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Yet despite first-hand accounts of their biology, little is known regarding the physiological adjustments underlying their evolution to this environment. Here, the adult-expressed hemoglobin (Hb; \u03b1\n                    <jats:sub>2<\/jats:sub>\n                    \u03b2\/\u03b4\n                    <jats:sub>2<\/jats:sub>\n                    ) of this sirenian is shown to harbor a fixed amino acid replacement at an otherwise invariant position (\u03b2\/\u03b482Lys\u2192Asn) that alters multiple aspects of Hb function. First, our functional characterization of recombinant sirenian Hb proteins demonstrates that the Hb-O\n                    <jats:sub>2<\/jats:sub>\n                    affinity of this sub-Arctic species was less affected by temperature than those of living (sub)tropical sea cows. This phenotype presumably safeguarded O\n                    <jats:sub>2<\/jats:sub>\n                    delivery to cool peripheral tissues and largely arises from a reduced intrinsic temperature sensitivity of the\n                    <jats:italic>H. gigas<\/jats:italic>\n                    protein. Additional experiments on\n                    <jats:italic>H. gigas<\/jats:italic>\n                    \u03b2\/\u03b482Asn\u2192Lys mutant Hb further reveal this exchange renders Steller\u2019s sea cow Hb unresponsive to the potent intraerythrocytic allosteric effector 2,3-diphosphoglycerate, a radical modification that is the first documented example of this phenotype among mammals. Notably, \u03b2\/\u03b482Lys\u2192Asn moreover underlies the secondary evolution of a reduced blood-O\n                    <jats:sub>2<\/jats:sub>\n                    affinity phenotype that would have promoted heightened tissue and maternal\/fetal O\n                    <jats:sub>2<\/jats:sub>\n                    delivery. This conclusion is bolstered by analyses of two Steller\u2019s sea cow prenatal Hb proteins (Hb Gower I; \u03b6\n                    <jats:sub>2<\/jats:sub>\n                    \u03b5\n                    <jats:sub>2<\/jats:sub>\n                    and HbF; \u03b1\n                    <jats:sub>2<\/jats:sub>\n                    \u03b3\n                    <jats:sub>2<\/jats:sub>\n                    ) that suggest an exclusive embryonic stage expression pattern, and reveal uncommon replacements in\n                    <jats:italic>H. gigas<\/jats:italic>\n                    HbF (\u03b338Thr\u2192Ile and \u03b3101Glu\u2192Asp) that increased Hb-O\n                    <jats:sub>2<\/jats:sub>\n                    affinity relative to dugong HbF. Finally, the \u03b2\/\u03b482Lys\u2192Asn replacement of the adult\/fetal protein is shown to increase protein solubility, which may have elevated red blood cell Hb content within both the adult and fetal circulations and contributed to meeting the elevated metabolic (thermoregulatory) requirements and fetal growth rates associated with this species cold adaptation.\n                  <\/jats:p>","DOI":"10.7554\/elife.85414","type":"journal-article","created":{"date-parts":[[2023,6,1]],"date-time":"2023-06-01T06:00:36Z","timestamp":1685599236000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.85414","source":"Crossref","is-referenced-by-count":1,"title":["Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller\u2019s sea cows"],"prefix":"10.7554","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0664-0864","authenticated-orcid":true,"given":"Anthony V","family":"Signore","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02gfys938","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Manitoba","place":["Winnipeg, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillip R","family":"Morrison","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03rmrcq20","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Zoology, University of British Columbia","place":["Vancouver, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Colin J","family":"Brauner","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03rmrcq20","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Zoology, University of British Columbia","place":["Vancouver, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela","family":"Fago","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01aj84f44","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Aarhus University","place":["Aarhus, Denmark"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roy E","family":"Weber","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01aj84f44","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Aarhus University","place":["Aarhus, Denmark"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7005-7086","authenticated-orcid":true,"given":"Kevin L","family":"Campbell","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02gfys938","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Manitoba","place":["Winnipeg, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2023,6,1]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"9752","DOI":"10.1021\/bi200876e","article-title":"Isolated Hb Providence \u039282Asn and \u039282Asp fractions are more stable than native HbA0 under oxidative stress conditions","volume":"50","author":"Abraham","year":"2011","journal-title":"Biochemistry"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"W344","DOI":"10.1093\/nar\/gkw408","article-title":"Consurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules","volume":"44","author":"Ashkenazy","year":"2016","journal-title":"Nucleic Acids Research"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"2376","DOI":"10.1021\/bi00708a022","article-title":"Calorimetric determination of the heat of oxygenation of human hemolgobin as a function of pH and the extent of reaction","volume":"13","author":"Atha","year":"1974","journal-title":"Biochemistry"},{"key":"bib4","doi-asserted-by":"publisher","first-page":"333","DOI":"10.3109\/03630268508997009","article-title":"A new case of hemoglobin providence (\u03b12\u03b22 82 (EF6) Lys\u2192 Asn or Asp) discovered in a French Caucasian family. 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