CYGB2_DANRE
ID CYGB2_DANRE Reviewed; 179 AA.
AC Q575S8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cytoglobin-2;
GN Name=cygb2 {ECO:0000312|ZFIN:ZDB-GENE-060920-1};
GN Synonyms=cygb-2 {ECO:0000312|EMBL:CAG25612.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAG25612.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16199220; DOI=10.1016/j.bbrc.2005.08.271;
RA Fuchs C., Luckhardt A., Gerlach F., Burmester T., Hankeln T.;
RT "Duplicated cytoglobin genes in teleost fishes.";
RL Biochem. Biophys. Res. Commun. 337:216-223(2005).
CC -!- FUNCTION: May have a protective function during conditions of oxidative
CC stress. May be involved in intracellular oxygen storage or transfer.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q921A4}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, with highest
CC levels in brain and eye, and considerably lower levels in skin, gut,
CC heart, gill, liver and muscle. {ECO:0000269|PubMed:16199220}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ635229; CAG25612.1; -; mRNA.
DR AlphaFoldDB; Q575S8; -.
DR SMR; Q575S8; -.
DR STRING; 7955.ENSDARP00000120009; -.
DR PaxDb; Q575S8; -.
DR Ensembl; ENSDART00000187763; ENSDARP00000148052; ENSDARG00000114471.
DR Ensembl; ENSDART00000188886; ENSDARP00000152544; ENSDARG00000109892.
DR ZFIN; ZDB-GENE-060920-1; cygb2.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_10_1_1; -.
DR InParanoid; Q575S8; -.
DR OMA; ETQRAWT; -.
DR PhylomeDB; Q575S8; -.
DR TreeFam; TF332967; -.
DR Reactome; R-DRE-203615; eNOS activation.
DR Reactome; R-DRE-8981607; Intracellular oxygen transport.
DR PRO; PR:Q575S8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0098809; F:nitrite reductase activity; IDA:ZFIN.
DR GO; GO:0019825; F:oxygen binding; IDA:ZFIN.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR013314; Globin_lamprey/hagfish.
DR PANTHER; PTHR46783; PTHR46783; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR01906; FISHGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW Transport.
FT CHAIN 1..179
FT /note="Cytoglobin-2"
FT /id="PRO_0000262322"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 17..167
FT /note="Globin"
FT /evidence="ECO:0000255"
FT BINDING 81
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:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 113
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:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 179 AA; 20598 MW; EF7CFE95E34D41EF CRC64;
MEKEREDEET EGRERPEPLT DVERGIIKDT WARVYASCED VGVTILIRFF VNFPSAKQYF
SQFQDMEDPE EMEKSSQLRK HARRVMNAIN TVVENLHDPE KVSSVLVLVG KAHAFKYKVE
PIYFKILSGV ILEILAEEFG ECFTPEVQTS WSKLMAALYW HITGAYTEVG WVKLSSSAV