HBS1_DROME
ID HBS1_DROME Reviewed; 670 AA.
AC Q9W074; Q86NR4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein HBS1 {ECO:0000305};
GN Name=HBS1 {ECO:0000312|FlyBase:FBgn0042712};
GN ORFNames=CG1898 {ECO:0000312|FlyBase:FBgn0042712};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAO41445.1, ECO:0000312|EMBL:ADA53579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO41445.1};
RA Stapleton M., Booth B., Brokstein P., Hong L., Agbayani A., Carlson J.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PELO, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26124316; DOI=10.15252/embr.201540084;
RA Yang F., Zhao R., Fang X., Huang H., Xuan Y., Ma Y., Chen H., Cai T.,
RA Qi Y., Xi R.;
RT "The RNA surveillance complex Pelo-Hbs1 is required for transposon
RT silencing in the Drosophila germline.";
RL EMBO Rep. 16:965-974(2015).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PELO, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30824860; DOI=10.1038/s41598-019-39530-6;
RA Li Z., Yang F., Xuan Y., Xi R., Zhao R.;
RT "Pelota-interacting G protein Hbs1 is required for spermatogenesis in
RT Drosophila.";
RL Sci. Rep. 9:3226-3226(2019).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (By similarity). In the presence of pix and pelo,
CC is required for 48S complex formation from 80S ribosomes and
CC dissociation of vacant 80S ribosomes (By similarity). Together with
CC pelo and in presence of pix, recognizes stalled ribosomes and promotes
CC dissociation of elongation complexes assembled on non-stop mRNAs; this
CC triggers endonucleolytic cleavage of the mRNA, a mechanism to release
CC non-functional ribosomes and to degrade damaged mRNAs as part of the
CC No-Go Decay (NGD) pathway (By similarity). Together with pelo, required
CC for transposon silencing in the ovary and testis (PubMed:26124316).
CC Together with pelo, promotes meiosis and spermatid individualization
CC during spermatogenesis (PubMed:30824860).
CC {ECO:0000250|UniProtKB:Q9Y450, ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:30824860}.
CC -!- SUBUNIT: Interacts with pelo. {ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:30824860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30824860}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level).
CC {ECO:0000269|PubMed:26124316}.
CC -!- DISRUPTION PHENOTYPE: In germlines, increases transposable elements
CC transcription at both mRNA and protein levels (PubMed:26124316).
CC Results in male sterility: male testes are morphologically normal but
CC no mature sperm is formed (PubMed:30824860). Results in defective
CC meiosis and spermatid individualization during spermatogenesis
CC (PubMed:30824860). {ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:30824860}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AE014296; AAF47584.2; -; Genomic_DNA.
DR EMBL; AE014296; AHN57931.1; -; Genomic_DNA.
DR EMBL; BT003766; AAO41445.1; -; mRNA.
DR EMBL; BT120040; ADA53579.1; -; mRNA.
DR RefSeq; NP_001286906.1; NM_001299977.1.
DR RefSeq; NP_652729.2; NM_144472.4.
DR AlphaFoldDB; Q9W074; -.
DR SMR; Q9W074; -.
DR IntAct; Q9W074; 4.
DR STRING; 7227.FBpp0072745; -.
DR PaxDb; Q9W074; -.
DR PRIDE; Q9W074; -.
DR DNASU; 117365; -.
DR EnsemblMetazoa; FBtr0072866; FBpp0072745; FBgn0042712.
DR EnsemblMetazoa; FBtr0345807; FBpp0311793; FBgn0042712.
DR GeneID; 117365; -.
DR KEGG; dme:Dmel_CG1898; -.
DR UCSC; CG1898-RA; d. melanogaster.
DR CTD; 117365; -.
DR FlyBase; FBgn0042712; HBS1.
DR VEuPathDB; VectorBase:FBgn0042712; -.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_007265_3_6_1; -.
DR InParanoid; Q9W074; -.
DR OMA; SVEDEHC; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q9W074; -.
DR Reactome; R-DME-429958; mRNA decay by 3' to 5' exoribonuclease.
DR SignaLink; Q9W074; -.
DR BioGRID-ORCS; 117365; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 117365; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0042712; Expressed in testis and 30 other tissues.
DR ExpressionAtlas; Q9W074; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0007291; P:sperm individualization; IGI:UniProtKB.
DR GO; GO:0048137; P:spermatocyte division; IGI:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR037189; HBS1-like_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF109732; SSF109732; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Translation regulation.
FT CHAIN 1..670
FT /note="Protein HBS1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451922"
FT DOMAIN 245..468
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..261
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 310..314
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 331..334
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 393..396
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 432..434
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 556
FT /note="S -> N (in Ref. 3; AAO41445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 74165 MW; 769A30A1771F76D6 CRC64;
MSRHRIVRTM DYNDEYDGYD DIYGHSVEDE HCISPTDAQQ WLYDRARGQQ SISAFISKNK
DIQEEEADED EDEDAAFAKA RRDSESFQMP QLDEIEQAKL SSCVDEVRSV VGDAVSERRI
VETSMKFDYD MQKILDEILN EETNKSAKPA VNKMKAPAAP VLPKTVSKTV PTPPPKISLK
EPRRGFEIPS PKVPSSPVVS GRNTPVDISA GDDISRSSAT VFKVSKEQAV RNARQLYEKE
RADQKSHIHM IVIGHVDAGK STLMGHLLYD TGNVSQRVMH KHEQESKKLG KQSFMYAWVL
DETGEERARG ITMDVGQSRI ETKTKIVTLL DAPGHKDFIP NMISGATQAD VALLVVDATR
GEFESGFELG GQTREHAILV RSLGVNQLGV VINKLDTVGW SQDRFTEIVT KLKSFLKLAG
FKDSDVSFTP CSGLTGENLT KKAQEPALTN WYSGRHLLDV IENFKIPERA IDRPLRMSVS
DIYKGTGSGF CISGRVETGV LCLNDKVLVG ASREQAQVKS LTMNEFPQTC VFAGDQVSVT
LPALDINNVT VGCIISDPQT PIPVTTRFQA RIIVFNVKVP ITMGFPVLLH HQSLIEPAVV
CKLTASIHKS TGEVVKKKPR CLGNNSCALV ELETSRPICI ERYADFKELG RVMLRVAGVT
IAAGMVTKIR
