ID   EIF2D_BOVIN             Reviewed;         579 AA.
AC   Q58CR3; Q29RI3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Eukaryotic translation initiation factor 2D;
DE            Short=eIF2d;
DE   AltName: Full=Ligatin;
GN   Name=EIF2D; Synonyms=LGTN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC       the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC       binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC       the P-site of 40S ribosomes, the situation that takes place during
CC       initiation complex formation on some specific RNAs. Its activity in
CC       tRNA binding with 40S subunits does not require the presence of the
CC       aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC       (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC       its role in initiation, can promote release of deacylated tRNA and mRNA
CC       from recycled 40S subunits following ABCE1-mediated dissociation of
CC       post-termination ribosomal complexes into subunits (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
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DR   EMBL; BT021884; AAX46731.1; -; mRNA.
DR   EMBL; BC114158; AAI14159.1; -; mRNA.
DR   RefSeq; NP_001030276.1; NM_001035104.1.
DR   AlphaFoldDB; Q58CR3; -.
DR   SMR; Q58CR3; -.
DR   STRING; 9913.ENSBTAP00000013769; -.
DR   PaxDb; Q58CR3; -.
DR   PRIDE; Q58CR3; -.
DR   GeneID; 511844; -.
DR   KEGG; bta:511844; -.
DR   CTD; 1939; -.
DR   eggNOG; KOG2522; Eukaryota.
DR   HOGENOM; CLU_012487_2_0_1; -.
DR   InParanoid; Q58CR3; -.
DR   OrthoDB; 401807at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR   CDD; cd11608; eIF2D_C; 1.
DR   InterPro; IPR039757; EIF2D.
DR   InterPro; IPR039759; eIF2D_SUI1.
DR   InterPro; IPR041366; Pre-PUA.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR12217; PTHR12217; 1.
DR   Pfam; PF17832; Pre-PUA; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF47592; SSF47592; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS50296; SUI1; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..579
FT                   /note="Eukaryotic translation initiation factor 2D"
FT                   /id="PRO_0000130610"
FT   DOMAIN          93..173
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT   DOMAIN          378..462
FT                   /note="SWIB/MDM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT   DOMAIN          486..559
FT                   /note="SUI1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT   REGION          222..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
SQ   SEQUENCE   579 AA;  63647 MW;  92215E1B03493AE0 CRC64;
     MFAKAFRVKS NTAIKGSDRR KLRADVAAVF PTLGTDQVSE LVPGKEELNI VKLYAHRGDA
     VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVVP
     PAGLPQVQKG DLCAVALVGN RAPVAVGVAA MSTAEMLASG LKGRGFCVLH SYQDHLWRSG
     DKSSPPSIAP LALNPPDLSE GKGCVKADTA LQGAMRQLTL EEEVQQRCEE KSPSEATEDP
     GPGGLHVDPM DSKTLQEQMD ELLQTCFLHA LKCSVRKADL PLLTSTLLGS HMFSCCPEGR
     QLDIKKSSYK KLSKFLQHMQ QEQIIQVQEL SKGVESIVAV DWKHPRITSF VIPEPSPTSQ
     TIQEGSREQP YHPPDIKPLY CVPASMTLLF QESGHKKGSV LEGSEVRTFV INYAKKNDLV
     DADNKNLVKL DPILCDCILE KDEQHTVTKL PWDSLLGRCL EKLQPAYQVT FPGQEPIVKK
     GRICPIDITL AQKASNKKVT VVRNLEAYGL DPRSVAATLQ QRCQASTTVT SAPGLKDSVQ
     VQIQGNQIHH LGRLLLEEYR LPRKHIQGLE KAPKPGKKK