K9IMD0

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005769 early endosome	IEA GO_REF:0000118	MARK AS OVER ANNOTATED	Summary: Mark inherited receptor-recycling localization as over-annotation. Reason: The focused lactotransferrin report found no positive evidence for a membrane or endosomal draculin pool. Early-endosome localization is inherited from mammalian lactoferrin-receptor recycling, a context not established for the secreted salivary bat protein. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md mammalian lactoferrin-receptor recycling itinerary
GO:0005886 plasma membrane	IEA GO_REF:0000118	MARK AS OVER ANNOTATED	Summary: Mark inherited receptor-recycling localization as over-annotation. Reason: The focused lactotransferrin report found no positive evidence for a membrane or endosomal draculin pool. Plasma-membrane localization is inherited from mammalian lactoferrin-receptor recycling, a context not established for the secreted salivary bat protein. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md mammalian lactoferrin-receptor recycling itinerary
GO:0019731 antibacterial humoral response	IEA GO_REF:0000118	KEEP AS NON CORE	Summary: Keep antibacterial humoral response as a non-core lactotransferrin-family inference. Reason: The focused report treats antibacterial and broader immune annotations as weak family-level carry-over, supported by salivary antimicrobial grouping but not by a direct draculin bactericidal assay. Keep the term as a peripheral lactotransferrin inference rather than the demonstrated draculin anticoagulant core. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md antibacterial/defense/immune (family carry-over + transcriptomic grouping only) PMID:23411029 Accessory glands were enriched with antimicrobials
GO:0035821 modulation of process of another organism	IEA GO_REF:0000108	ACCEPT	Summary: Retain the broad function associated with salivary anticoagulant activity. Reason: Native draculin inhibits prey coagulation factors and the 2013 proteomic/transcriptomic study maps the draculin scaffold to lactotransferrin. Modulation of another organism, negative regulation of an organismal process, and toxin activity are compatible with a salivary factor evolved to disrupt prey hemostasis. A narrower coagulation term does not invalidate them, and a BP term is not an appropriate replacement for an MF toxin assertion. Sequence-to-activity mapping remains explicitly qualified because recombinant confirmation is lacking. Supporting Evidence: PMID:7740503 Draculin inhibits the activated form of coagulation factors IX and X. PMID:23748026 established that it is a mutated version of the lactotransferrin scaffold.
GO:0055037 recycling endosome	IEA GO_REF:0000118	MARK AS OVER ANNOTATED	Summary: Mark inherited receptor-recycling localization as over-annotation. Reason: The focused lactotransferrin report found no positive evidence for a membrane or endosomal draculin pool. Recycling-endosome localization is inherited from mammalian lactoferrin-receptor recycling, a context not established for the secreted salivary bat protein. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md mammalian lactoferrin-receptor recycling itinerary
GO:0001503 ossification	IEA GO_REF:0000043	UNDECIDED	Summary: The inherited bone-regulatory role is unresolved. Reason: Lactotransferrin can affect osteoblast and osteoclast behavior in other mammals, but the report does not establish which receptor-dependent functions K9IMD0 retains. Absence of ossification measurements in a saliva-focused paper is not evidence of loss. Keep this specific physiological transfer unresolved pending a dedicated ossification/receptor review. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-uniprot.txt May have anabolic, differentiating file:DESRO/K9IMD0/K9IMD0-deep-research-falcon.md These functions are not directly assayed for the vampire-bat LTF/draculin sequence
GO:0002376 immune system process	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Keep immune system process as a non-core lactotransferrin-family inference. Reason: The focused report treats immune annotations as weak family-level carry-over, supported by salivary antimicrobial grouping but not by a direct draculin immune assay. Keep this broad immune term as a peripheral lactotransferrin inference rather than the demonstrated draculin anticoagulant core. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md antibacterial/defense/immune (family carry-over + transcriptomic grouping only) PMID:23411029 Accessory glands were enriched with antimicrobials
GO:0005576 extracellular region	IEA GO_REF:0000120	ACCEPT	Summary: Draculin is isolated from vampire bat saliva, consistent with extracellular region localization [PMID:7740503]. Reason: Saliva isolation indicates a secreted/extracellular protein [PMID:7740503].
GO:0005615 extracellular space	IEA GO_REF:0000120	ACCEPT	Summary: Draculin is a salivary anticoagulant protein, supporting extracellular space annotation [PMID:7740503]. Reason: Experimental purification from saliva supports extracellular space localization [PMID:7740503].
GO:0006508 proteolysis	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Keep proteolysis as a non-core consequence of unverified lactoferrin protease inheritance. Reason: The focused report found only partial conservation of the lactoferrin protease determinants in K9IMD0; the candidate nucleophile Ser is retained but the catalytic Lys is altered. Because the more specific serine-type peptidase row is retained as a caveated structural inference, proteolysis remains biologically plausible, but without a direct draculin protease assay it should remain peripheral to the anticoagulant core. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md catalytic Lys of the protease dyad
GO:0006811 monoatomic ion transport	IEA GO_REF:0000043	MARK AS OVER ANNOTATED	Summary: Mark inherited monoatomic-ion transport as over-annotation of partial iron binding. Reason: The focused report supports a conserved N-lobe ferric-binding site but found the C-lobe iron site degraded and no bat assay or receptor-recycling context for transport. Metal binding remains plausible; the broader ion-transport process is an over-transfer from mammalian lactotransferrin. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md bilobal transport is degraded
GO:0006826 iron ion transport	IEA GO_REF:0000120	MARK AS OVER ANNOTATED	Summary: Mark inherited iron-ion transport as over-annotation of partial iron binding. Reason: The focused report supports a conserved N-lobe ferric-binding site but found the C-lobe iron site degraded and no bat assay or receptor-recycling context for transport. Metal binding remains plausible; iron-ion transport is an over-transfer from mammalian lactotransferrin. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md bilobal transport is degraded
GO:0008233 peptidase activity	IEA GO_REF:0000043	MODIFY	Summary: Refine broad peptidase activity to caveated serine-type peptidase activity. Reason: The focused report found only partial conservation of the lactoferrin protease determinants in K9IMD0; the candidate nucleophile Ser is retained but the catalytic Lys is altered. Peptidase activity is therefore too broad for this keyword transfer; the caveated descendant serine-type peptidase activity captures the retained nucleophile while leaving the activity outside the demonstrated anticoagulant core. Proposed replacements: serine-type peptidase activity Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md catalytic Lys of the protease dyad
GO:0008236 serine-type peptidase activity	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Keep serine-type peptidase as a non-core inferred lactoferrin feature. Reason: The focused report treats serine-type peptidase activity as structurally defensible because K9IMD0 retains the candidate lactoferrin protease nucleophile, but it also found one catalytic residue altered and no direct bat assay. Keep the row as a peripheral inferred activity rather than as core draculin anticoagulant biology. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md GO:0008236 serine-type peptidase (nucleophile Ser conserved)
GO:0016787 hydrolase activity	IEA GO_REF:0000043	MODIFY	Summary: Refine broad hydrolase activity to caveated serine-type peptidase activity. Reason: The focused report found only partial conservation of the lactoferrin protease determinants in K9IMD0; the candidate nucleophile Ser is retained but the catalytic Lys is altered. Hydrolase activity is too broad for the evidence and should be refined to the caveated serine-type peptidase activity inferred from the retained nucleophile, outside the demonstrated anticoagulant core. Proposed replacements: serine-type peptidase activity Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md catalytic Lys of the protease dyad
GO:0042742 defense response to bacterium	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Keep defense response to bacterium as a non-core lactotransferrin-family inference. Reason: The focused report treats antibacterial and broader immune annotations as weak family-level carry-over, supported by salivary antimicrobial grouping but not by a direct draculin bactericidal assay. Keep the term as a peripheral lactotransferrin inference rather than the demonstrated draculin anticoagulant core. Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md antibacterial/defense/immune (family carry-over + transcriptomic grouping only) PMID:23411029 Accessory glands were enriched with antimicrobials
GO:0046872 metal ion binding	IEA GO_REF:0000043	MODIFY	Summary: Refine metal ion binding to caveated N-lobe ferric iron binding. Reason: The focused report supports retention of a conserved N-lobe Fe(3+)/carbonate-binding site but also found that the C-lobe iron site is broken by Y454-to-D452 replacement. Metal ion binding remains biologically plausible as a non-core, sequence-based lactotransferrin feature; ferric iron binding names the supported ligand without implying intact bilobal iron transport or purified bat binding kinetics. Proposed replacements: ferric iron binding Supporting Evidence: file:DESRO/K9IMD0/K9IMD0-uniprot.txt Transferrins are iron binding transport proteins which can file:DESRO/K9IMD0/K9IMD0-uniprot.txt /ligand="Fe(3+)" file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md N-lobe iron site is fully conserved file:DESRO/K9IMD0/K9IMD0-hypotheses/lactotransferrin-functions-and-draculin-specialization/openscientist.md C-lobe iron site is broken (Y454→D452)
GO:0051241 negative regulation of multicellular organismal process	IEA GO_REF:0000117	ACCEPT	Summary: Retain the broad function associated with salivary anticoagulant activity. Reason: Native draculin inhibits prey coagulation factors and the 2013 proteomic/transcriptomic study maps the draculin scaffold to lactotransferrin. Modulation of another organism, negative regulation of an organismal process, and toxin activity are compatible with a salivary factor evolved to disrupt prey hemostasis. A narrower coagulation term does not invalidate them, and a BP term is not an appropriate replacement for an MF toxin assertion. Sequence-to-activity mapping remains explicitly qualified because recombinant confirmation is lacking. Supporting Evidence: PMID:7740503 Draculin inhibits the activated form of coagulation factors IX and X. PMID:23748026 established that it is a mutated version of the lactotransferrin scaffold.
GO:0090729 toxin activity	IEA GO_REF:0000043	ACCEPT	Summary: Retain the broad function associated with salivary anticoagulant activity. Reason: Native draculin inhibits prey coagulation factors and the 2013 proteomic/transcriptomic study maps the draculin scaffold to lactotransferrin. Modulation of another organism, negative regulation of an organismal process, and toxin activity are compatible with a salivary factor evolved to disrupt prey hemostasis. A narrower coagulation term does not invalidate them, and a BP term is not an appropriate replacement for an MF toxin assertion. Sequence-to-activity mapping remains explicitly qualified because recombinant confirmation is lacking. Supporting Evidence: PMID:7740503 Draculin inhibits the activated form of coagulation factors IX and X. PMID:23748026 established that it is a mutated version of the lactotransferrin scaffold.
GO:0004867 serine-type endopeptidase inhibitor activity	IDA PMID:10556567 Draculin, the anticoagulant factor in vampire bat saliva, is...	NEW	Summary: Draculin inhibits activated coagulation proteases IXa and Xa, consistent with serine-type endopeptidase inhibitor activity [PMID:7740503; PMID:10556567]. Reason: GOA lacks the specific serine protease inhibitor activity, but biochemical studies show direct inhibition of FXa/IXa [PMID:7740503; PMID:10556567]. The assignment follows the curated native draculin evidence and 2013 sequence/proteomic mapping; recombinant K9IMD0 confirmation is still lacking (PMID:23411029), so the sequence-to-activity mapping remains qualified. Supporting Evidence: PMID:10556567 noncompetitive inhibitor of activated factor X. PMID:7740503 Draculin inhibits the activated form of coagulation factors IX and X. PMID:23411029 However, it remains to be confirmed whether recombinant bat salivary lactotransferrin display anticoagulant activity.
GO:0005615 extracellular space	IDA PMID:10556567 Draculin, the anticoagulant factor in vampire bat saliva, is...	ACCEPT	Summary: Draculin is a salivary anticoagulant protein, consistent with extracellular space localization [PMID:10556567]. Reason: The study describes draculin as a factor in vampire bat saliva, supporting extracellular localization [PMID:10556567]. Supporting Evidence: PMID:10556567 Draculin, the anticoagulant factor in vampire bat saliva, is a tight-binding,
GO:0005615 extracellular space	IDA PMID:23748026 Dracula's children: molecular evolution of vampire bat venom...	ACCEPT	Summary: Draculin is part of vampire bat oral secretions/venom, supporting extracellular space localization [PMID:23748026]. Reason: The proteomic/transcriptomic study discusses vampire bat oral secretions and draculin, consistent with extracellular secretion [PMID:23748026]. Supporting Evidence: PMID:23748026 While vampire bat oral secretions have been the subject of intense research,
GO:0005615 extracellular space	IDA PMID:7740503 Purification and partial characterization of draculin, the a...	ACCEPT	Summary: Draculin was purified from vampire bat saliva, supporting extracellular space localization [PMID:7740503]. Reason: Isolation from saliva indicates a secreted extracellular protein [PMID:7740503]. Supporting Evidence: PMID:7740503 From the saliva of the vampire bat Desmodus rotundus, we isolated an unknown
GO:0005615 extracellular space	IDA PMID:9795244 Expression of biological activity of draculin, the anticoagu...	ACCEPT	Summary: Draculin is a glycoprotein isolated from vampire bat saliva, supporting extracellular space localization [PMID:9795244]. Reason: The study explicitly describes draculin as isolated from saliva, consistent with extracellular space [PMID:9795244]. Supporting Evidence: PMID:9795244 Draculin, a glycoprotein isolated from vampire bat (Desmodus rotundus) saliva,
GO:0030195 negative regulation of blood coagulation	IDA PMID:10556567 Draculin, the anticoagulant factor in vampire bat saliva, is...	ACCEPT	Summary: Draculin inhibits activated factor X, supporting negative regulation of blood coagulation [PMID:10556567]. Reason: Direct biochemical evidence shows draculin inhibits FXa, consistent with anticoagulant activity [PMID:10556567]. Supporting Evidence: PMID:10556567 noncompetitive inhibitor of activated factor X.
GO:0030195 negative regulation of blood coagulation	IDA PMID:7740503 Purification and partial characterization of draculin, the a...	ACCEPT	Summary: Draculin inhibits activated coagulation factors IX and X, supporting negative regulation of blood coagulation [PMID:7740503]. Reason: Experimental data show inhibition of IXa/Xa by draculin [PMID:7740503]. Supporting Evidence: PMID:7740503 Draculin inhibits the activated form of coagulation factors IX and X.
GO:0030195 negative regulation of blood coagulation	IDA PMID:9795244 Expression of biological activity of draculin, the anticoagu...	ACCEPT	Summary: Draculin inhibits activated coagulation factors IXa and Xa, supporting negative regulation of blood coagulation [PMID:9795244]. Reason: The study states draculin is a natural anticoagulant that inhibits IXa/Xa [PMID:9795244]. Supporting Evidence: PMID:9795244 is a natural anticoagulant which inhibits activated coagulation factors IX (IXa)

Gene Description

Existing Annotations Review

Core Functions

Salivary anticoagulant activity attributed to draculin through native IXa/Xa inhibition and the lactotransferrin sequence/proteomic mapping; recombinant confirmation for exact K9IMD0 remains pending.

References

Suggested Questions for Experts

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📚 Additional Documentation

Notes

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