IF2H_RAT
ID IF2H_RAT Reviewed; 472 AA.
AC C9WPN6; A0A096MIV4; A0A0G2JU42; C9WPN7; W8CEN7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3, Y-linked;
DE EC=3.6.5.3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma, Y-linked;
DE Short=eIF-2-gamma Y;
GN Name=Eif2s3y;
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].
RX PubMed=24759410; DOI=10.1038/nature13151;
RA Cortez D., Marin R., Toledo-Flores D., Froidevaux L., Liechti A.,
RA Waters P.D., Gruetzner F., Kaessmann H.;
RT "Origins and functional evolution of Y chromosomes across mammals.";
RL Nature 508:488-493(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/Mcwi; TISSUE=Embryonic spleen;
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 [4]
RP IDENTIFICATION OF EIF2S3 HOMOLOGS.
RX PubMed=9736774; DOI=10.1093/hmg/7.11.1725;
RA Ehrmann I.E., Ellis P.S., Mazeyrat S., Duthie S., Brockdorff N.,
RA Mattei M.-G., Gavin M.A., Affara N.A., Brown G.M., Simpson E.,
RA Mitchell M.J., Scott D.M.;
RT "Characterization of genes encoding translation initiation factor eIF-
RT 2gamma in mouse and human: sex chromosome localization, escape from X-
RT inactivation and evolution.";
RL Hum. Mol. Genet. 7:1725-1737(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-290 AND 349-472.
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=20333173; DOI=10.1093/gbe/evp001;
RA Pink C.J., Swaminathan S.K., Dunham I., Rogers J., Ward A., Hurst L.D.;
RT "Evidence that replication-associated mutation alone does not explain
RT between-chromosome differences in substitution rates.";
RL Genome Biol. Evol. 1:13-22(2009).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=25548914; DOI=10.1371/journal.pone.0115792;
RA Huby R.D., Glaves P., Jackson R.;
RT "The incidence of sexually dimorphic gene expression varies greatly between
RT tissues in the rat.";
RL PLoS ONE 9:E115792-E115792(2014).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B (By similarity). Along with its paralog on
CC chromosome X, may contribute to spermatogenesis up to the round
CC spermatid stage (By similarity). {ECO:0000250|UniProtKB:P32481,
CC ECO:0000250|UniProtKB:Q9Z0N2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: The eukaryotic translation initiation factor 2 complex/eIF2 is
CC a heterotrimer composed of an alpha subunit, also called subunit 1
CC (encoded by EIF2S1), a beta subunit, also called subunit 2 (encoded by
CC EIF2S2) and a gamma subunit, also called subunit 3 (encoded by 2
CC homologous genes Eif2s3x and Eif2s3y). {ECO:0000250|UniProtKB:P41091}.
CC -!- TISSUE SPECIFICITY: Widely expressed in males.
CC {ECO:0000269|PubMed:25548914}.
CC -!- MISCELLANEOUS: Has a homolog on chromosome X (Eif2s3x).
CC {ECO:0000269|PubMed:9736774}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; GATN01000003; JAC06680.1; -; mRNA.
DR EMBL; AABR07038871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC242953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC158736; AAI58737.1; -; mRNA.
DR EMBL; FJ775731; ACX55123.1; -; mRNA.
DR EMBL; FJ775732; ACX55124.1; -; mRNA.
DR RefSeq; NP_001161138.1; NM_001167666.1.
DR AlphaFoldDB; C9WPN6; -.
DR SMR; C9WPN6; -.
DR IntAct; C9WPN6; 1.
DR jPOST; C9WPN6; -.
DR PRIDE; C9WPN6; -.
DR Ensembl; ENSRNOT00000088593; ENSRNOP00000068958; ENSRNOG00000060048.
DR GeneID; 100312984; -.
DR KEGG; rno:100312984; -.
DR CTD; 26908; -.
DR RGD; 2314438; Eif2s3y.
DR GeneTree; ENSGT00550000074801; -.
DR OMA; FESCKMK; -.
DR OrthoDB; 903135at2759; -.
DR PRO; PR:C9WPN6; -.
DR Proteomes; UP000002494; Chromosome Y.
DR Bgee; ENSRNOG00000060048; Expressed in thymus and 18 other tissues.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
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 Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; GTP-binding; Hydrolase; Initiation factor; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT CHAIN 2..472
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3, Y-linked"
FT /id="PRO_0000435884"
FT DOMAIN 39..247
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 48..55
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 76..80
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 134..137
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 190..193
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 225..227
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 51..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 190..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 225..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0N1"
FT CONFLICT 39
FT /note="Q -> K (in Ref. 1; JAC06680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51154 MW; B28023BB0F52AD85 CRC64;
MAGGEAGVTL GQPHLSRQDL ATLDVTKLTP LSHEIISRQA TINIGTIGHV AHGKSTVVKA
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDSSCPRPE CYRSCGSSTP DEFPSDIPGI
KGNFRLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV
KKIPVPLRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTID DE
