MYO7A (human, Q13402, USH1B) — curation notes

Journal of research done while reviewing the GOA annotations. Provenance is given inline
as [PMID:NNNN "verbatim quote"] or [file:...] where a quote comes from a cached
publication or the deep-research report.

1. Identity and architecture

Unconventional myosin-VIIa, HGNC:7606, disease alias USH1B. Domain layout: N-terminal
motor domain, neck with five IQ motifs, a single-alpha-helix (SAH) lever-arm extension,
then a long tail of two MyTH4-FERM modules separated by an SH3 domain.

PMID:21687988

PMID:11964381

The InterPro FERM/Band-4.1 signatures on this entry therefore describe the cargo-binding
tail, not an acyl-CoA-binding enzyme — worth noting because the deep-research prompt
listed only FERM domains.

2. Motor biochemistry — the human protein

Heissler & Manstein characterised the isolated human motor domain fused to an artificial
lever arm. The key facts for annotation are a rate-limiting ADP release step, high duty
ratio, and high F-actin affinity:

PMID:21687988

PMID:21687988

PMID:21687988

PMID:21687988

Free Mg2+ in the physiological range switches the motor between cargo-moving and
tension-bearing modes. This is the biochemical basis for treating MYO7A as a
tension-holding motor rather than a fast transporter, and it justifies ACCEPTing
GO:0000146, GO:0051015, GO:0005524 and GO:0030048 as core.

Caveat recorded in the reference review: the construct is a motor domain plus artificial
lever arm, so these numbers describe the motor module, not the autoinhibited full-length
molecule. Full-length human MYO7A is monomeric and folded until cargo adaptors open it
(Holló et al. 2023, JBC 299:105243, via the deep-research report; not separately cached).

The functionally decisive site is the UTLD of mature stereocilia, not the base:

PMID:21709241

PMID:21709241

PMID:21709241

The tripartite MYO7A–sans(USH1G)–harmonin-b(USH1C) complex was demonstrated by
co-transfection in COS7 cells; the hair-cell localisation is rodent. Hence the new
GO:1990435 annotation was entered as ISS rather than IDA for the human protein.

This is a tension-bearing complex of the mature bundle — deliberately distinguished in
the review from the transient ankle-link/USH2 complex of developing bundles.

UniProt states the same network at the level of function:
"Motor protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and
MYO7A that mediates mechanotransduction in cochlear hair cells."
(MYO7A-uniprot.txt, FUNCTION block, ECO:0000269|PubMed:21709241.)

4. RPE — melanosomes, phagosomes, lysosomes

MYRIP is the RAB27A effector that couples melanosomes to the motor:

PMID:11964381

PMID:11964381

PMID:11964381

Human loss-of-function evidence for the melanosome role (basis for the NEW GO:0032400
annotation, IMP):

PMID:19643958

PMID:19643958

Note the direction of the effect: the motor constrains long-range (microtubule-driven)
movement, i.e. it captures and retains melanosomes on apical cortical actin. That is why
GO:0032400 melanosome localization was preferred over GO:0032402 melanosome transport.

Lysosomes:

PMID:16001398

PMID:16001398

The same paper summarises the phagosome literature: myosin-VIIa is not needed for ROS
binding or ingestion, only for later steps —
PMID:16001398 and
PMID:16001398.

This is the reason GO:0007040 lysosome organization was MODIFYed to GO:0032418 lysosome
localization
on both the IDA and the ARBA IEA: the demonstrated activity is positioning
of the organelle, not biogenesis.

5. Photoreceptors, connecting cilium and opsin transport

PMID:8842737
(pigment epithelium and photoreceptors) — and crucially the species difference that
explains why shaker-1 mice have no retinal phenotype:
PMID:8842737.

Sub-cellular distribution in human photoreceptors:
PMID:8842737

Opsin transport and the spectrin betaV scaffold:
PMID:23704327
PMID:23704327

Both of the vague "intracellular protein localization" (GO:0008104) annotations — the
Ensembl IEA and the curator ISS, both from mouse P97479 — were MODIFYed to GO:0036372
opsin transport on this basis.

6. Judgement calls recorded during the review

7. Calmodulin / light chains

PMID:15300860

PMID:15300860

GO:0005516 calmodulin binding accepted as core: the IQ-bound light chains are the lever
arm, and Ca2+-dependent CaM dissociation is how the motor is switched off. UniProt also
records CALML4 as a Ca2+-insensitive light chain (PubMed:32209652), which may preserve
lever-arm integrity when Ca2+ rises.

8. Open questions for the core-functions / experiment sections