AHSP_MOUSE
ID AHSP_MOUSE Reviewed; 102 AA.
AC Q9CY02; O70427;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Alpha-hemoglobin-stabilizing protein;
DE AltName: Full=Erythroid differentiation-related factor;
DE AltName: Full=Erythroid-associated factor;
GN Name=Ahsp; Synonyms=Edrf, Eraf;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Erythroblast;
RX PubMed=12569662;
RA Liu S.G., Zhang Z.Y., Ma J., Zhang J.B., Xue S.P.;
RT "Subtractive cDNA cloning and analysis of murine erythroid terminal
RT differentiation related factor.";
RL Zhongguo Yi Xue Ke Xue Yuan Xue Bao 21:94-98(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Miele G., Manson J., Clinton M.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12066189; DOI=10.1038/nature00803;
RA Kihm A.J., Kong Y., Hong W., Russell J.E., Rouda S., Adachi K., Simon M.C.,
RA Blobel G.A., Weiss M.J.;
RT "An abundant erythroid protein that stabilizes free alpha-haemoglobin.";
RL Nature 417:758-763(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:12066189}.
CC -!- SUBUNIT: Monomer. Forms a heterodimer with free alpha-hemoglobin. Does
CC not bind beta-hemoglobin nor alpha(2)beta(2) hemoglobin A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12066189}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, bone marrow, and blood, with
CC highest levels in bone marrow. {ECO:0000269|PubMed:11231637,
CC ECO:0000269|PubMed:12066189}.
CC -!- INDUCTION: By GATA-1 during erythroid maturation.
CC -!- SIMILARITY: Belongs to the AHSP family. {ECO:0000305}.
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DR EMBL; AF364516; AAK50855.1; -; mRNA.
DR EMBL; AF060220; AAC15075.1; -; mRNA.
DR EMBL; AF485327; AAO49383.1; -; Genomic_DNA.
DR EMBL; AK011084; BAB27388.1; -; mRNA.
DR EMBL; AK028172; BAC25789.1; -; mRNA.
DR RefSeq; NP_573508.1; NM_133245.1.
DR AlphaFoldDB; Q9CY02; -.
DR SMR; Q9CY02; -.
DR iPTMnet; Q9CY02; -.
DR PhosphoSitePlus; Q9CY02; -.
DR CPTAC; non-CPTAC-3760; -.
DR MaxQB; Q9CY02; -.
DR PRIDE; Q9CY02; -.
DR ProteomicsDB; 281821; -.
DR DNASU; 170812; -.
DR GeneID; 170812; -.
DR KEGG; mmu:170812; -.
DR CTD; 51327; -.
DR MGI; MGI:2158492; Ahsp.
DR InParanoid; Q9CY02; -.
DR PhylomeDB; Q9CY02; -.
DR PRO; PR:Q9CY02; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9CY02; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030492; F:hemoglobin binding; IEA:InterPro.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0006457; P:protein folding; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:MGI.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..102
FT /note="Alpha-hemoglobin-stabilizing protein"
FT /id="PRO_0000064510"
SQ SEQUENCE 102 AA; 11832 MW; 095A66942A06C7BA CRC64;
MAPFQSNKDL ISTGIKEFNV LLDQQVFDDP LISEEDMVIV VHDWVNLYTN YYKKLVHGEQ
EEQDRAMTEF QQELSTLGSQ FLAKYRTFLK SKEPPSNTLP SS
