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Database: UniProt
Entry: A0A2R9CMV9_PANPA
LinkDB: A0A2R9CMV9_PANPA
Original site: A0A2R9CMV9_PANPA 
ID   A0A2R9CMV9_PANPA        Unreviewed;       556 AA.
AC   A0A2R9CMV9;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819, ECO:0000256|PIRNR:PIRNR017222};
DE            Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
GN   Name=EIF2A {ECO:0000313|Ensembl:ENSPPAP00000042423.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000042423.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000042423.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000042423.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC       number of specific mRNAs. Acts by directing the binding of methionyl-
CC       tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC       binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC       whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC       GTP-dependent manner. {ECO:0000256|ARBA:ARBA00003993,
CC       ECO:0000256|PIRNR:PIRNR017222}.
CC   -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC       {ECO:0000256|ARBA:ARBA00009573, ECO:0000256|PIRNR:PIRNR017222}.
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DR   EMBL; AJFE02092671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02092672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02092673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02092674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9CMV9; -.
DR   Ensembl; ENSPPAT00000065353.1; ENSPPAP00000042423.1; ENSPPAG00000043784.1.
DR   GeneTree; ENSGT00730000111053; -.
DR   Proteomes; UP000240080; Chromosome 3.
DR   Bgee; ENSPPAG00000043784; Expressed in placenta and 6 other cell types or tissues.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011387; TIF2A.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR   PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   PIRSF; PIRSF017222; eIF2A; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000256|PIRNR:PIRNR017222};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|PIRNR:PIRNR017222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW   ECO:0000256|PIRNR:PIRNR017222}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          193..382
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          405..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  61870 MW;  DB989B8AC6896BC4 CRC64;
     MAPSTPLLTV RGSEGLYMVN GPPHFTESTV FPRESGKNCK VYTFSKDGTL FAWGNGEKVN
     IISVTNKGLL HSFDLPKAVC LEFSPKNTVL ATWQPYTTSK DGTAGIPNLQ LYDVKTGTCL
     KSFIQKKMQN WCPSWSEDET LCARSVNNEV HFFENNNFNT IANKLHLQKI NDFVLSPGPQ
     PYKVAVYVPG SKDKVTMLWN KKATAVLVIA STDVDKTGAS YYGEQTLHYI ATNGESAVVQ
     LPKNGPIYDV VWNSSSTEFC AVYGFMPAKA TIFNLKCDPV FDFGTGPRNA AYYSPHGHIL
     VLAGFGNLRG QMEVWDVKNY KLISKPVASD STYFAWCPDG EHILTATCAP RLRVNNGYKI
     WHYTGSILHK YDVPSNAELW QVSWQPFLDG IFPAKTITYQ AVPSEVPNEE PKVATAYRPP
     ALRNKPITNS KLHEEEPPQN MKPQSGNDKP LSKTALKNQR KHEAKKAAKQ EARSDRSPDL
     APTPAPQSTP RNTVSQSISG DPEIDKKIKN LKKKLKAIEQ LKEQAATGKQ LEKNQLEKIQ
     KETALLQELE DLELGI
//
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