IRX10L notes (IRX10 family review, 2026-10-29)

Deep research

just deep-research-falcon ARATH IRX10L --fallback perplexity-lite failed in this
session (no provider available: "Provider 'perplexity' not available"). The review
rests on the cached primary literature listed below, read directly.

The IRX10 clade (GT47)

Arabidopsis has two members, IRX10 (At1g27440, Q9FZJ1) and IRX10-L (At5g61840,
Q940Q8), in the exostosin-related GT47 family PTHR11062. PANTHER puts them in
different subfamilies: IRX10 in SF370 ("BETA-1,4-XYLOSYLTRANSFERASE IRX10-RELATED")
and IRX10L in SF200 ("BETA-1,4-XYLOSYLTRANSFERASE IRX10L-RELATED"), which in the
local PTHR11062 entries table also holds rice Os01g0926700 (Q8S1X7) and moss
GT47A (A9RGD8). Both are xylan backbone beta-1,4-xylosyltransferases (xylan
synthases).

IRX10L-specific

Curation issues found (shared with the paralog)

  1. GO:0080116 glucuronoxylan glucuronosyltransferase activity (IMP, PMID:18980662,
    on both genes; IBA on IRX10L from PTN001667002) is the wrong MF. The paper
    reports loss of beta(1,4) xylosyltransferase activity. GlcA transfer is done by
    GT8 GUX enzymes PMID:26043357. MODIFY to GO:0047517;
    recorded as a TAIR source defect. The term probably stems from the GUT1/GUT2
    aliases (after tobacco NpGUT1).
  2. GO:0009101 glycoprotein biosynthetic process (InterPro2GO, IPR004263) does not
    apply to plant xylan synthases; removed.
  3. IRX10L rows citing PMID:25141999 as IMP (cell wall biogenesis) and IDA (Golgi
    apparatus): the paper is in vitro biochemistry only and cites Sogaard et al.
    2012 for topology. Terms kept/refined, evidence-code defects recorded.
  4. UniProt naming (now recorded as UNIPROT source_defects on the GO:0080116 IMP row): both Q9FZJ1 and Q940Q8 carry the alt names "Glucuronoxylan
    glucuronosyltransferase 1/2" (AtGUT1/AtGUT2), and the IRX10 FUNCTION text says
    "especially in the formation of GlcUA side chain of xylans". Both are legacy and
    conflict with the direct biochemistry. Worth reporting to UniProt.
  5. Topology: UniProt models residues 1-21/2-22 as a type II signal anchor, while
    Wu et al. 2009 and Urbanowicz et al. 2014 describe a signal peptide; AoIRX10 is
    described as lumenal and held by IRX9/IRX14. Golgi membrane kept as the
    location; the anchoring mechanism is left as a question.