ID O57410_CHAGU Unreviewed; 103 AA. AC O57410; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Myoglobin {ECO:0000256|ARBA:ARBA00019044, ECO:0000256|RuleBase:RU251113}; OS Champsocephalus gunnari (Mackerel icefish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Champsocephalus. OX NCBI_TaxID=52237 {ECO:0000313|EMBL:AAC64482.1}; RN [1] {ECO:0000313|EMBL:AAG16642.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Heart ventricle {ECO:0000313|EMBL:AAG16642.1}; RA Vayda M.E., Yuan M.-L., Small D.J., Costello L., Sidell B.D.; RT "Extreme conservation of the myoglobin gene among Antarctic notothenioid RT fishes."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAC64482.1} RP NUCLEOTIDE SEQUENCE. 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; AF006611; AAC64482.1; -; Genomic_DNA. DR EMBL; U71054; AAG16642.1; -; mRNA. DR AlphaFoldDB; O57410; -. 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|RuleBase:RU000356}; KW Iron {ECO:0000256|RuleBase:RU251113}; KW Metal-binding {ECO:0000256|RuleBase:RU251113}; KW Muscle protein {ECO:0000256|ARBA:ARBA00023179, KW ECO:0000256|RuleBase:RU251113}; KW Oxygen transport {ECO:0000256|ARBA:ARBA00022621, KW ECO:0000256|RuleBase:RU000356}; Transport {ECO:0000256|RuleBase:RU000356}. FT DOMAIN 7..91 FT /note="Globin family profile" FT /evidence="ECO:0000259|PROSITE:PS01033" FT REGION 80..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..103 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 103 AA; 10732 MW; DAACCBCC4A1F99FB CRC64; MADFDMVLKC WGPVEADHAT HGSLVLTRLF TEHPETLKLF PKFAGIAHGD LAGDAGVSAH GATVLNKLGD LLKARGAHAA LPKPLSSSHA TPPSTRSPLL TSS //