ID Q98963_9TELE Unreviewed; 110 AA. AC Q98963; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 105. DE RecName: Full=Myoglobin {ECO:0000256|ARBA:ARBA00019044, ECO:0000256|RuleBase:RU251113}; DE Flags: Fragment; OS Notothenia coriiceps (black rockcod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Notothenia. OX NCBI_TaxID=8208 {ECO:0000313|EMBL:AAC69245.1}; RN [1] {ECO:0000313|EMBL:AAC69245.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Heart ventricle {ECO:0000313|EMBL:AAC69245.1}; RA Vayda M.E., Small D.J., Sidell B.D.; RT "Expression of the myoglobin gene in Antarctic channichthyid fishes."; RL (In) Battaglia B., Valencia J., Walton S.W.H. (eds.); RL VI SCAR ANTARCTIC COMMUNITIES, pp.1-1, Cambridge University Press, RL Cambridge, UK (1996). RN [2] {ECO:0000313|EMBL:AAC69245.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Heart ventricle {ECO:0000313|EMBL:AAC69245.1}; RX PubMed=9694664; DOI=10.1007/PL00006372; RA Small D.J., Vayda M.E., Sidell B.D.; RT "A novel vertebrate myoglobin gene containing three A+T-rich introns is RT conserved among Antarctic teleost species which differ in myoglobin RT expression."; RL J. Mol. Evol. 47:156-166(1998). CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the CC movement of oxygen within muscles. {ECO:0000256|ARBA:ARBA00002755, CC ECO:0000256|RuleBase:RU251113}. 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; U68350; AAC69245.1; -; mRNA. DR AlphaFoldDB; Q98963; -. DR SMR; Q98963; -. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019825; F:oxygen binding; IEA:UniProtKB-UniRule. DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule. DR Gene3D; 6.10.140.2100; -; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR002335; Myoglobin. DR PANTHER; PTHR47132; MYOGLOBIN; 1. DR PANTHER; PTHR47132:SF1; MYOGLOBIN; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00613; MYOGLOBIN. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 2: Evidence at transcript level; 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 Muscle protein {ECO:0000256|ARBA:ARBA00023179, KW ECO:0000256|RuleBase:RU251113}; KW Oxygen transport {ECO:0000256|ARBA:ARBA00022621, ECO:0000256|PROSITE- KW ProRule:PRU00238}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE- KW ProRule:PRU00238}. FT DOMAIN 1..110 FT /note="Globin family profile" FT /evidence="ECO:0000259|PROSITE:PS01033" FT BINDING 54 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 83 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" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAC69245.1" FT NON_TER 110 FT /evidence="ECO:0000313|EMBL:AAC69245.1" SQ SEQUENCE 110 AA; 11630 MW; B43B5865F0E6708F CRC64; VLKCWGPMEA DYATHGGLVL TRLFTEHPET LKLFPKFAGI AHGDLAGDAG VSAHGATVLN KLGDLLKARG AHAALLKPLS SSHATKHKIP IINFKLIAEV IGKVMEEKAG //