ID O88753_RAT Unreviewed; 147 AA. AC O88753; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 161. DE SubName: Full=Epsilon 2 globin {ECO:0000313|EMBL:CAA39766.1}; DE SubName: Full=Globin b3 {ECO:0000313|EMBL:SAI82214.1}; DE SubName: Full=Hemoglobin, epsilon 2 {ECO:0000313|Ensembl:ENSRNOP00000044821.1}; GN Name=Hbe2 {ECO:0000313|Ensembl:ENSRNOP00000044821.1, GN ECO:0000313|RGD:1564524}; GN Synonyms=epsilon 2 {ECO:0000313|EMBL:CAA39766.1}, Glnb3 GN {ECO:0000313|EMBL:SAI82214.1}, Hbe2_predicted GN {ECO:0000313|RGD:1564524}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:CAA39766.1}; RN [1] {ECO:0000313|EMBL:CAA39766.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar {ECO:0000313|EMBL:CAA39766.1}; RA Hiroyuki S.; RL Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAA39766.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar {ECO:0000313|EMBL:CAA39766.1}; RX PubMed=10196478; DOI=10.1016/S0378-1119(99)00055-4; RA Sato H., Inokuchi N., Nagae Y., Okazaki T.; RT "Molecular cloning and characterization of two sets of alpha-theta genes in RT the rat alpha-like globin gene cluster."; RL Gene 230:91-99(1999). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000044821.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000044821.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [4] {ECO:0000313|EMBL:SAI82214.1} RP NUCLEOTIDE SEQUENCE. RX DOI=10.1016/j.genrep.2016.10.009; RA Premzl M.; RT "Comparative genomic analysis of eutherian globin genes."; RL Gene Rep 5:163-166(2016). RN [5] {ECO:0000313|EMBL:SAI82214.1} RP NUCLEOTIDE SEQUENCE. RX DOI=10.1016/j.genrep.2019.100414; RA Premzl M.; RT "Eutherian third-party data gene collections."; RL Gene Rep 16:100414-100414(2019). RN [6] {ECO:0000313|Ensembl:ENSRNOP00000044821.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000044821.1}; RG Ensembl; RL Submitted (JUL-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the globin family. CC {ECO:0000256|ARBA:ARBA00008705, ECO:0000256|PROSITE-ProRule:PRU00238, CC ECO:0000256|RuleBase:RU000356}. 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; X56327; CAA39766.1; -; Genomic_DNA. DR EMBL; LT548167; SAI82214.1; -; Genomic_DNA. DR RefSeq; NP_001019976.1; NM_001024805.1. DR SMR; O88753; -. DR STRING; 10116.ENSRNOP00000044821; -. DR PaxDb; 10116-ENSRNOP00000044821; -. DR Ensembl; ENSRNOT00000048484.2; ENSRNOP00000044821.1; ENSRNOG00000030784.2. DR GeneID; 502359; -. DR KEGG; rno:502359; -. DR AGR; RGD:1564524; -. DR CTD; 502359; -. DR RGD; 1564524; Hbe2. DR eggNOG; KOG3378; Eukaryota. DR GeneTree; ENSGT00940000164134; -. DR HOGENOM; CLU_003827_10_0_1; -. DR OMA; SELHCER; -. DR OrthoDB; 5356926at2759; -. DR TreeFam; TF333268; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000030784; Expressed in testis. 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:0031721; F:hemoglobin alpha binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; cd08925; Hb-beta-like; 1. DR Gene3D; 1.10.490.10; Globins; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR012292; Globin/Proto. DR InterPro; IPR002337; Hemoglobin_b. DR PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF47; HEMOGLOBIN SUBUNIT BETA-H0; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00238}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00238}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00238}; KW Oxygen transport {ECO:0000256|ARBA:ARBA00022621, ECO:0000256|PROSITE- KW ProRule:PRU00238}; Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE- KW ProRule:PRU00238}. FT DOMAIN 2..147 FT /note="Globin family profile" FT /evidence="ECO:0000259|PROSITE:PS01033" FT BINDING 64 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:0000256|PROSITE-ProRule:PRU00238" FT BINDING 93 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 /evidence="ECO:0000256|PROSITE-ProRule:PRU00238" SQ SEQUENCE 147 AA; 16388 MW; 8F83E066420FA556 CRC64; MVHFTAEEKA AIISIWEKVD LEKLGGETLG RLLIVYPWTQ RFFDKFGNLS SAPAIMGNPQ IRAHGKKVLV SLGLAVENMD NLKETFAHLS ELHCDKLHVD PENFKLLGNV LVIVLSSYFG KEFTAEVQAA WQKLVAGVAT ALSHKYH //