Proteins undergo translation with the help of ribosomes, which can be found in either cytoplasm or on the rough endoplasmic reticulum (rough ER). Proteins synthesized on the ribosomes in cytoplasm are destined for somewhere inside the cell. On the other hand, proteins synthesized on the rough ER are processed in the ER and Golgi apparatus and are transported to the membrane or the extracellular matrix. Since the protein in the question is found on a membrane, it must have been synthesized on the ribosomes on the rough ER.  

Recall that all three types of RNA are used in translation. mRNA is the template strand used to synthesize the protein molecule. It contains the information regarding the sequence of amino acids in the protein molecule. tRNA is involved in transporting the amino acid to the growing polypeptide chain. rRNA molecules make up the ribosomes, the location of translation.

Polymerase enzymes are used in DNA replication (DNA polymerase) and transcription (RNA polymerase). They are not involved in translation.

Translation begins when a start codon is recognized in the mRNA molecule. The start codon is AUG, which codes for the amino acid methionine; therefore, all proteins begin with methionine. There are multiple stop codons; therefore, the ending of proteins could be different from one another.

Note that the question is asking about the state of a protein molecule after the completion of translation. A protein can undergo further processing events in the rough ER and Golgi apparatus during which the starting methionine may be cleaved; therefore, the ultimate end product of proteins might have a different starting amino acid.

Like transcription, there are slight differences between prokaryotic and eukaryotic translation. In prokaryotes transcription and translation are coupled and occur in the cytoplasm. Recall that in eukaryotes, translation can occur either in the cytoplasm or on the rough ER. Membrane and secretory proteins are synthesized in ribosomes on the rough ER whereas the cytosolic proteins are synthesized in ribosomes in cytoplasm.

The start codon for both prokaryotic and eukaryotic translation is AUG. This codes for the amino acid methionine, which is usually the first amino acid added to a growing polypeptide chain.

As mentioned, coupling of transcription and translation only occurs in the prokaryotes. Eukaryotic transcription occurs in the nucleus and the products need to undergo post-transcriptional modification before entering the cytoplasm for translation; therefore, the two processes aren’t coupled in eukaryotes.

Every protein begins with methionine, therefore, this will be found in all proteins upon completion of translation. Recall that this methionine might be excised when the protein is further processed in eukaryotes.

5' AUG 3' is the start codon for polypeptide synthesis and corresponds to the amino acid methionine.

All nucleotide triplets can theoretically occur in translation. The genetic code is basically universal to all species, except for mitochondria, which create proteins independently from the cell. Each codon translates to an amino acid, a stop codon, or a start codon (which is also an amino acid, methionine). There are indeed 64 possible combinations of the nucleotides, by rules of combinatorics. The 5' terminal is written on the left, as a convention among biologists.

There are three tRNA binding sites -- A, P, and E (for Aminoacyl, Peptidyl, and Exit) -- but only one mRNA binding site. The enzyme which bonds amino acids carried by tRNAs at A and P is indeed called peptidyl transferase. tRNA is held at A and P when its anticodon matches the codon of the mRNA to be translated. Because each codon is three codons long, per amino acid, the mRNA is indeed shifted three nucleotides' length through the ribosome, each time an amino acid is added to the growing chain.

Among the amino acids, there are two which only have one codon that code for them: tryptophan (UGG), and methionine. Methionine, is, of course, special among them, because the same codon is also the start codon -- AUG. Aspartic acid, asparagine, tyrosine, and phenylalanine all each have two possible corresponding codons (respectively: GAC/GAU, AAC/AAU, UAC/UAU, and UUC/UUU).

eIF2B is a GEF (guanine nucleotide exchange factor) for eIF1 eIF2. 

eEF1A first binds to the aminoacyl-tRNA and has GTPase activity. eEF1B is a GEF for eEF1A. eEF2 has the elongation role similar to EF-G in prokaryotes. Neither Ran-GTP nor IP3 are elongation factors.