ID   AHSP_BOVIN              Reviewed;          92 AA.
AC   Q865F8; A4PJ03; Q3ZBI2; Q9BDR6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Alpha-hemoglobin-stabilizing protein;
DE   AltName: Full=Erythroid-associated factor;
GN   Name=AHSP; Synonyms=ERAF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Miele G., Manson J., Clinton M.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Otsuka Y., Ito D., Katsuoka K., Arashiki N., Inaba M.;
RT   "Bovine AHSP 5'-flanking.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-89.
RX   PubMed=11231637; DOI=10.1038/85515;
RA   Miele G., Manson J., Clinton M.;
RT   "A novel erythroid-specific marker of transmissible spongiform
RT   encephalopathies.";
RL   Nat. Med. 7:361-364(2001).
CC   -!- FUNCTION: Acts as a chaperone to prevent the harmful aggregation of
CC       alpha-hemoglobin during normal erythroid cell development. Specifically
CC       protects free alpha-hemoglobin from precipitation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Forms a heterodimer with free alpha-hemoglobin. Does
CC       not bind beta-hemoglobin nor alpha(2)beta(2) hemoglobin A (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AHSP family. {ECO:0000305}.
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DR   EMBL; AF485326; AAO49382.1; -; mRNA.
DR   EMBL; AB300618; BAF56597.1; -; Genomic_DNA.
DR   EMBL; BC103281; AAI03282.1; -; mRNA.
DR   EMBL; AF317803; AAK28063.1; -; Genomic_DNA.
DR   RefSeq; NP_803488.1; NM_177522.2.
DR   AlphaFoldDB; Q865F8; -.
DR   SMR; Q865F8; -.
DR   STRING; 9913.ENSBTAP00000008467; -.
DR   PaxDb; Q865F8; -.
DR   Ensembl; ENSBTAT00000008467; ENSBTAP00000008467; ENSBTAG00000006457.
DR   GeneID; 338381; -.
DR   KEGG; bta:338381; -.
DR   CTD; 51327; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006457; -.
DR   VGNC; VGNC:97237; AHSP.
DR   eggNOG; ENOG502SXDF; Eukaryota.
DR   GeneTree; ENSGT00390000003648; -.
DR   InParanoid; Q865F8; -.
DR   OMA; DWIKFYL; -.
DR   OrthoDB; 1413428at2759; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000006457; Expressed in semen and 93 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030492; F:hemoglobin binding; IEA:InterPro.
DR   GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   InterPro; IPR015317; A_Hb_stabilising_prot.
DR   InterPro; IPR036468; AHSP_sf.
DR   PANTHER; PTHR15914; PTHR15914; 1.
DR   Pfam; PF09236; AHSP; 1.
DR   SUPFAM; SSF109751; SSF109751; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..92
FT                   /note="Alpha-hemoglobin-stabilizing protein"
FT                   /id="PRO_0000064508"
FT   CONFLICT        36
FT                   /note="A -> D (in Ref. 4; AAK28063)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="D -> A (in Ref. 4; AAK28063)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="N -> P (in Ref. 4; AAK28063)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   92 AA;  10718 MW;  3CEC6F30F44F197E CRC64;
     MALIQTNKDL ISKGIKEFNI LLNQQVFSDP AISEEAMVTV VNDWVSFYIN YYKKQLSGEQ
     DEQDKALQEF RQELNTLSAS FLDKYRNFLK SS