BIT2 (YBR270C) curation notes
Journal-style working notes for the AI GO-annotation review of Saccharomyces cerevisiae BIT2.
Provenance is recorded inline as [PMID:xxxx "verbatim supporting text"] or [source "..."].
BIT2-specific evidence is kept strictly separate from evidence about its paralog BIT61.
Identity (from UniProt P38346 / SGD S000000474)
- UniProt: P38346, entry name
BIT2_YEAST, 545 aa, 61.2 kDa.
- RecName: "Probable target of rapamycin complex 2 subunit BIT2" (Short: "TORC2 subunit BIT2");
AltName "Binding partner of TOR2 protein 2".
- Systematic name: YBR270C (chromosome II); ORF name YBR1738; SGD:S000000474; GeneID 852573.
- Evidence at protein level (PE1). Reference proteome UP000002311.
- Sequence note: the protein is largely low-complexity; UniProt annotates two disordered regions
(residues 1–24 and 78–166) with polar-residue compositional bias (MobiDB-lite). The globular
portion is C-terminal (roughly residues ~170–545), which is where the Pfam HbrB match lies.
Family / domain (inline domain analysis of the UniProt record)
- Pfam PF08539 (HbrB), InterPro IPR013745 (Bit61/PRR5), PANTHER PTHR32428
("TARGET OF RAPAMYCIN COMPLEX 2 SUBUNIT BIT61-RELATED"), subfamily PTHR32428:SF2.
- PANTHER family members (
interpro/panther/PTHR32428/PTHR32428-entries.csv) place BIT2 in the
same SF2 subfamily as:
- S. cerevisiae BIT61 (P47041) — the WGD paralog (also SF2);
- S. pombe bit61 (O74547) and SPAC6B12.03c (O14208);
- and the mammalian/vertebrate orthologs are the PRR5 / PRR5L proteins (Proline-rich
protein 5 / 5-like; SF3/SF4), i.e. Protor-1 / Protor-2, the accessory regulatory
subunits of mTORC2.
So the whole family is the fungal Bit61/Bit2 ↔ metazoan PRR5/Protor lineage of TORC2/mTORC2
accessory subunits. This orthology is the strongest grounding for "TORC2 subunit".
- The HbrB/Bit61-PRR5 domain has no known catalytic activity; PRR5/Protor are described as
accessory/regulatory (non-catalytic) subunits. There is no nucleotide-binding, kinase, or other
enzymatic motif in the sequence. Consistent with an accessory/scaffolding subunit, not an
enzyme. This underlies the MF-dark call below.
KNOWN about BIT2 specifically (BIT2, not BIT61)
- BIT2 is a subunit of TORC2 (part of the TOR complex 2).
- GOA:
GO:0031932 TORC2 complex, IDA, PMID:15689497, assigned by SGD (part_of). This is the
experimental anchor for complex membership.
- The TORC2 subunit inventory in the cryo-EM paper explicitly names BIT2 as an alternative
paralog subunit: PMID:29170376. NOTE: TORC2 contains Bit61 or Bit2 — the two paralogs are alternative,
largely interchangeable accessory subunits of the same complex.
- BIT2 physically interacts with TORC2 components / effectors.
- UniProt SUBUNIT: "Interacts with the target of rapamycin complex 2 (TORC2) subunit TSC11 and
the TORC2 effectors SLM1 and SLM2." {ECO:0000269|PubMed:11283351, ECO:0000269|PubMed:15689497}.
- These are the physical-interaction data (Ito et al. 2001 genome-wide two-hybrid PMID:11283351;
Fadri et al. 2005 PMID:15689497) that place BIT2 in the TORC2/Slm1-Slm2 interaction network.
- CAUTION: PMID:15689497 is cached abstract-only (
full_text_available: false); its abstract
foregrounds Slm1/Slm2 binding Avo2 and Bit61 PMID:15689497. The BIT2 IDA to
TORC2 complex is attributed by the SGD curator to this paper, so the BIT2-specific data are in
the full text / figures that I cannot see. Per project rules I do NOT remove or downgrade the
experimental IDA on the basis that the abstract names the paralog.
- Non-essential; viable null. bit2Δ is viable in S288C; high-throughput phenotyping reports
decreased resistance to oxidative stress and to a farnesyltransferase inhibitor (SGD phenotype
summary, high-throughput screens) [https://yeastgenome.org/locus/S000000474]. No strong,
specific single-mutant growth phenotype is documented, consistent with paralog redundancy with
BIT61.
KNOWN about the paralog BIT61 (kept separate — do NOT attribute to BIT2)
- The cryo-EM TORC2 structure was solved from TORC2 purified via Bit61-TAP in a bit2Δ strain;
the structural placement ("Finger2", the acute angle of the rhombohedron, contact with Avo3) is
therefore for Bit61, not BIT2: PMID:29170376 and PMID:29170376. I will NOT
cite the Finger2/edge placement as BIT2 evidence — only the general "Bit61 or its paralog Bit2 is
a TORC2 subunit" statement is BIT2-applicable.
- BIT61 (YJL058C, P47041) has its own SGD phenotypes (decreased competitive fitness on minimal/SC
media, decreased resistance to acid pH, elevated chromosome loss) — these are BIT61, not BIT2.
NOT known about BIT2 (the knowledge gaps)
- BIT2's specific molecular activity within TORC2 is undefined. The Bit61/PRR5 (HbrB) domain
has no catalytic activity; BIT2 is an accessory/regulatory subunit whose molecular contribution
(does it modulate substrate selection? complex stability? localization? effector, e.g. Slm1/Slm2,
engagement?) has not been demonstrated for BIT2 specifically. GOA already flags this: the SGD MF
annotation is GO:0003674 molecular_function ND (no data).
- BIT2's non-redundant function vs BIT61 is unknown. TORC2 contains "Bit61 or its paralog Bit2";
whether the two paralogs are functionally distinct (differential expression, condition-specific
incorporation, distinct effector bias) or fully redundant is not established. No bit2Δ bit61Δ
double-mutant phenotype is annotated at SGD.
- No strong single-mutant loss-of-function phenotype pins down a BIT2-specific biological role;
the reported phenotypes are high-throughput sensitivities (oxidative stress; farnesyltransferase
inhibitor), not a mechanistic assignment.
GOA annotations to review (7 rows in BIT2-goa.tsv)
GO:0007163 establishment or maintenance of cell polarity — IBA (GO_REF:0000033), involved_in.
Phylogenetic (IBA). TORC2/Slm-actin axis does regulate polarized growth/actin, so this is
plausible at the family level but is a downstream/process-level inference, not BIT2-specific
experimental data. → KEEP_AS_NON_CORE (family/process-level, not core BIT2 activity).
GO:0019887 protein kinase regulator activity — IBA (GO_REF:0000033), enables. IBA-projected MF.
BIT2 as a TORC2 accessory subunit plausibly contributes to regulating the Tor2 kinase, but there
is no BIT2 experimental MF; "regulator of the kinase" via being part of the complex is the family
rationale. This is the least uninformative MF available. → KEEP_AS_NON_CORE (IBA family MF; not an
independently demonstrated BIT2 activity; better captured as contributes_to at the complex level).
GO:0031932 TORC2 complex — IBA (GO_REF:0000033), part_of. → ACCEPT (redundant with the IDA row
but phylogenetically well-supported; core).
GO:0038203 TORC2 signaling — IBA (GO_REF:0000033), involved_in. → ACCEPT/KEEP (core BP; TORC2
membership implies participation in TORC2 signaling).
GO:0031932 TORC2 complex — IDA, PMID:15689497, part_of. → ACCEPT (experimental anchor;
core). Defer to SGD curator; do not REMOVE despite abstract-only cache foregrounding Bit61.
GO:0038203 TORC2 signaling — IC (inferred from GO:0031932 complex membership),
PMID:15689497, involved_in. → ACCEPT (IC directly from the experimental complex membership; core).
GO:0003674 molecular_function — ND (GO_REF:0000015), enables. Root MF, no data. → ACCEPT/KEEP
(honestly reflects that BIT2's specific MF is undetermined — the MF-dark gap; this is the correct
use of ND, not a defect).
Core function synthesis
- Core: BIT2 is an accessory (non-catalytic) subunit of TORC2, the rapamycin-insensitive TOR
complex 2 (Tor2, Lst8, Avo1, Avo2, Avo3/Tsc11, and Bit61-or-Bit2). It participates in TORC2
signaling. Membership is experimental (IDA) and phylogenetically supported (IBA); orthology to
metazoan PRR5/Protor (accessory mTORC2 subunits) corroborates an accessory/regulatory role.
- MF: best expressed as contributes_to a TORC2/kinase-regulatory activity rather than an
independently enabled activity; BIT2's own biochemical activity is unknown (MF-dark).
- Because BIT2 is one of two interchangeable paralog subunits, its individual functional weight is
intrinsically hard to pin down (redundancy with BIT61).
Deep-research provider status
Automated deep research was attempted twice via just deep-research-falcon yeast BIT2
--fallback perplexity-lite. Both attempts failed: the falcon provider timed out/was killed
(exit 143/144) and the perplexity-lite fallback returned HTTP 401 (API quota exceeded). No
-deep-research-{provider}.md file was produced, and none was fabricated. This review is
therefore grounded directly in the UniProt record (P38346), the GOA TSV, the cached primary
literature (PMID:15689497, PMID:11283351, PMID:29170376), the PANTHER/InterPro family record
(PTHR32428 / IPR013745 / PF08539), and the SGD locus page — all cited with provenance above.
References gathered / cached
- PMID:15689497 — Fadri et al. 2005, Mol Biol Cell (abstract-only cache). IDA anchor for TORC2
complex membership; SLM1/SLM2 interaction. relevance HIGH.
- PMID:11283351 — Ito et al. 2001, PNAS (full text cached; genome-wide two-hybrid). Physical
interaction data underlying the TSC11/SLM1/SLM2 interactions in UniProt SUBUNIT. relevance MEDIUM
(systematic screen; BIT2 data in supplementary interaction tables, not discussed in body text).
- PMID:29170376 — Karuppasamy et al. 2017, Nat Commun (full text cached). Cryo-EM TORC2 structure.
Establishes the "Bit61 or its paralog Bit2" subunit inventory (BIT2-applicable). CAUTION: all
structural placement is for Bit61 (purified from bit2Δ), NOT BIT2. relevance MEDIUM.
- SGD locus page S000000474 — phenotype/paralog summary (viable null; oxidative-stress &
farnesyltransferase-inhibitor sensitivities; WGD paralog BIT61).
- GO_REF:0000015 (ND policy), GO_REF:0000033 (phylogenetic IBA) — method references.