SRPR alpha

The NG domain region, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the signal recognition particle (SRP) complex subunit SRP54 (PubMed:34020957). The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (PubMed:34020957). GTPase induced rearrangement of SR drives SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957).

Component of the signal recognition particle (SRP) complex receptor (SR) (PubMed:16439358). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (PubMed:16675701, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit SRP54 (PubMed:34020957). SRP receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957).

Belongs to the GTP-binding SRP family.

• Endoplasmic reticulum membrane
• Peripheral membrane protein
• Cytoplasmic side
• Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain.

SRPR, SRPRA, Signal recognition particle receptor subunit alpha, SR-alpha, Docking protein alpha, DP-alpha

• entrezGene:6734
• omim:182180
• swissprot:P08240

Proteins

Metabolism

69811Da