GLOB6_CAEEL
ID GLOB6_CAEEL Reviewed; 389 AA.
AC Q18086;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Globin-like protein 6 {ECO:0000303|PubMed:20518498};
GN Name=glb-6 {ECO:0000312|EMBL:CCD65109.1, ECO:0000312|WormBase:C18C4.9};
GN ORFNames=C18C4.9;
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:CCD65109.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD65109.1};
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 TISSUE SPECIFICITY.
RX PubMed=18844991; DOI=10.1186/1471-2148-8-279;
RA Hoogewijs D., De Henau S., Dewilde S., Moens L., Couvreur M., Borgonie G.,
RA Vinogradov S.N., Roy S.W., Vanfleteren J.R.;
RT "The Caenorhabditis globin gene family reveals extensive nematode-specific
RT radiation and diversification.";
RL BMC Evol. Biol. 8:279-279(2008).
RN [4] {ECO:0000305, ECO:0000312|PDB:3MVC}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 195-355 IN COMPLEX WITH HEME, AND
RP FUNCTION.
RX PubMed=20518498; DOI=10.1021/bi100710a;
RA Yoon J., Herzik M.A., Winter M.B., Tran R., Olea C., Marletta M.A.;
RT "Structure and properties of a bis-histidyl ligated globin from
RT Caenorhabditis elegans.";
RL Biochemistry 49:5662-5670(2010).
CC -!- FUNCTION: May play a role as physiological sensor for oxygen via redox
CC signaling and/or electron transport. {ECO:0000269|PubMed:20518498}.
CC -!- TISSUE SPECIFICITY: Expressed in the head and tail neurons and nerve
CC cord. {ECO:0000269|PubMed:18844991}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages.
CC {ECO:0000269|PubMed:17916248}.
CC -!- INDUCTION: By anoxia. {ECO:0000269|PubMed:17916248}.
CC -!- MISCELLANEOUS: Does not bind carbon monoxide (CO), nitric oxide (NO) or
CC CN(-). {ECO:0000269|PubMed:20518498}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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; FO080608; CCD65109.1; -; Genomic_DNA.
DR RefSeq; NP_504469.1; NM_072068.4.
DR PDB; 3MVC; X-ray; 1.40 A; A/B=195-355.
DR PDBsum; 3MVC; -.
DR AlphaFoldDB; Q18086; -.
DR SMR; Q18086; -.
DR BioGRID; 47625; 2.
DR STRING; 6239.C18C4.9; -.
DR EPD; Q18086; -.
DR PaxDb; Q18086; -.
DR EnsemblMetazoa; C18C4.9.1; C18C4.9.1; WBGene00015969.
DR GeneID; 182780; -.
DR KEGG; cel:CELE_C18C4.9; -.
DR UCSC; C18C4.9; c. elegans.
DR CTD; 182780; -.
DR WormBase; C18C4.9; CE29586; WBGene00015969; glb-6.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_710267_0_0_1; -.
DR InParanoid; Q18086; -.
DR OMA; NIWRQVY; -.
DR OrthoDB; 874789at2759; -.
DR EvolutionaryTrace; Q18086; -.
DR PRO; PR:Q18086; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00015969; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
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.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..389
FT /note="Globin-like protein 6"
FT /id="PRO_0000422180"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 286
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:3MVC"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 244..267
FT /evidence="ECO:0007829|PDB:3MVC"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:3MVC"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:3MVC"
FT HELIX 325..352
FT /evidence="ECO:0007829|PDB:3MVC"
SQ SEQUENCE 389 AA; 43527 MW; 529C672CD4D859F2 CRC64;
MGNQSTKSTH GTTRVSHSKS AHHNSSRVTS DVIPRSASAI SSHERFFSDS QSSSPPAVCP
VSAPGKYRNF PGKDVPPICL TDEYNNSDDE VFCSTRTSKQ SPLATGCPRQ NLGSPGNRRS
VDSTNSDLLE AVTPRSHISV KRTVSSGTEH APDHANMQKS SSLKFTRPGV RSETKETTPS
TSSNPTMFPC IHQFLHLTQP QILFVRKTWN HARNQGALEP AISIFRNSFF KNPEIRQMIM
FGTKNEGHER LKKHAQLFTV LMDDLIANLD SPSATVAGLR EAGEKHVWPT RNQYGCPFHA
HLLDQFATAM IERTLEWGEK KDRTETTQRG WTKIVLFVTE QLKEGFQDEQ KRARRIKAQI
KTSAGSSSFE ISTKTKQSDM KRFHTLDNM
