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Database: UniProt
Entry: EIF2D_BOVIN
LinkDB: EIF2D_BOVIN
Original site: EIF2D_BOVIN 
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   30-AUG-2017, entry version 77.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC       manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC       finds its position in the P-site of 40S ribosomes, the situation
CC       that takes place during initiation complex formation on some
CC       specific RNAs. Its activity in tRNA binding with 40S subunits does
CC       not require the presence of the aminoacyl moiety. Possesses the
CC       unique ability to deliver non-Met (elongator) tRNAs into the P-
CC       site of the 40S subunit. In addition to its role in initiation,
CC       can promote release of deacylated tRNA and mRNA from recycled 40S
CC       subunits following ABCE1-mediated dissociation of post-termination
CC       ribosomal complexes into subunits (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
DR   EMBL; BT021884; AAX46731.1; -; mRNA.
DR   EMBL; BC114158; AAI14159.1; -; mRNA.
DR   RefSeq; NP_001030276.1; NM_001035104.1.
DR   UniGene; Bt.59019; -.
DR   ProteinModelPortal; 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   eggNOG; ENOG410XSAV; LUCA.
DR   HOVERGEN; HBG006268; -.
DR   InParanoid; Q58CR3; -.
DR   KO; K15027; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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   GO; GO:0002192; P:IRES-dependent translational initiation of linear mRNA; IBA:GO_Central.
DR   Gene3D; 1.10.245.10; -; 1.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.30.780.10; -; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
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.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Initiation factor;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    579       Eukaryotic translation initiation factor
FT                                2D.
FT                                /FTId=PRO_0000130610.
FT   DOMAIN       93    173       PUA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00161}.
FT   DOMAIN      486    559       SUI1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00200}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P41214}.
FT   MOD_RES     232    232       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P41214}.
FT   MOD_RES     356    356       Phosphoserine.
FT                                {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
//
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