The Oxygen-Regulated Protein (ORP) Family
An oxygen regulated protein, the parental member of this family, is of 2156 aas in length with possibly as many as 3 hydrophobic regions long enough to be TMSs, one at residue 210, one at residue 1130 and one at residue 1250. It is also called microtubule-associated protein, and it regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells and plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.
References:
The Oxygen-Regulated Protein, ORP, protein of 2156 aas in length with possibly as many as 3 hydrophobic regions long enough to be TMSs, one at residue 210, one at residue 1130 and one at residue 1250. It is also called microtubule-associated protein, and it regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells and plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.
ORP of Homo sapiens
Retinitis pigmentosa 1-like 1 protein isoform X48 of 2364 aas and possibly 0 TMSs.
RP1 isoforms X48 of Accipiter gentilis (Northern goshawk)
Uncharacterized protein of 1875 aas. This protein shows 4 regions of sequence similarity with TC# 9.B.449.1.2. Regions 1 and 2 in both proteins are in the same order, but regions 3 and 4 are inverted as revealed using TC BLAST. This could be real or atifacual doe to sequencing errors.
UP of Ovis aries
Dehydrin ERD10, LTI (low temperature induced) protein, designated LTI29, LTI45 and LTI49, of 260 aas and 0 TMSs. Chaperone activities of ERD10 and ERD14, two disordered stress-related plant proteins, have been documented (Kovacs et al. 2008).
ERD10 of Arabidopsis thaliana
Dehydrin, ERD14, of 185 aas with 0 TMSs. It is an intrinsically disordered protein acting as a chaperone which prevents heat-induced aggregation and/or inactivation of various substrates, and it binds to acidic phospholipid vesicles without affecting membrane fluidity (Kovacs et al. 2008).
ERD14 of Arabidopsis thaliana