K9IYM3

UniProt ID: K9IYM3
Organism: Desmodus rotundus
Review Status: INITIALIZED
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Gene Description

Secreted serpin-like plasma protease C1 inhibitor candidate from vampire bat salivary gland.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004867 serine-type endopeptidase inhibitor activity
IEA
GO_REF:0000120 		ACCEPT
Summary: Putative plasma protease C1 inhibitor annotation supports serine-type endopeptidase inhibitor activity.
Reason: UniProt classifies this protein as a plasma protease C1 inhibitor (serpin family).
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"SubName: Full=Putative plasma protease c1 inhibitor"
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"Belongs to the serpin family."
file:DESRO/K9IYM3/K9IYM3-deep-research-falcon.md
K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily.
GO:0005576 extracellular region
IEA
GO_REF:0000120 		ACCEPT
Summary: Extracellular region is the appropriate localization term for a secreted protein. GO:0005615 (extracellular space) is obsolete.
Reason: UniProt indicates secretion; extracellular region is the correct term since GO:0005615 (extracellular space) is obsolete.
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"SUBCELLULAR LOCATION: Secreted"
GO:0005615 extracellular space
IEA
GO_REF:0000120 		MODIFY
Summary: GO:0005615 (extracellular space) is obsolete; use GO:0005576 (extracellular region) instead.
Reason: GO:0005615 is obsolete; replace with GO:0005576 (extracellular region).
Proposed replacements: extracellular region
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"SUBCELLULAR LOCATION: Secreted"
GO:0006508 proteolysis
IEA
GO_REF:0000043 		REMOVE
Summary: Proteolysis is inappropriate for a serpin inhibitor and lacks supporting evidence.
Reason: Serpins inhibit proteases rather than catalyze proteolysis; no evidence for proteolytic activity in this protein.
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"Belongs to the serpin family."
GO:0007596 blood coagulation
IEA
GO_REF:0000043 		MARK AS OVER ANNOTATED
Summary: Blood coagulation annotation is inferred from keywords without direct evidence in DESRO.
Reason: No experimental evidence for this specific process in DESRO K9IYM3; annotation is keyword-based.
GO:0007599 hemostasis
IEA
GO_REF:0000043 		MARK AS OVER ANNOTATED
Summary: Hemostasis annotation is broad and inferred without direct evidence for this DESRO protein.
Reason: Keyword-based inference lacks direct experimental support.
GO:0008233 peptidase activity
IEA
GO_REF:0000043 		REMOVE
Summary: Peptidase activity is inconsistent with a serpin inhibitor and lacks evidence.
Reason: This protein is annotated as a protease inhibitor rather than an enzyme.
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"Belongs to the serpin family."
GO:0030414 peptidase inhibitor activity
IEA
GO_REF:0000043 		MODIFY
Summary: Peptidase inhibitor activity is a broad parent term; use the specific serine-type endopeptidase inhibitor activity.
Reason: Serpin annotation supports serine-type endopeptidase inhibitor activity.
Supporting Evidence:
file:DESRO/K9IYM3/K9IYM3-uniprot.txt
"Belongs to the serpin family."
GO:0042730 fibrinolysis
IEA
GO_REF:0000043 		MARK AS OVER ANNOTATED
Summary: Fibrinolysis annotation is inferred without direct evidence for this DESRO protein.
Reason: Keyword-based inference lacks experimental support in DESRO.

Core Functions

Secreted serpin-family protease inhibitor (plasma protease C1 inhibitor-like).

Molecular Function:
serine-type endopeptidase inhibitor activity
Cellular Locations:
extracellular region
Supporting Evidence:
  • file:DESRO/K9IYM3/K9IYM3-uniprot.txt
    SubName: Full=Putative plasma protease c1 inhibitor
  • file:DESRO/K9IYM3/K9IYM3-uniprot.txt
    Belongs to the serpin family.
  • file:DESRO/K9IYM3/K9IYM3-uniprot.txt
    SUBCELLULAR LOCATION: Secreted
  • file:DESRO/K9IYM3/K9IYM3-deep-research-falcon.md
    K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily.

References

GO_REF:0000043
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods

Deep Research

Falcon

(K9IYM3-deep-research-falcon.md)
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 11 citations 2026-01-21T11:14:21.655532

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: Functional annotation of UniProt K9IYM3 (putative plasma protease C1 inhibitor; serpin family) from Desmodus rotundus

Plan and verification of identity
- Identity and organism: K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily. Serpins share a conserved fold and a reactive center loop (RCL) used for suicide-substrate inhibition of serine proteases; these features match the UniProt domain annotations (Serpin domain/superfamily). Independent proteomics in vampire bat serum detected an ortholog annotated and mapped to human SERPING1 (plasma protease C1 inhibitor), supporting the assignment of a circulating C1 inhibitor–like serpin in D. rotundus (Neely et al., Journal of Proteome Research, 2021; DOI: 10.1021/acs.jproteome.0c00995) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8). Domain/family alignment and mechanism are consistent with mammalian C1 inhibitor (SERPING1) literature, including recent structural work (Garrigues et al., Journal of Immunology, 2024; DOI: 10.4049/jimmunol.2400194) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 2-4).

1) Key concepts and definitions
- C1 inhibitor (C1‑INH; SERPING1): a secreted, heavily glycosylated serpin that regulates multiple blood protease cascades by forming a covalent complex with target proteases after initial formation of a non‑covalent Michaelis–Menten (M–M) complex. It is the only canonical complement regulator in the SERPIN family (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2).
- Serpin mechanism: The exposed RCL is engaged by the target protease; cleavage triggers large conformational change, trapping the protease in an irreversible complex. Recent structural data show that exosite contacts outside the RCL contribute substantially to affinity and specificity in the C1‑INH:C1s complex (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 11-12).
- Bat ortholog evidence: D. rotundus serum proteomics detected complement proteins, including SERPING1/plasma protease C1 inhibitor among 31 complement activation proteins profiled; targeted MS could quantify these proteins in bat serum, supporting circulating, secreted C1‑INH in this species (Neely et al., 2021; Apr 2021) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8).

2) Current mechanistic understanding (targets, mechanism, localization)
- Primary enzymatic targets:
• Complement classical pathway: C1r and C1s (inhibits their active forms); recent crystal structure of the human C1‑INH:C1s M–M complex demonstrates extensive non‑RCL interfaces and validates key exosite interactions on C1s and C1‑INH that promote initial recognition prior to covalent trapping (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17).
• Lectin pathway: MASP proteases (by homology and known mammalian C1‑INH specificity; exosite-based recognition principles extend to MASPs) (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 15-16).
• Contact system/coagulation/fibrinolysis: plasma kallikrein and factor XIIa are canonical C1‑INH targets; the 2024 structural/mechanistic analysis notes C1‑INH’s regulation across all four blood proteolytic cascades (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2).
- Mechanism of inhibition:
• Non‑covalent M–M complex forms through RCL engagement and extensive exosite interfaces (nearly half of the interface originates outside the RCL on both partners), then RCL cleavage and insertion trap the protease in a covalent complex (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 11-12).
• Cofactor potentiation: polyanionic cofactors such as heparin and related glycosaminoglycans can enhance C1‑INH activity; basic residues on C1‑INH mediate this potentiation, consistent with serpin–glycan allosteric effects (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 11-12, garrigues2024thecrystalstructure pages 15-16).
- Localization and maturation:
• C1‑INH is a secreted, glycoprotein circulating in plasma. Structural work and prior biochemistry note heavy glycosylation and interactions with heparin-like glycans; these features are consistent with secretory pathway maturation and plasma localization (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 2-4, garrigues2024thecrystalstructure pages 11-12). In vampire bats, serum proteomics confirms presence in blood (Neely et al., 2021; Apr 2021) (neely2021surveyingthevampire pages 3-5).

3) Pathway roles
- Complement classical pathway: C1‑INH controls initiation by inhibiting activated C1r/C1s, preventing unchecked cleavage of C4 and C2 (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17).
- Lectin pathway: by analogy and known mammalian biology, C1‑INH inhibits MASP proteases; exosite determinants on MASP-2 that control C2 activation provide a conceptual framework for C1‑INH recognition (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 15-16).
- Contact system: C1‑INH inhibits factor XIIa and plasma kallikrein, thereby restraining bradykinin generation. The 2024 study reiterates these cross‑cascade regulatory roles (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2).
- Coagulation/fibrinolysis: C1‑INH modulates proteases in these cascades, contributing to overall hemostatic balance; this multi-cascade regulation is emphasized in the recent structural paper (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2).

4) Recent developments and latest research (priority 2023–2024)
- New structural insight (2024): First crystal structure of the Michaelis–Menten complex between human C1‑INH and C1s (3.94 Å) delineates how extensive exosite interfaces outside the RCL drive recognition, validated by mutagenesis and surface plasmon resonance. This clarifies specificity determinants for C1‑INH toward complement proteases and informs inhibitor design (Garrigues et al., 2024; Jul 2024; URL: https://doi.org/10.4049/jimmunol.2400194) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17, garrigues2024thecrystalstructure pages 11-12, garrigues2024thecrystalstructure pages 2-4).
- Exosite and cofactor regulation: The study compiles evidence that heparin and other polyanions potentiate C1‑INH, and that substrate-recognition exosites on C1s (and MASPs) are central to both natural substrate binding and serpin engagement, refining mechanistic models (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 11-12, garrigues2024thecrystalstructure pages 15-16).
- Genetic and pathogenicity notes: The structural/mechanistic review within the article references SERPING1 variant classes (including missense variants that impair complex formation) and pathogen strategies (e.g., bacterial proteins binding C1‑INH), highlighting clinical and infection biology relevance; these perspectives contextualize SERPING1 dysfunction (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 11-12, garrigues2024thecrystalstructure pages 15-16).
- Bat immunoproteomics resource: While from 2021, the D. rotundus serum proteome establishes a platform for targeted measurement of C1‑INH and other complement factors in wild vampire bats, enabling future 2023–2024 comparative and ecological immunology work; the authors report 31 complement activation proteins and detection of a SERPING1 ortholog (Neely et al., 2021; Apr 2021; URL: https://doi.org/10.1021/acs.jproteome.0c00995) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8).

5) Expert opinions and authoritative perspectives
- Garrigues et al. (2024) provide an authoritative, peer‑reviewed structural and mechanistic analysis from the Journal of Immunology, emphasizing that non‑RCL exosite interactions are crucial for C1‑INH engagement of C1s and likely other targets, reshaping how specificity is understood for SERPING1 across its protease repertoire (Jul 2024; URL: https://doi.org/10.4049/jimmunol.2400194) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17, garrigues2024thecrystalstructure pages 11-12).
- Neely et al. (2021) contribute a foundational bat serum proteomic dataset in Journal of Proteome Research, offering practical guidance for immunoprotein detection in bats and listing SERPING1 among detected complement proteins, supporting the conservation and circulating presence of C1‑INH in D. rotundus (Apr 2021; URL: https://doi.org/10.1021/acs.jproteome.0c00995) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8).

6) Relevant statistics and data
- Structural parameters: The C1‑INH:C1s M–M complex was resolved at 3.94 Å; refinement Rwork/Rfree were 26.2%/28.1% in space group P 42 21 2. Heparin oligosaccharide was included during co‑purification/crystallization to emulate physiologic cofactor interactions (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 2-4).
- Interface composition: Nearly half of the C1‑INH:C1s interface arises from residues outside the RCL; mutations on exosite loops reduced affinity in surface plasmon resonance assays, quantifying exosite contributions to binding (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17).
- Bat serum proteomics coverage: DIA proteomics of D. rotundus serum identified 361–376 proteins using RefSeq mapping and reported 31 complement activation proteins suitable for targeted MS. SERPING1/plasma protease C1 inhibitor was present among complement identifications (Neely et al., 2021; Apr 2021) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8).

Functional inference for K9IYM3 in Desmodus rotundus
- Given UniProt annotation, conserved serpin domains, and independent serum detection of a SERPING1 ortholog in D. rotundus, K9IYM3 most likely encodes the bat ortholog of plasma protease C1 inhibitor. By strong homology to mammalian SERPING1, its primary role is extracellular/plasma inhibition of C1r and C1s (classical pathway), MASPs (lectin pathway), and key proteases in the contact (FXIIa, plasma kallikrein), coagulation, and fibrinolytic cascades. Mechanistically, it employs an RCL‑driven suicide inhibition with substantial exosite-mediated recognition, and its activity is modulated by polyanionic glycans. The protein is secreted, heavily glycosylated, and localized to blood plasma, consistent with its detection in vampire bat serum proteomes (Garrigues et al., 2024; Jul 2024; Neely et al., 2021; Apr 2021) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 11-12, neely2021surveyingthevampire pages 3-5).

Mandatory ambiguity check and limitations
- The identifier “K9IYM3” is a UniProt accession (not a gene symbol). Literature specifically on “K9IYM3” is limited; organism‑specific experimental characterization in D. rotundus beyond proteomic detection is lacking in accessible sources. Therefore, functional annotations are inferred from conserved serpin domains and extensive mammalian SERPING1 literature, plus species‑specific evidence of serum presence in D. rotundus (Neely et al., 2021; Apr 2021) (neely2021surveyingthevampire pages 3-5). The recent mechanistic insights (exosite recognition, glycan potentiation) derive from human C1‑INH:C1s structural work (Garrigues et al., 2024; Jul 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 11-12).

References with URLs and dates
- Garrigues RJ, Garrison MP, Garcia BL. The Crystal Structure of the Michaelis-Menten Complex of C1 Esterase Inhibitor and C1s Reveals Novel Insights into Complement Regulation. Journal of Immunology. Jul 2024. DOI: 10.4049/jimmunol.2400194; URL: https://doi.org/10.4049/jimmunol.2400194 (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17, garrigues2024thecrystalstructure pages 11-12, garrigues2024thecrystalstructure pages 2-4).
- Neely BA, Janech MG, Fenton MB, et al. Surveying the Vampire Bat (Desmodus rotundus) Serum Proteome: A Resource for Identifying Immunological Proteins and Detecting Pathogens. Journal of Proteome Research. Apr 2021. DOI: 10.1021/acs.jproteome.0c00995; URL: https://doi.org/10.1021/acs.jproteome.0c00995 (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8).

Data availability statement
- Protein identity and organism: UniProt K9IYM3 annotation (described in the prompt) aligns with serpin family and plasma protease C1 inhibitor function. Bat serum proteomics provides orthogonal evidence of a SERPING1 ortholog circulating in Desmodus rotundus (Neely et al., 2021) (neely2021surveyingthevampire pages 3-5, neely2021surveyingthevampire pages 7-8). The most up-to-date mechanistic details are supported by the 2024 human C1‑INH:C1s structure (Garrigues et al., 2024) (garrigues2024thecrystalstructure pages 1-2, garrigues2024thecrystalstructure pages 16-17, garrigues2024thecrystalstructure pages 11-12).

References

  1. (neely2021surveyingthevampire pages 3-5): Benjamin A. Neely, Michael G. Janech, M. Brock Fenton, Nancy B. Simmons, Alison M. Bland, and Daniel J. Becker. Surveying the vampire bat (desmodus rotundus) serum proteome: a resource for identifying immunological proteins and detecting pathogens. Journal of Proteome Research, 20:2547-2559, Apr 2021. URL: https://doi.org/10.1021/acs.jproteome.0c00995, doi:10.1021/acs.jproteome.0c00995. This article has 25 citations and is from a peer-reviewed journal.

  2. (neely2021surveyingthevampire pages 7-8): Benjamin A. Neely, Michael G. Janech, M. Brock Fenton, Nancy B. Simmons, Alison M. Bland, and Daniel J. Becker. Surveying the vampire bat (desmodus rotundus) serum proteome: a resource for identifying immunological proteins and detecting pathogens. Journal of Proteome Research, 20:2547-2559, Apr 2021. URL: https://doi.org/10.1021/acs.jproteome.0c00995, doi:10.1021/acs.jproteome.0c00995. This article has 25 citations and is from a peer-reviewed journal.

  3. (garrigues2024thecrystalstructure pages 1-2): Ryan J. Garrigues, Matthew P Garrison, and Brandon L. Garcia. The crystal structure of the michaelis-menten complex of c1 esterase inhibitor and c1s reveals novel insights into complement regulation. Journal of immunology, 213:718-729, Jul 2024. URL: https://doi.org/10.4049/jimmunol.2400194, doi:10.4049/jimmunol.2400194. This article has 2 citations and is from a domain leading peer-reviewed journal.

  4. (garrigues2024thecrystalstructure pages 2-4): Ryan J. Garrigues, Matthew P Garrison, and Brandon L. Garcia. The crystal structure of the michaelis-menten complex of c1 esterase inhibitor and c1s reveals novel insights into complement regulation. Journal of immunology, 213:718-729, Jul 2024. URL: https://doi.org/10.4049/jimmunol.2400194, doi:10.4049/jimmunol.2400194. This article has 2 citations and is from a domain leading peer-reviewed journal.

  5. (garrigues2024thecrystalstructure pages 11-12): Ryan J. Garrigues, Matthew P Garrison, and Brandon L. Garcia. The crystal structure of the michaelis-menten complex of c1 esterase inhibitor and c1s reveals novel insights into complement regulation. Journal of immunology, 213:718-729, Jul 2024. URL: https://doi.org/10.4049/jimmunol.2400194, doi:10.4049/jimmunol.2400194. This article has 2 citations and is from a domain leading peer-reviewed journal.

  6. (garrigues2024thecrystalstructure pages 16-17): Ryan J. Garrigues, Matthew P Garrison, and Brandon L. Garcia. The crystal structure of the michaelis-menten complex of c1 esterase inhibitor and c1s reveals novel insights into complement regulation. Journal of immunology, 213:718-729, Jul 2024. URL: https://doi.org/10.4049/jimmunol.2400194, doi:10.4049/jimmunol.2400194. This article has 2 citations and is from a domain leading peer-reviewed journal.

  7. (garrigues2024thecrystalstructure pages 15-16): Ryan J. Garrigues, Matthew P Garrison, and Brandon L. Garcia. The crystal structure of the michaelis-menten complex of c1 esterase inhibitor and c1s reveals novel insights into complement regulation. Journal of immunology, 213:718-729, Jul 2024. URL: https://doi.org/10.4049/jimmunol.2400194, doi:10.4049/jimmunol.2400194. This article has 2 citations and is from a domain leading peer-reviewed journal.

Citations

  1. garrigues2024thecrystalstructure pages 1-2
  2. garrigues2024thecrystalstructure pages 15-16
  3. neely2021surveyingthevampire pages 3-5
  4. garrigues2024thecrystalstructure pages 2-4
  5. neely2021surveyingthevampire pages 7-8
  6. garrigues2024thecrystalstructure pages 11-12
  7. garrigues2024thecrystalstructure pages 16-17
  8. https://doi.org/10.4049/jimmunol.2400194
  9. https://doi.org/10.1021/acs.jproteome.0c00995
  10. https://doi.org/10.1021/acs.jproteome.0c00995,
  11. https://doi.org/10.4049/jimmunol.2400194,

📚 Additional Documentation

Notes

(K9IYM3-notes.md)

K9IYM3 Research Notes

Key findings

  • UniProt annotates this protein as a putative plasma protease C1 inhibitor [file:DESRO/K9IYM3/K9IYM3-uniprot.txt "SubName: Full=Putative plasma protease c1 inhibitor"].
  • UniProt indicates the protein is secreted [file:DESRO/K9IYM3/K9IYM3-uniprot.txt "SUBCELLULAR LOCATION: Secreted"].
  • UniProt places the protein in the serpin family [file:DESRO/K9IYM3/K9IYM3-uniprot.txt "Belongs to the serpin family."].
  • Deep research summary notes the Desmodus rotundus serpin annotation [file:DESRO/K9IYM3/K9IYM3-deep-research-falcon.md "K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily."].

📄 View Raw YAML

 
id: K9IYM3
gene_symbol: K9IYM3
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9430
  label: Desmodus rotundus
description: 'Secreted serpin-like plasma protease C1 inhibitor candidate from vampire
  bat salivary gland.'
existing_annotations:
  - term:
      id: GO:0004867
      label: serine-type endopeptidase inhibitor activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: Putative plasma protease C1 inhibitor annotation supports 
        serine-type endopeptidase inhibitor activity.
      action: ACCEPT
      reason: UniProt classifies this protein as a plasma protease C1 inhibitor 
        (serpin family).
      supported_by:
        - reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
          supporting_text: '"SubName: Full=Putative plasma protease c1 inhibitor"'
        - &id002
          reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
          supporting_text: '"Belongs to the serpin family."'
        - reference_id: file:DESRO/K9IYM3/K9IYM3-deep-research-falcon.md
          supporting_text: 'K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily.'
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: Extracellular region is the appropriate localization term for a
        secreted protein. GO:0005615 (extracellular space) is obsolete.
      action: ACCEPT
      reason: UniProt indicates secretion; extracellular region is the correct
        term since GO:0005615 (extracellular space) is obsolete.
      supported_by:
        - &id001
          reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
          supporting_text: '"SUBCELLULAR LOCATION: Secreted"'
  - term:
      id: GO:0005615
      label: extracellular space
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: GO:0005615 (extracellular space) is obsolete; use GO:0005576
        (extracellular region) instead.
      action: MODIFY
      reason: GO:0005615 is obsolete; replace with GO:0005576 (extracellular
        region).
      proposed_replacement_terms:
        - id: GO:0005576
          label: extracellular region
      supported_by:
        - *id001
  - term:
      id: GO:0006508
      label: proteolysis
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Proteolysis is inappropriate for a serpin inhibitor and lacks 
        supporting evidence.
      action: REMOVE
      reason: Serpins inhibit proteases rather than catalyze proteolysis; no 
        evidence for proteolytic activity in this protein.
      supported_by:
        - *id002
  - term:
      id: GO:0007596
      label: blood coagulation
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Blood coagulation annotation is inferred from keywords without 
        direct evidence in DESRO.
      action: MARK_AS_OVER_ANNOTATED
      reason: No experimental evidence for this specific process in DESRO 
        K9IYM3; annotation is keyword-based.
  - term:
      id: GO:0007599
      label: hemostasis
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Hemostasis annotation is broad and inferred without direct 
        evidence for this DESRO protein.
      action: MARK_AS_OVER_ANNOTATED
      reason: Keyword-based inference lacks direct experimental support.
  - term:
      id: GO:0008233
      label: peptidase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Peptidase activity is inconsistent with a serpin inhibitor and 
        lacks evidence.
      action: REMOVE
      reason: This protein is annotated as a protease inhibitor rather than an 
        enzyme.
      supported_by:
        - *id002
  - term:
      id: GO:0030414
      label: peptidase inhibitor activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Peptidase inhibitor activity is a broad parent term; use the 
        specific serine-type endopeptidase inhibitor activity.
      action: MODIFY
      reason: Serpin annotation supports serine-type endopeptidase inhibitor 
        activity.
      proposed_replacement_terms:
        - id: GO:0004867
          label: serine-type endopeptidase inhibitor activity
      supported_by:
        - *id002
  - term:
      id: GO:0042730
      label: fibrinolysis
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: Fibrinolysis annotation is inferred without direct evidence for 
        this DESRO protein.
      action: MARK_AS_OVER_ANNOTATED
      reason: Keyword-based inference lacks experimental support in DESRO.
references:
  - id: GO_REF:0000043
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword 
      mapping
    findings: []
  - id: GO_REF:0000120
    title: Combined Automated Annotation using Multiple IEA Methods
    findings: []
core_functions:
  - description: Secreted serpin-family protease inhibitor (plasma protease C1 inhibitor-like).
    supported_by:
      - reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
        supporting_text: 'SubName: Full=Putative plasma protease c1 inhibitor'
      - reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
        supporting_text: Belongs to the serpin family.
      - reference_id: file:DESRO/K9IYM3/K9IYM3-uniprot.txt
        supporting_text: 'SUBCELLULAR LOCATION: Secreted'
      - reference_id: file:DESRO/K9IYM3/K9IYM3-deep-research-falcon.md
        supporting_text: 'K9IYM3 is annotated as a putative plasma protease C1 inhibitor from Desmodus rotundus (common vampire bat), belonging to the serpin superfamily.'
    molecular_function:
      id: GO:0004867
      label: serine-type endopeptidase inhibitor activity
    locations:
      - id: GO:0005576
        label: extracellular region