HBS1L_RAT
ID HBS1L_RAT Reviewed; 679 AA.
AC Q6AXM7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=HBS1-like protein;
GN Name=Hbs1l;
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway. In the presence of ABCE1 and PELO, is required for
CC 48S complex formation from 80S ribosomes and dissociation of vacant 80S
CC ribosomes. Together with PELO and in presence of ABCE1, recognizes
CC stalled ribosomes and promotes dissociation of elongation complexes
CC assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of
CC the mRNA, a mechanism to release non-functional ribosomes and to
CC degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway.
CC {ECO:0000250|UniProtKB:Q9Y450}.
CC -!- SUBUNIT: Interacts with the SKI complex.
CC {ECO:0000250|UniProtKB:Q9Y450}.
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; BC079463; AAH79463.1; -; mRNA.
DR RefSeq; NP_001011934.1; NM_001011934.1.
DR AlphaFoldDB; Q6AXM7; -.
DR SMR; Q6AXM7; -.
DR STRING; 10116.ENSRNOP00000019734; -.
DR iPTMnet; Q6AXM7; -.
DR PhosphoSitePlus; Q6AXM7; -.
DR jPOST; Q6AXM7; -.
DR PaxDb; Q6AXM7; -.
DR Ensembl; ENSRNOT00000019734; ENSRNOP00000019734; ENSRNOG00000014531.
DR GeneID; 293408; -.
DR KEGG; rno:293408; -.
DR CTD; 10767; -.
DR RGD; 1308509; Hbs1l.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_007265_3_6_1; -.
DR InParanoid; Q6AXM7; -.
DR OMA; SVEDEHC; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q6AXM7; -.
DR Reactome; R-RNO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:Q6AXM7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014531; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; Q6AXM7; baseline and differential.
DR Genevisible; Q6AXM7; RN.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
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; 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 Acetylation; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Translation regulation.
FT CHAIN 1..679
FT /note="HBS1-like protein"
FT /id="PRO_0000091494"
FT DOMAIN 253..477
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 171..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..269
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 318..322
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 339..342
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 401..404
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 440..442
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 200..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 339..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 401..404
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 617
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
SQ SEQUENCE 679 AA; 74774 MW; 51D18EB5E8999A73 CRC64;
MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDNPEE EYGYEDLKES
SNSLLNHQLS EIDQARLYSC LDHMREVLGD AVPDDILTEA ILKHKFDVQK ALSVVLEQDG
VQTLKEKSER AVCAGQPSKV ISRSSQSESE IVPKVAKMTV SGKKQTMGFE VPGLPSEENG
HNVRAPYKGP PGDDVSIASP NVPETGTPKS TAHPPSLQTS EELGCTPTPL RKSGKLRQQI
DVKAGLEKRQ GGKQLLNLVV IGHVDAGKST LMGHMLYLLG NVNKRTMHKY EQESKKAGKA
SFAYAWVLDE TGEERERGVT MDVGMTKFET TTKVVTLMDA PGHKDFIPNM ITGAAQADVA
VLVVDASRGE FEAGFETGGQ TREHGLLVRS LGVTQLAVAV NKMDQVNWQQ ERFQEITGKL
GHFLKQAGFK ESDVAFIPTS GLSGENLTSR SQSSDLTKWY KGLCLLEQID SFKPPQRSID
KPFRLCVSDV FKDQGSGFCV TGKIEAGYVQ TGDRLLAMPP NETCTAKGIT LHDEPVDWAA
AGDHVSLTLV GMDIIKINVG CIFCGPKEPI KACTRFRARI LIFNIEVPIT KGFPVLLHYQ
TVSEPAVIKR LISVLNKSTG EVTKKKPKLL TKGQNALVEL QTQRPVALEL YKDFKELGRF
MLRYGGSTVA AGVVTEIKE
