GLB26_CAEEL
ID GLB26_CAEEL Reviewed; 183 AA.
AC Q22663;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Globin-like protein 26 {ECO:0000303|PubMed:17916248};
GN Name=glb-26 {ECO:0000312|EMBL:CAA99921.1, ECO:0000312|WormBase:T22C1.2};
GN ORFNames=T22C1.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA99921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA99921.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:17916248};
RX PubMed=17916248; DOI=10.1186/1471-2164-8-356;
RA Hoogewijs D., Geuens E., Dewilde S., Vierstraete A., Moens L.,
RA Vinogradov S., Vanfleteren J.R.;
RT "Wide diversity in structure and expression profiles among members of the
RT Caenorhabditis elegans globin protein family.";
RL BMC Genomics 8:356-356(2007).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP HEME-BINDING.
RX PubMed=20361867; DOI=10.1186/1471-2091-11-17;
RA Geuens E., Hoogewijs D., Nardini M., Vinck E., Pesce A., Kiger L., Fago A.,
RA Tilleman L., De Henau S., Marden M.C., Weber R.E., Van Doorslaer S.,
RA Vanfleteren J., Moens L., Bolognesi M., Dewilde S.;
RT "Globin-like proteins in Caenorhabditis elegans: in vivo localization,
RT ligand binding and structural properties.";
RL BMC Biochem. 11:17-17(2010).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=21674044; DOI=10.1371/journal.pone.0020478;
RA Kiger L., Tilleman L., Geuens E., Hoogewijs D., Lechauve C., Moens L.,
RA Dewilde S., Marden M.C.;
RT "Electron transfer function versus oxygen delivery: a comparative study for
RT several hexacoordinated globins across the animal kingdom.";
RL PLoS ONE 6:E20478-E20478(2011).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, EPR SPECTROSCOPY,
RP NUCLEAR LOCALIZATION SIGNAL, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF
RP GLY-2.
RX PubMed=23251335; DOI=10.1371/journal.pone.0048768;
RA Tilleman L., De Henau S., Pauwels M., Nagy N., Pintelon I., Braeckman B.P.,
RA De Wael K., Van Doorslaer S., Adriaensen D., Timmermans J.P., Moens L.,
RA Dewilde S.;
RT "An N-myristoylated globin with a redox-sensing function that regulates the
RT defecation cycle in Caenorhabditis elegans.";
RL PLoS ONE 7:E48768-E48768(2012).
CC -!- FUNCTION: Plays a role in electron transport. Utilizes the bis-histidyl
CC hexacoordinated complex with iron to transfer electrons to cytochrome c
CC and molecular oxygen. Plays a regulatory role in the periodicity of the
CC defecation cycle under oxidative stress conditions. Not involved in
CC imparting protection against general conditions of oxidative stress.
CC May participate in redox reactions under anaerobic conditions.
CC {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:21674044,
CC ECO:0000269|PubMed:23251335}.
CC -!- SUBUNIT: Homodimer. Occurs in an equilibrium of monomeric and dimeric
CC forms in solution. {ECO:0000269|PubMed:20361867,
CC ECO:0000269|PubMed:21674044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20361867,
CC ECO:0000269|PubMed:23251335}. Nucleus lamina
CC {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Cell
CC membrane {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}.
CC Note=Transported to the nucleus by myristoylation of the N-terminal
CC glycine. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}.
CC -!- TISSUE SPECIFICITY: Detected in the head mesodermal cell. In the tail
CC region, detected in the stomatointestinal and anal depressor muscle
CC cells. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, but
CC expression relative to adult is decreased in the L3 and dauer stages.
CC {ECO:0000269|PubMed:17916248, ECO:0000269|PubMed:20361867}.
CC -!- INDUCTION: Up-regulated by anoxia but not affected by hypoxia.
CC {ECO:0000269|PubMed:17916248, ECO:0000269|PubMed:20361867}.
CC -!- MISCELLANEOUS: Binds carbon monoxide (CO).
CC {ECO:0000269|PubMed:20361867}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255}.
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DR EMBL; Z75550; CAA99921.1; -; Genomic_DNA.
DR PIR; T25102; T25102.
DR RefSeq; NP_492188.1; NM_059787.3.
DR AlphaFoldDB; Q22663; -.
DR SMR; Q22663; -.
DR STRING; 6239.T22C1.2; -.
DR iPTMnet; Q22663; -.
DR PaxDb; Q22663; -.
DR EnsemblMetazoa; T22C1.2.1; T22C1.2.1; WBGene00011913.
DR GeneID; 172564; -.
DR KEGG; cel:CELE_T22C1.2; -.
DR UCSC; T22C1.2; c. elegans.
DR CTD; 172564; -.
DR WormBase; T22C1.2; CE06490; WBGene00011913; glb-26.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_099983_0_0_1; -.
DR InParanoid; Q22663; -.
DR OMA; NAWRHMS; -.
DR OrthoDB; 1497077at2759; -.
DR PhylomeDB; Q22663; -.
DR PRO; PR:Q22663; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011913; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR CDD; cd01040; Mb-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleus; Oxygen transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23251335"
FT CHAIN 2..183
FT /note="Globin-like protein 26"
FT /evidence="ECO:0000269|PubMed:20361867"
FT /id="PRO_0000422159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23251335"
FT BINDING 77
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9NPG2"
FT BINDING 109
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9NPG2"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:23251335"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation and transport to
FT nucleus."
FT /evidence="ECO:0000269|PubMed:23251335"
SQ SEQUENCE 183 AA; 21057 MW; 88D04980508BED63 CRC64;
MGSSTSTPAP PPKKNKPEGR KADNQILNSY QKSIVRNAWR HMSQKGPSNC GSTITRRMMA
RKSTIGDILD RSTLDYHNLQ IVEFLQKVMQ SLDEPDKISK LCQEIGQKHA KYRRSKGMKI
DYWDKLGEAI TETIREYQGW KIHRESLRAA TVLVSYVVDQ LRFGYSRGLH VQGSRETKED
DEE
