT globin gene.";
RL Mol. Cell. Biol. 5:1025-1033(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2444404; DOI=10.1242/dev.99.4.493;
RA Wilkinson D.G., Bailes J.A., Champion J.E., McMahon A.P.;
RT "A molecular analysis of mouse development from 8 to 10 days post coitum
RT detects changes only in embryonic globin expression.";
RL Development 99:493-500(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-142.
RC TISSUE=Erythroid cell;
RX PubMed=6084630; DOI=10.1016/0378-1119(84)90215-4;
RA Farace M.-G., Hill A., Tripodi M., Padgett R.W., Raschella G., Gambari R.,
RA Fantoni A., Hutchison C.A. III, Edgell M.H.;
RT "Molecular cloning and sequence analysis of a cDNA coding for the mouse
RT alpha-like embryonic globin chain x.";
RL Gene 31:241-245(1984).
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; X62302; CAA44187.1; -; Genomic_DNA.
DR EMBL; M26898; AAA37702.1; -; mRNA.
DR EMBL; AK077590; BAC36881.1; -; mRNA.
DR EMBL; BC051988; AAH51988.1; -; mRNA.
DR EMBL; M13125; AAA37794.1; -; mRNA.
DR CCDS; CCDS24522.1; -.
DR PIR; A23283; A23283.
DR RefSeq; NP_034535.1; NM_010405.4.
DR AlphaFoldDB; P06467; -.
DR SMR; P06467; -.
DR BioGRID; 200216; 4.
DR ComplexPortal; CPX-2938; Early embryonic hemoglobin complex.
DR ComplexPortal; CPX-2939; Embryonic hemoglobin complex.
DR STRING; 10090.ENSMUSP00000020531; -.
DR iPTMnet; P06467; -.
DR PhosphoSitePlus; P06467; -.
DR CPTAC; non-CPTAC-3819; -.
DR jPOST; P06467; -.
DR PaxDb; P06467; -.
DR PeptideAtlas; P06467; -.
DR PRIDE; P06467; -.
DR ProteomicsDB; 270895; -.
DR Antibodypedia; 8877; 277 antibodies from 30 providers.
DR DNASU; 15126; -.
DR Ensembl; ENSMUST00000020531; ENSMUSP00000020531; ENSMUSG00000055609.
DR GeneID; 15126; -.
DR KEGG; mmu:15126; -.
DR UCSC; uc007ijj.2; mouse.
DR CTD; 15126; -.
DR MGI; MGI:96019; Hba-x.
DR VEuPathDB; HostDB:ENSMUSG00000055609; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000158623; -.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P06467; -.
DR OMA; AAMFPND; -.
DR OrthoDB; 1398217at2759; -.
DR PhylomeDB; P06467; -.
DR TreeFam; TF332328; -.
DR BioGRID-ORCS; 15126; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hba-x; mouse.
DR PRO; PR:P06467; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P06467; protein.
DR Bgee; ENSMUSG00000055609; Expressed in yolk sac and 86 other tissues.
DR ExpressionAtlas; P06467; baseline and differential.
DR Genevisible; P06467; MM.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; ISO:MGI.
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:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0015671; P:oxygen transport; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; IC:ComplexPortal.
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 2: Evidence at transcript level;
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_0000052852"
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 CONFLICT 44
FT /note="F -> L (in Ref. 5; AAA37794)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="V -> L (in Ref. 2; AAA37702)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> N (in Ref. 2; AAA37702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 16235 MW; 9E9D246806744851 CRC64;
MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG
FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP
EVHEAWDKFM SILSSILTEK YR
