CYGB_RAT
ID CYGB_RAT Reviewed; 190 AA.
AC Q921A4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytoglobin;
DE AltName: Full=Histoglobin;
DE Short=HGb;
DE AltName: Full=Stellate cell activation-associated protein;
GN Name=Cygb; Synonyms=Stap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 5-12 AND 36-44.
RC TISSUE=Liver;
RX PubMed=11320098; DOI=10.1074/jbc.m102630200;
RA Kawada N., Kristensen D.B., Asahina K., Nakatani K., Minamiyama Y.,
RA Seki S., Yoshizato K.;
RT "Characterization of a stellate cell activation-associated protein (STAP)
RT with peroxidase activity found in rat hepatic stellate cells.";
RL J. Biol. Chem. 276:25318-25323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May have a protective function during conditions of oxidative
CC stress. May be involved in intracellular oxygen storage or transfer.
CC Plays a role in the development of liver fibrosis. Has a peroxidase
CC activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Stellate cells and liver.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ245663; CAC59827.1; -; mRNA.
DR EMBL; BC088455; AAH88455.1; -; mRNA.
DR RefSeq; NP_570100.1; NM_130744.2.
DR AlphaFoldDB; Q921A4; -.
DR SMR; Q921A4; -.
DR STRING; 10116.ENSRNOP00000016067; -.
DR PhosphoSitePlus; Q921A4; -.
DR SwissPalm; Q921A4; -.
DR jPOST; Q921A4; -.
DR PaxDb; Q921A4; -.
DR PRIDE; Q921A4; -.
DR Ensembl; ENSRNOT00000016067; ENSRNOP00000016067; ENSRNOG00000011541.
DR GeneID; 170520; -.
DR KEGG; rno:170520; -.
DR CTD; 114757; -.
DR RGD; 69415; Cygb.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000155004; -.
DR HOGENOM; CLU_003827_10_1_1; -.
DR InParanoid; Q921A4; -.
DR OMA; ETQRAWT; -.
DR OrthoDB; 1379813at2759; -.
DR PhylomeDB; Q921A4; -.
DR TreeFam; TF332967; -.
DR Reactome; R-RNO-203615; eNOS activation.
DR Reactome; R-RNO-8981607; Intracellular oxygen transport.
DR PRO; PR:Q921A4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011541; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q921A4; baseline and differential.
DR Genevisible; Q921A4; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0004096; F:catalase activity; IDA:RGD.
DR GO; GO:0047888; F:fatty acid peroxidase activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IDA:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:RGD.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IDA:RGD.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:RGD.
DR GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Cytoglobin"
FT /id="PRO_0000053386"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 17..167
FT /note="Globin"
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 190 AA; 21497 MW; 7EC3CB390DCEC804 CRC64;
MEKVPGDMEI ERRERNEELS EAERKAVQAT WARLYANCED VGVAILVRFF VNFPSAKQYF
SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE
PMYFKILSGV ILDVIAEEFA NDFPVETQKA WTKLRGLIYS HVTAAYKEVG WVQQVPNTTT
LPATLPSSGP
