H2F2_TRYB2
ID H2F2_TRYB2 Reviewed; 267 AA.
AC Q584U2; D6XHU7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=REH2-associated factor 2 {ECO:0000303|PubMed:26769962};
DE Flags: Precursor;
GN Name=H2F2 {ECO:0000303|PubMed:26769962};
GN ORFNames=Tb927.6.2140 {ECO:0000312|EMBL:AAX80847.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|EMBL:AAX80847.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAX80847.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAZ11776.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ11776.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [3] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE REH2C COMPLEX, INTERACTION WITH THE GRBC
RP COMPLEX; RECC COMPLEX; REMC COMPLEX, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000269|PubMed:26769962};
RX PubMed=26769962; DOI=10.1074/jbc.m115.708164;
RA Kumar V., Madina B.R., Gulati S., Vashisht A.A., Kanyumbu C., Pieters B.,
RA Shakir A., Wohlschlegel J.A., Read L.K., Mooers B.H.M., Cruz-Reyes J.;
RT "REH2C Helicase and GRBC Subcomplexes May Base Pair through mRNA and Small
RT Guide RNA in Kinetoplastid Editosomes.";
RL J. Biol. Chem. 291:5753-5764(2016).
CC -!- FUNCTION: May play a role in mitochondrial mRNA editing by facilitating
CC the association of the gRNA-binding (GRBC) complex with the RNA editing
CC core (RECC) complex (PubMed:26769962). However, appears to be
CC dispensable for mRNA editing per se (PubMed:26769962).
CC {ECO:0000269|PubMed:26769962}.
CC -!- SUBUNIT: Component of the REH2-associated complex (REH2C) composed of
CC helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various
CC editing stages; the formation of the complex is RNA-independent
CC (PubMed:26769962). Interacts with various editing complexes including
CC the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex
CC (also known as the MRB1 complex) and the RNA editing mediator (REMC)
CC complex (PubMed:26769962). {ECO:0000269|PubMed:26769962}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26769962}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the procyclic stage (at protein
CC level). {ECO:0000269|PubMed:26769962}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the procyclic stage
CC does not cause defects in RHE2 interaction with H2F1 or their
CC association with components of the RECC and GRBC editing complexes;
CC however, causes a slight decrease in the association of the GRBC
CC complex with the RECC complex (PubMed:26769962). No defect in
CC mitochondrial mRNA editing (PubMed:26769962).
CC {ECO:0000269|PubMed:26769962}.
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DR EMBL; AC074259; AAX80847.1; -; Genomic_DNA.
DR EMBL; CP000069; AAZ11776.1; -; Genomic_DNA.
DR RefSeq; XP_845335.1; XM_840242.1.
DR AlphaFoldDB; Q584U2; -.
DR PaxDb; Q584U2; -.
DR GeneID; 3657848; -.
DR KEGG; tbr:Tb927.6.2140; -.
DR VEuPathDB; TriTrypDB:Tb927.6.2140; -.
DR eggNOG; ENOG502RZ8Q; Eukaryota.
DR InParanoid; Q584U2; -.
DR OMA; GSRFPFY; -.
DR Proteomes; UP000008524; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031019; C:mitochondrial mRNA editing complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IBA:GO_Central.
DR GO; GO:0000963; P:mitochondrial RNA processing; IC:GeneDB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; mRNA processing; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..267
FT /note="REH2-associated factor 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5010844239"
SQ SEQUENCE 267 AA; 28771 MW; A25992DD65EA35D5 CRC64;
MFRWSWCRLI ISKVSAESYV DYLQNSDREL PALSEIFPRH GTGTGELVKF HSLLCEAMKD
HNFNYVGIKV VPPTSPPLQC LRATEPVCVP IFSNSFQGSV FSAKQHRIQF VEPLFVIRLG
RDPPTQLTAN TVPAVCDAFF PGVEFVGSRY PFYPPHTTGF AADLGGCVAV HLGEAVSLGS
ASLESLGDTN FVVTRREEPI QVGAGKNCLG GPGAAVALAV SYAASMGWPL REKHYIFCSG
VGSRSPALAG EYKVNYGAYG SVSASLT
