H2F1_TRYB2
ID H2F1_TRYB2 Reviewed; 524 AA.
AC Q585P3; D6XHQ1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=REH2-associated factor 1 {ECO:0000303|PubMed:26769962};
DE Flags: Precursor;
GN Name=H2F1 {ECO:0000303|PubMed:26769962};
GN ORFNames=Tb927.6.1680 {ECO:0000312|EMBL:AAX79728.1};
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:AAX79728.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAX79728.1};
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 (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAZ11730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ11730.1};
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 AND REH2, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL 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).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE REH2C COMPLEX, INTERACTION WITH THE GRBC
RP COMPLEX; RECC COMPLEX AND REMC COMPLEX, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000269|PubMed:31034523};
RX PubMed=31034523; DOI=10.1371/journal.pone.0211525;
RA Kumar V., Doharey P.K., Gulati S., Meehan J., Martinez M.G., Hughes K.,
RA Mooers B.H.M., Cruz-Reyes J.;
RT "Protein features for assembly of the RNA editing helicase 2 subcomplex
RT (REH2C) in Trypanosome holo-editosomes.";
RL PLoS ONE 14:e0211525-e0211525(2019).
CC -!- FUNCTION: Plays an important role in mitochondrial mRNA editing by
CC promoting the assembly of the mRNA editosome (PubMed:26769962,
CC PubMed:31034523). Facilitates the recruitment of mRNA to the REH2C
CC complex and promotes the interaction between various editing complexes
CC including REH2C, GRBC, REMC and RECC complexes (PubMed:26769962,
CC PubMed:31034523). {ECO:0000269|PubMed:26769962,
CC ECO:0000269|PubMed:31034523}.
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, PubMed:31034523). Within the complex, interacts with
CC REH2; the interaction is direct (PubMed:26769962). Interacts with
CC various editing complexes including the RNA editing core (RECC)
CC complex, the gRNA-binding (GRBC) complex (also known as the MRB1
CC complex) and the RNA editing mediator (REMC) complex (PubMed:26769962,
CC PubMed:31034523). {ECO:0000269|PubMed:26769962,
CC ECO:0000269|PubMed:31034523}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26769962,
CC ECO:0000269|PubMed:31034523}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the procyclic stage (at protein
CC level). {ECO:0000269|PubMed:26769962, ECO:0000269|PubMed:31034523}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the procyclic stage
CC causes a reduction in mitochondrial mRNA editing (PubMed:26769962).
CC Formation of the REH2C complex is not affected but REH2C complex
CC association with the GRBC, REMC, RECC complexes and with and pre-mRNA
CC is impaired (PubMed:26769962). Integrity of the GRBC complex is not
CC affected but GRBC complex association with the RECC complex and pre-
CC mRNA is reduced (PubMed:26769962). Causes a slight decrease in REH2
CC protein levels (PubMed:26769962, PubMed:31034523). Does not affect the
CC RNA unwinding activity of the REH2C complex (PubMed:26769962).
CC {ECO:0000269|PubMed:26769962, ECO:0000269|PubMed:31034523}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX79728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAZ11730.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013353; AAX79728.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000069; AAZ11730.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_845289.1; XM_840196.1.
DR AlphaFoldDB; Q585P3; -.
DR PaxDb; Q585P3; -.
DR GeneID; 3657804; -.
DR KEGG; tbr:Tb927.6.1680; -.
DR eggNOG; ENOG502RW3S; Eukaryota.
DR InParanoid; Q585P3; -.
DR OMA; HVAKDHP; -.
DR Proteomes; UP000008524; Chromosome 6.
DR GO; GO:0031019; C:mitochondrial mRNA editing complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000963; P:mitochondrial RNA processing; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:GeneDB.
DR GO; GO:0006396; P:RNA processing; IDA:GeneDB.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Metal-binding; Mitochondrion; mRNA processing; Reference proteome; Repeat;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..524
FT /note="REH2-associated factor 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455619"
FT ZN_FING 48..70
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255"
FT ZN_FING 121..147
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255"
FT ZN_FING 226..249
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..312
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255"
FT ZN_FING 334..357
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..399
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..429
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 443..465
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 463..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 58050 MW; 122FE01BA3554D9E CRC64;
MRRWLVASMA PQLHQLLQPV RRCHHPLRIP SVQLAAPRSH THEDIAYASC PACSRVVHMC
DMLTHLITAH RELDQTHCRK MCTERLALYE RVIGVPLKKS ELTSSGRRVL DFLPTVLPTG
YMCNWCDRRS DVYATRDKFL KHVADVHTDI DLEEVEPHVP LPPRGVVVEK SNGDGGPQPT
RRLNGVVAVA EKSEPINAVP RILGISLPRG VDRPLKATAQ FSDTEFPCEL CNRTFNSEID
LLQHLETRHP DGTAEGPAGV DSAAIADVAQ FSAKEATTGG DQRVHVICDL CVSSSKVYKM
PSALFSHIRF KHPNEDAAFH VERLIREQKT VSSFVCTVCQ KAFASAAALD GHFNSKHAEQ
GEAQNVVGRV TANNCWWCHD CEKGFSSAKG LHGHMQNKHG LSSQTHPCPA CKRVFADIYS
LEEHLSLQHK TIRLSDIGLL THVKCSTCER FFLSHEDLHR HAVKHHKKDP RAPAQPFEAP
TSASHVAAST SAAVPSEVEA TASPQGPRKV KKRKKTTEVS EVTS
