Proteins / MAFIP

DarkQ8WZ33 · Homo sapiens (Human) · 124 aa

MAFIP

MaFF-interacting protein

AI prediction, not experimentally verified. The function, GO terms and reasoning are generated by a model (BioReason-Pro). Treat them as a hypothesis to test, not as a fact.

Predicted 3D structure

AlphaFold model.

In plain language

MAFIP has barely been studied. The model's best guess: A human tektin-like scaffold that assembles higher-order protein complexes during spermatogenesis. By using a filament-forming core to bind partners, it organizes nuclear assemblies that coordinate germ-cell quality control and promote apoptotic execution pathways.

Predicted function

A human tektin-like scaffold that assembles higher-order protein complexes during spermatogenesis.

Confidence: the model gives no confidence score, and this protein has no known function to compare with. Treat it as a hypothesis.

Sequence · 124 aa · coloured by model confidence
1MLCPRAAFLV11GSFHGVFPGP21PASSHWEFWV31PSTPVGAYFC41PPQPQLTPPN51TPKLVSEVEE61LYKSITALRE71KLLQAEQSLR81NLKDIHMSLE91KDVTAMTNSV101FIDRQKCMAH111RTCYPTILQL121AGYQ

Protein domains

Known building blocks found by InterPro, placed along the 124 amino acids of the chain. Hover or tap a block for details.

150100124

Predicted function

Model summary

A human tektin-like scaffold that assembles higher-order protein complexes during spermatogenesis. By using a filament-forming core to bind partners, it organizes nuclear assemblies that coordinate germ-cell quality control and promote apoptotic execution pathways. Its activity centers on multivalent protein interactions that stabilize regulatory platforms, thereby facilitating caspase activation within the nucleus during spermatogenic checkpoints.

Predicted Gene Ontology terms

Molecular function

What it does chemically

Biological process

Which larger process it takes part in

  • GO:0006919 activation of cysteine-type endopeptidase activity involved in apoptotic process

Cellular component

Where in the cell it sits

Model reasoning

How the model got to its answer

  1. 01

    I begin with the InterPro architecture.

    Two overlapping family signatures define the core of the polypeptide: IPR000435 (Tektin-like family, residues 53–123) and IPR048256 (Tektin-like family, residues 53–115). This tandem assignment to the tektin superfamily marks a coiled-coil–rich, non-enzymatic scaffold class that polymerizes into filamentous assemblies and binds other cytoskeletal elements. The restricted span of these domains concentrated in the central region implies that the N- and C-termini contribute auxiliary interaction surfaces rather than catalytic motifs. The absence of catalytic domains and the presence of a filament-forming family signature causally enforce a molecular role dominated by multivalent protein binding, aligning with GO:0005515 protein binding.

  2. 02

    Tektin-like scaffolds typically stabilize higher-order cytoskeletal structures and couple them to regulatory modules.

    In germ cells, such scaffolds can nucleate or reinforce assemblies that coordinate chromosome dynamics and cytoskeletal forces. A scaffold that organizes complexes around chromatin and cytoskeleton can influence apoptotic checkpoints during spermatogenesis. By assembling or exposing pro-apoptotic platforms, a tektin-like framework can facilitate the cascade that culminates in caspase activation. This mechanistic linkage supports the biological process formalized as GO:0006919 activation of cysteine-type endopeptidase activity involved in apoptotic process.

  3. 03

    Cellular placement follows from this architecture and function.

    Tektin-like assemblies are classically cytoskeletal, yet many germ-cell scaffolds shuttle between cytoplasm and nucleus to coordinate chromatin state and apoptosis. The explicit evidence here points to a nuclear residence (GO:0005634 nucleus), which is consistent with a role in spermatogenic checkpoints where nuclear assemblies govern DNA-associated transitions and trigger caspase pathways. A nuclear-localized tektin-like scaffold can anchor or signal to nuclear pores and chromatin-bound complexes, thereby priming caspase activation during quality-control phases of germ-cell maturation.

  4. 04

    Integrating these lines, I infer a mechanism in which a tektin-like scaffold organizes nuclear complexes that sense or impose spermatogenic quality control, then promote caspase activation to eliminate defective germ cells.

    Likely partners include cytoskeletal and spindle-associated proteins that interface with nuclear events, as well as nuclear transport and apoptotic regulators. I hypothesize transient assemblies with tektin family members and axonemal/spindle-associated adaptors to form a structural hub; with nuclear pore and chromatin regulators to gate access to apoptotic signaling; and with caspase-activating modules that execute the apoptotic program during spermatogenesis.

Technical details

InterPro entries

Sources

Method

BioReason-Pro with the ESM3 protein language model (esm3-sm-open-v1). How the atlas is made →

API

/api/v1/proteins/Q8WZ33 · API docs