GO_REF:0000002

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000003

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000024

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000033

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000107

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000116

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000117

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

GO_REF:0000121

GO reference used by source annotation pipeline

Source annotation pipeline provenance; biological support was assessed from UniProt and cached literature where available.

"GO_REF entry used to trace source annotation method rather than as primary biological evidence."

PMID:10648842

Hepatic epidermal growth factor-regulated mitogen-activated protein kinase kinase kinase activity in the rat: lack of identity with known forms of raf and MEKK.

Araf evidence concern: the paper detects A-Raf protein but does not positively identify A-Raf as the EGF-sensitive hepatic MEK kinase.

"Western immunoblotting confirmed that Raf-1, A-Raf, B-Raf, MEKK1 and MEKK2 were present at similar levels in E19 and adult liver. However, specific immunoprecipitation kinase assays did not detect any kinases that could account for marked EGF sensitivity or the higher level of activity in E19 fetuses."

PMID:22609986

PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12.

In human cells, ARAF (but not BRAF or CRAF) is required for Galpha12-induced RFFL upregulation and PRR5L ubiquitination; source of the TOR-signaling and proteasomal-catabolism annotations transferred to rat Araf.

"Knockdown of ARAF, but not BRAF or CRAF, by siRNAs inhibited Gα12QL-mediated upregulation of RFFL expression and polyubiquitination of PRR5L"

PMID:9779826

Expression of mitogen-activated protein kinase pathways during postnatal development of rat heart.

Raf/MAPK pathway components are documented in rat heart development, supporting MAPK signaling context by traceable author statement rather than a direct Araf kinase assay.

"Expression of mitogen-activated protein kinase pathways during postnatal development of rat heart."

Reactome:R-RNO-188339

Reactome pathway annotation

Reactome pathway annotation provenance; used as traceable context rather than primary experimental support.

"Reactome pathway annotation"

file:rat/Araf/Araf-deep-research-falcon.md

Falcon deep research report: rat Araf (A-Raf proto-oncogene serine/threonine-protein kinase, UniProt P14056)

Falcon synthesis confirms rat Araf/P14056 is a RAF-family Ser/Thr kinase acting as an upstream node in the canonical RAS->RAF->MEK->ERK MAPK cascade, with RAFs acting as MEK kinases that phosphorylate and activate MEK1/2.

"Araf encodes a RAF-family serine/threonine kinase that functions as an upstream node in the canonical **RAS→RAF→MEK→ERK** MAPK cascade."
Falcon notes A-Raf is repeatedly characterized as a comparatively weak/low-activity MEK kinase relative to B-Raf, so its physiological roles may be more context- and scaffolding-dependent.

"However, multiple sources emphasize that **A‑Raf has comparatively low MEK kinase activity** relative to B‑Raf"
Falcon describes canonical RAF localization - cytosolic inactive monomers recruited to the plasma membrane upon RAS-GTP engagement, supporting plasma membrane and cytosol localization annotations.

"RAF family members are described as cytosolic in the inactive state and recruited to the **plasma membrane** upon RAS‑GTP engagement as part of activation."
Falcon reports context-dependent A-Raf mitochondrial localization (with MST2) in tumor contexts, supporting the mitochondrion annotation as inference for the rat ortholog from broader ARAF biology.

"A‑Raf has been reported to localize to **mitochondria** (together with MST2) in tumor contexts"
Falcon describes a kinase-independent A-Raf function - binding MST2 and suppressing MST2-mediated apoptosis - supporting the negative regulation of apoptotic process annotation.

"A‑Raf is described as binding **MST2** and suppressing MST2-mediated apoptosis, indicating kinase-independent pathway crosstalk."
Falcon highlights a non-catalytic mechanism whereby ARAF increases RAS-GTP by antagonizing NF1 (a RasGAP) binding to RAS, positioning A-Raf as a regulator of the RAS node in addition to acting downstream.

"**ARAF can increase RAS‑GTP by antagonizing NF1 (a RasGAP) binding to RAS**, thereby reducing NF1-stimulated GTP hydrolysis."
Rat-specific evidence - A-Raf protein (P14056) is upregulated in rat retina two weeks after partial optic nerve transection, consistent with RAF/MAPK roles in survival/stress signaling.

"In rat retina two weeks after partial optic nerve transection, integrated SWATH and targeted MRM proteomics quantified **A‑Raf (P14056)** as **upregulated** in the temporal quadrant with **ratio 1.55**, **log2FC ~0.63**, **p = 0.04**."