PMID:21633110(https://pubmed.ncbi.nlm.nih.gov/21633110/), DOI 10.1091/mbc.E11-02-0157, directly establishes GTP-dependent Rap1 effector binding and junctional recruitment. PMID:17916086(https://pubmed.ncbi.nlm.nih.gov/17916086/) supports microtubule/PIP2 interactions. PMID:23317506(https://pubmed.ncbi.nlm.nih.gov/23317506/) gives the ICAP1 competition structure, and PMID:20332120(https://pubmed.ncbi.nlm.nih.gov/20332120/) links CCM1 to VE-cadherin/Par polarity organization. These supply the molecular scaffold mechanism, independently of the Falcon synthesis. The early PMID:9285558 two-hybrid speculation that KRIT1 might regulate Krev-1 does not establish GEF/GAP catalysis; use the directly demonstrated small-GTPase binding function.
PMID:20616044(https://pubmed.ncbi.nlm.nih.gov/20616044/) reports inhibition of endothelial proliferation, apoptosis, migration, lumen formation and sprouting. The same biology supports the broad horse developmental-process GOA rows, but does not establish spermatogenic piRNA production. ROS/FOXO1/SOD2 effects in PMID:20668652(https://pubmed.ncbi.nlm.nih.gov/20668652/) are regulatory phenotypes rather than intrinsic redox catalysis.
The horse record is719 aa and aligns at 98.5% identity across 719 paired residues to736 aa human KRIT1. The N-terminal interaction motifs and C-terminal FERM scaffold are retained; see the full alignment for the internal 17 aa gap. The initial horse search returned studies mentioning conserved KRIT1 structures but no horse-specific functional assay. Human Falcon research is complete; no separate horse Edison was selected.