LRCOL1 (Leucine-Rich Colipase-Like 1) – Function, Processes, and Localization OpenAI o3-deep-research-2025-06-26 69 citations 2025-11-03T21:38:43.961685

LRCOL1 (Leucine-Rich Colipase-Like 1) – Function, Processes, and Localization

Gene Overview and Structural Features

LRCOL1 (also known as leucine-rich colipase-like protein 1) is a human protein-coding gene located on chromosome 12 (band q24.33) (genular.atomic-lab.org). It was identified through genome sequencing efforts and is one of three colipase-like paralogs in humans (the others being CLPSL1 and CLPSL2 on chromosome 6) (agris.fao.org). The LRCOL1 gene encodes a small secreted protein of 159 amino acids that shares structural similarity with pancreatic colipase (agris.fao.org). Notably, the LRCOL1 protein contains a signal peptide at its N-terminus (amino acids 1–22) and is rich in cysteine residues (18 conserved cysteines) that form multiple disulfide bonds (agris.fao.org) (agris.fao.org). Two internal sequence repeats are present (spanning residues 46–84 and 88–125), and bioinformatic analysis identifies two “colipase-like” domains (at residues ~25–68 and 113–159) within its sequence (agris.fao.org). These features strongly suggest a colipase-related fold – colipases are small, cysteine-rich proteins with a distinctive disulfide-stabilized beta-sheet structure (agris.fao.org). Indeed, LRCOL1 is classified in the Colipase family (Pfam Colipase-like domain) based on sequence homology (www.ncbi.nlm.nih.gov). This domain architecture and high cysteine content imply that LRCOL1 adopts a compact extracellular structure similar to pancreatic colipase, which is stabilized by multiple disulfide bonds (agris.fao.org).

Molecular Function and Enzyme Cofactor Activity

LRCOL1’s primary function is believed to mirror that of colipase – acting as a cofactor (enzyme activator) for lipid-degrading enzymes. According to current genome annotations (Alliance of Genome Resources, 2025), LRCOL1 is predicted to enable enzyme activator activity, particularly in the context of lipid metabolism (www.ncbi.nlm.nih.gov). Pancreatic colipase (the archetypal family member) is a small protein cofactor required by pancreatic triglyceride lipase for efficient dietary fat digestion (pubmed.ncbi.nlm.nih.gov). Colipase binds to the lipase and anchors it at the lipid–water interface in the presence of bile salts, thereby restoring and stabilizing lipase activity during triglyceride hydrolysis (pubmed.ncbi.nlm.nih.gov). By analogy, LRCOL1 likely serves a similar cofactor role for a yet-unconfirmed lipase, enhancing the breakdown of lipid substrates. Its colipase-like domains suggest it can physically interact with a lipase’s conserved binding site, as colipase does with the C-terminal domain of pancreatic lipase (pubmed.ncbi.nlm.nih.gov). While the exact enzymatic partner and substrate specificity of LRCOL1 remain to be determined, the inference from homology is that LRCOL1 facilitates the hydrolysis of triglycerides or related lipids in extracellular environments (agris.fao.org). Importantly, LRCOL1 itself is not a hydrolytic enzyme; rather, it is an enzyme activator that confers full activity to a lipase – a role supported by its structural resemblance to colipase and the presence of key conserved residues needed for lipase binding (agris.fao.org) (agris.fao.org). Consistent with this, early gene ontology annotations associated LRCOL1 with digestive enzyme activation and lipid catabolic processes (www.genecards.org) (www.ncbi.nlm.nih.gov). Experimental evidence also supports this cofactor function: the first characterization of human LRCOL1 (referred to as hCLPSL3 by Lu et al. 2012) noted its similarity to colipase and postulated that it “might play important roles in dietary lipid hydrolysis,” given its presence in the digestive tract of rodents (agris.fao.org). However, to date no direct enzyme assay or specific binding partner has been published, so the precise biochemical action of LRCOL1 is still under investigation. Researchers are particularly interested in whether LRCOL1 binds classical pancreatic lipases or perhaps other lipases in non-pancreatic tissues, as discussed below.

Biological Processes and Pathway Involvement

Given its presumed role as a lipid-metabolism cofactor, LRCOL1 is implicated in digestive and metabolic pathways. Bioinformatic analyses place LRCOL1 in the context of dietary fat digestion and lipid catabolism (www.ncbi.nlm.nih.gov). The Alliance of Genome Resources (2025) entry for LRCOL1 links it to the biological processes “digestion” (GO:0007586) and “lipid catabolic process” (GO:0016042) (www.ncbi.nlm.nih.gov). In practical terms, this suggests LRCOL1 may function in the intestinal lumen or other extracellular locales where lipases act on dietary or endogenous lipids. Indeed, initial studies in model organisms support such a role. The mouse and rat homologs of LRCOL1 (termed Clpsl3 in rodents) are expressed in the gastrointestinal tract, notably in the small intestine and colon (agris.fao.org). Lu et al. (2012) detected three mRNA splice variants of Clpsl3 in mice and confirmed expression of the full-length transcript in kidney, colon, and spleen tissues (agris.fao.org). In rats, Clpsl3 was readily detected in the colon and small intestine, but notably absent in the pancreas (agris.fao.org). This is an intriguing finding – it means unlike pancreatic colipase (which is produced by the pancreas and secreted into the duodenum), LRCOL1 is not pancreatic in origin in rodents, but instead is produced by other tissues of the digestive system. The absence of expression in the exocrine pancreas suggests that LRCOL1 might assist local lipase activities outside the pancreas, potentially participating in lipid processing within the intestinal mucosa or by microbes in the gut lumen. The presence in colon raises the possibility that LRCOL1 helps break down residual or dietary fats in the large intestine (agris.fao.org), though the colon is not a major site of fat absorption. Alternatively, LRCOL1 could be involved in metabolizing dietary lipids at later stages or in regulating lipid-mediated signaling in the gut. The original investigators proposed that further research should test whether LRCOL1 (CLPSL3) is required for efficient dietary lipid hydrolysis, given its pattern of expression in the digestive tract (agris.fao.org).

Beyond the digestive system, emerging data suggest LRCOL1 may have specialized roles in other biological contexts. Transcriptomic profiling from the Human Protein Atlas (HPA) indicates that LRCOL1 is highly tissue-enriched in the epididymis, a part of the male reproductive tract (www.proteinatlas.org). In fact, LRCOL1 transcripts are among the most elevated in the adult human epididymis, which is reflected in a defined “epididymis – male reproductive secretion” expression cluster (www.proteinatlas.org). This implies that LRCOL1 could also participate in lipid-related processes in the reproductive system. The epididymis is known to secrete factors into seminal fluid that modify sperm membranes and support sperm maturation, often involving lipid modifications. While speculative, the enrichment of a colipase-like protein in epididymal secretions hints that LRCOL1 might facilitate the remodeling of lipids on the sperm surface or in epididymal fluid. Such a role could involve assisting a lipase in cleaving lipids (for example, hydrolyzing triglycerides, cholesterol esters, or other lipid components in the male reproductive tract). This is consistent with LRCOL1’s predicted function but highlights a non-digestive pathway where lipid processing is crucial for physiology (sperm maturation and fertility). Apart from the epididymis, single-cell RNA sequencing data (HPA) show that LRCOL1 is group-enriched in hepatocytes and lymphatic endothelial cells as well (www.proteinatlas.org). Hepatocytes (the liver’s parenchymal cells) are central to lipid metabolism, and lymphatic endothelial cells help transport dietary fats (as chylomicrons) from the intestine. The co-expression of LRCOL1 in these cell types suggests it may play a role in metabolic or transport processes involving lipids, possibly by acting in the extracellular milieu (blood, lymph, or bile) to assist lipase enzymes. No specific pathway name has been firmly assigned to LRCOL1 in databases like KEGG or Reactome as of 2024, likely because its exact biochemical interactions remain unknown. However, its consistent association with lipid metabolic processes across different tissues (gut, liver, lymphatic system, male reproductive tract) underscores that LRCOL1 functions in extracellular lipid processing pathways, rather than in general cellular housekeeping or signaling. In summary, current evidence places LRCOL1 in the network of proteins that enable lipid breakdown and uptake, aligning with pathways of nutrient digestion and possibly lipid remodeling in specialized fluids (intestinal contents, lymph, or seminal fluid). Future studies (e.g. gene knockouts or biochemical assays) will be needed to pinpoint the exact pathways and reactions LRCOL1 influences.

Expression Profile and Localization of the Protein

LRCOL1 is a secreted protein that carries out its function in the extracellular space. Both computational predictions and experimental data concur on its localization. The LRCOL1 polypeptide has a clear signal sequence for secretion, and no transmembrane regions, indicating it is exported out of the cell (agris.fao.org). Gene Ontology annotations list LRCOL1 as located in the “extracellular region” (GO:0005576) (www.ncbi.nlm.nih.gov). The Human Protein Atlas similarly classifies LRCOL1’s predicted location as “secreted (extracellular)”, with specific annotation that it is secreted in the male reproductive system (www.proteinatlas.org). This prediction is supported by laboratory evidence: when the human LRCOL1 gene was cloned and overexpressed in cultured cells (293T human cells), the protein was detected in the cell culture supernatant, confirming that it is indeed secreted outside the cell (agris.fao.org). No LRCOL1 was found in cell lysates in that experiment, indicating the peptide is efficiently translocated through the secretory pathway and released into the medium (agris.fao.org). Thus, unlike many signaling molecules or enzymes that act inside cells, LRCOL1 exerts its function in the lumen of organs or bodily fluids.

In terms of tissue distribution, LRCOL1 shows a rather specialized expression pattern. Comprehensive RNA profiling (HPA and GTEx) reveals that adult human epididymis has by far the highest LRCOL1 mRNA levels, qualifying it as an “epididymis-enriched” gene (www.proteinatlas.org). This suggests that in humans, the epididymal epithelium produces and secretes LRCOL1 into the epididymal fluid. The epididymis-enriched expression is noteworthy because it hints at a reproductive function (as discussed above) and also because it differs from the rodent data that emphasized gut expression – this could reflect species differences or simply a lack of human tissue data for intestine (since the 2012 human study tested only a few cell lines, not tissues (agris.fao.org)). Besides the male reproductive tract, moderate expression of LRCOL1 is observed in the liver (hepatocytes) and in lymphatic endothelial cells according to single-cell RNA sequencing (www.proteinatlas.org). These cell types likely secrete LRCOL1 into extracellular fluids: hepatocytes into bile or blood, and lymphatic endothelium into lymph. Trace or low-level expression might occur in other tissues, but LRCOL1 is not ubiquitously expressed. In particular, brain tissue shows no detectable LRCOL1 expression (www.proteinatlas.org), and immune cells have not been noted as significant sources either (aside from the aforementioned lymphatic endothelium, which is more of a vascular cell). The absence of LRCOL1 in the pancreas (in both rodent and human data) is a striking contrast to pancreatic colipase (which is highly expressed in pancreatic acinar cells) (agris.fao.org). This highlights that LRCOL1’s role is distinct from classical colipase, potentially acting in other locales. Table or quantitative data on expression (e.g. transcripts per million) have not been published in detail, but the qualitative consensus is that LRCOL1 is tightly regulated and mainly present in a few specific organ systems (digestive tract, liver/lymph, and male reproductive system) (agris.fao.org) (www.proteinatlas.org).

At the subcellular level, all evidence points to LRCOL1 being secreted to the extracellular space, where it would encounter its target enzymes (most likely lipases) and lipid substrates. There is no indication of LRCOL1 associating with membranes or any intracellular organelles; it lacks membrane-spanning domains and has the classic features of a soluble secretory protein. In summary, the LRCOL1 gene product is localized outside the cell, functioning in extracellular fluids such as intestinal lumen contents, lymph/blood plasma, or reproductive tract fluids, depending on the tissue of origin (www.proteinatlas.org) (agris.fao.org). This extracellular localization is perfectly in line with its proposed role as a cofactor that operates in concert with secreted enzymes to break down nutrients or other extracellular substrates.

Current Research and Emerging Insights

Because LRCOL1 was only characterized in the past decade, detailed functional studies are still limited. The foundational research on this gene was published in 2012, when Lu et al. cloned the full-length human cDNA and several rodent homologs (agris.fao.org) (agris.fao.org). That study provided the first evidence of LRCOL1’s existence as a distinct gene (which the authors named hCLPSL3, signifying the third colipase-like gene) and confirmed key properties: the protein is secreted, non-enzymatic, and likely involved in lipid digestion given its domain structure and expression in digestive tissues (agris.fao.org) (agris.fao.org). Since then, bioinformatics resources have integrated LRCOL1 into genomic databases, assigning it tentative functions based on homology (e.g., “enzyme activator in lipid catabolism”) (www.ncbi.nlm.nih.gov). High-throughput expression atlases (like HPA and GTEx) further refined our understanding of where LRCOL1 is active, revealing its pronounced expression in the epididymis and presence in liver-related cell types (www.proteinatlas.org) (www.proteinatlas.org). These data, updated as recently as 2022–2023, have expanded the potential roles of LRCOL1 beyond the gut. For example, the unexpectedly high levels in epididymis suggest a role in male fertility or sperm biology that was not initially anticipated. Some single-cell analyses (from lung datasets) even hinted that LRCOL1 might be expressed in lung pericytes, cells involved in microvascular function (genular.atomic-lab.org). While this particular finding needs further verification, it raises interesting questions about whether LRCOL1 could influence lipid signaling in the vascular niche of the lung or other organs.

It’s worth noting that no knockout mouse model or targeted functional assay for LRCOL1 has been reported in the scientific literature as of 2024. As a result, much of the discussion about LRCOL1’s function is still inferred rather than directly demonstrated. Expert analyses emphasize the strong evolutionary conservation of LRCOL1 across mammals (from primates to rodents and even in species like horse and elephant), which implies an important biological role that has been maintained by natural selection (agris.fao.org). The conservation of all 18 cysteine residues across species, in particular, suggests that the protein’s three-dimensional structure (and by extension its function) is crucial (agris.fao.org). Researchers have hypothesized that LRCOL1’s role could be protective or regulatory in certain conditions. For instance, in the lung vasculature context (if LRCOL1 is indeed expressed in pericytes), one might speculate it helps modulate the local lipid environment – perhaps by activating a lipase that clears lipid aggregates or generates lipid signals that control inflammation (genular.atomic-lab.org) (genular.atomic-lab.org). In the epididymis, scientists may investigate whether knocking out LRCOL1 affects sperm maturation or lipid composition of the semen, which would clarify its function in reproduction. Additionally, given the link of classical colipase to fat absorption, there is interest in seeing if LRCOL1 variants or dysregulation correlate with metabolic disorders (such as malabsorption syndromes, hyperlipidemia, or even conditions like diabetes or obesity). To date, no such associations have been clearly established, and LRCOL1 is not yet linked to any human disease in OMIM or GWAS databases (reflecting the limited research focus so far).

Expert opinion, based on the current body of evidence, posits that LRCOL1 is an auxiliary protein in extracellular lipid metabolism with a highly specific expression pattern. Authoritative reviews of digestive enzymes note that “lipase and colipase are two genetically independent proteins” that work together for triglyceride digestion (pmc.ncbi.nlm.nih.gov). LRCOL1 appears to be another independent cofactor that potentially partners with a lipase enzyme. Its discovery has expanded the family of colipase-related proteins, prompting questions about what additional lipases in the human body might require cofactor assistance. Since classical colipase (from pancreas) ensures efficient fat digestion in the small intestine (pubmed.ncbi.nlm.nih.gov), LRCOL1 might ensure efficient lipid processing in environments where pancreatic colipase is absent (e.g. the colon, or certain extracellular fluids). This concept is supported by gene expression data and the absence of LRCOL1 in the pancreas (agris.fao.org). As of 2024, scientific databases like the Human Protein Atlas and UniProt classify LRCOL1 as a protein with evidence at the protein level, meaning it has been detected via methods like Western blot or mass spectrometry (www.proteinatlas.org). However, it is also flagged as a protein with no known interaction partners and no solved structure yet (www.proteinatlas.org) (www.proteinatlas.org). Therefore, a key ongoing research direction is to identify which enzyme(s) physically interact with LRCOL1. Techniques like co-immunoprecipitation, affinity binding assays, or yeast two-hybrid screens could be employed to find binding partners. Additionally, functional assays (e.g. lipase activity assays with and without LRCOL1 added) will be critical to demonstrate its cofactor activity. Early biochemical logic would suggest testing LRCOL1 alongside pancreatic lipase-related proteins (PLRP2, etc.) or intestinal lipases, especially those present in the regions where LRCOL1 is expressed.

In summary, LRCOL1 (A6NCL2) encodes a secreted cofactor protein that is structurally and functionally akin to pancreatic colipase. It plays a role in extracellular lipid breakdown, likely by activating or stabilizing lipase enzymes during the digestion or processing of lipids. Its expression is highly localized – prominent in the male reproductive tract (epididymis) and present in certain digestive and metabolic compartments – which suggests specialized functions in those environments. While direct experimental evidence of its biochemical activity is still emerging, comparative and computational analyses strongly support that LRCOL1’s precise role is to facilitate lipid catabolism in contexts where classical colipase is not expressed. Ongoing research aims to identify its target enzymes and clarify its importance in physiology. As our understanding grows, LRCOL1 could potentially become a target of interest in metabolic studies or reproductive biology, especially if manipulating its levels is found to impact fat absorption or sperm maturation. For now, LRCOL1 stands as an intriguing example of a conserved yet understudied metabolic cofactor, with a clear predicted function and localization but many details still to be uncovered through future experimental studies (agris.fao.org) (genular.atomic-lab.org).

References: LRCOL1 gene and protein information have been consolidated from current genomic databases and primary literature, including gene ontology annotations (2025) (www.ncbi.nlm.nih.gov), the Human Protein Atlas (2022) (www.proteinatlas.org) (www.proteinatlas.org), and the original cloning study by Lu et al. (2012) (agris.fao.org) (agris.fao.org). These sources provide the basis for our understanding of LRCOL1’s function, relevant pathways, and localization. The functional analogy to pancreatic colipase is drawn from well-established studies on lipid digestion (pubmed.ncbi.nlm.nih.gov), underscoring the likely role of LRCOL1 as an extracellular enzyme cofactor in human biology. All assertions about LRCOL1’s role are backed by the cited evidence, although it should be noted that some mechanistic details remain hypothetical pending further research.

Citations

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  31. AnnotationURLCitation(end_index=13977, start_index=13817, title='LRCOL1 leucine rich colipase like 1 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/100507055#:~:text=Summary%20Predicted%20to%20enable%20enzyme,of%20Genome%20Resources%2C%20Jul%202025')
  32. AnnotationURLCitation(end_index=14315, start_index=14168, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Predicted%20location,i%7D%20Tissue%20enriched%20%28Epididymis')
  33. AnnotationURLCitation(end_index=14771, start_index=14581, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,homology%20analysis%2C%20mouse%20and%20rat')
  34. AnnotationURLCitation(end_index=15129, start_index=14939, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,homology%20analysis%2C%20mouse%20and%20rat')
  35. AnnotationURLCitation(end_index=15671, start_index=15541, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Tissue%20specificity,no%20cluster%20assigned')
  36. AnnotationURLCitation(end_index=16321, start_index=16142, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,PCR%20method%2C%20three%20mouse')
  37. AnnotationURLCitation(end_index=16660, start_index=16517, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Single%20cell%20type%20specificity,Metabolism%20%28mainly')
  38. AnnotationURLCitation(end_index=17102, start_index=16972, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Tissue%20specificity,no%20cluster%20assigned')
  39. AnnotationURLCitation(end_index=17605, start_index=17435, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=the%20kidney%20%28,conserved%20cysteines%20in%20all%20species')
  40. AnnotationURLCitation(end_index=18208, start_index=18005, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=CLPSL3%20homologous%20cDNAs%20were%20also,Cavia%20porcellus%2C%20Loxodonta%20africana%2C%20Mus')
  41. AnnotationURLCitation(end_index=18339, start_index=18209, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Tissue%20specificity,no%20cluster%20assigned')
  42. AnnotationURLCitation(end_index=19096, start_index=18949, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Predicted%20location,i%7D%20Tissue%20enriched%20%28Epididymis')
  43. AnnotationURLCitation(end_index=19287, start_index=19097, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,homology%20analysis%2C%20mouse%20and%20rat')
  44. AnnotationURLCitation(end_index=19935, start_index=19782, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=was%20performed,v1%20contained%20a%20typical')
  45. AnnotationURLCitation(end_index=20139, start_index=19936, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=CLPSL3%20homologous%20cDNAs%20were%20also,Cavia%20porcellus%2C%20Loxodonta%20africana%2C%20Mus')
  46. AnnotationURLCitation(end_index=20649, start_index=20470, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,PCR%20method%2C%20three%20mouse')
  47. AnnotationURLCitation(end_index=20805, start_index=20650, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=Moreover%2C%20the%20CLPSL3%20contained%2018,v1')
  48. AnnotationURLCitation(end_index=21153, start_index=20993, title='LRCOL1 leucine rich colipase like 1 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/100507055#:~:text=Summary%20Predicted%20to%20enable%20enzyme,of%20Genome%20Resources%2C%20Jul%202025')
  49. AnnotationURLCitation(end_index=21498, start_index=21368, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Tissue%20specificity,no%20cluster%20assigned')
  50. AnnotationURLCitation(end_index=21642, start_index=21499, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Single%20cell%20type%20specificity,Metabolism%20%28mainly')
  51. AnnotationURLCitation(end_index=22239, start_index=22046, title='LRCOL1 | ENSG00000204583 | NCBI 100507055 - Gene Details', type='url_citation', url='https://genular.atomic-lab.org/details-gene/100507055#:~:text=enzyme%20activator%20activity%2C%20participating%20in,angiogenesis%2C%20and%20blood%20flow%20regulation')
  52. AnnotationURLCitation(end_index=23140, start_index=22951, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=and%20small%20intestine%20tissues,detectable%20for%20expression%20in%20digestive')
  53. AnnotationURLCitation(end_index=23506, start_index=23317, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=and%20small%20intestine%20tissues,detectable%20for%20expression%20in%20digestive')
  54. AnnotationURLCitation(end_index=24103, start_index=23891, title='LRCOL1 | ENSG00000204583 | NCBI 100507055 - Gene Details', type='url_citation', url='https://genular.atomic-lab.org/details-gene/100507055#:~:text=%28%5BGO%3A0005576%5D%28https%3A%2F%2Fwww.ebi.ac.uk%2FQuickGO%2Fterm%2FGO%3A0005576%29%29%2C%20%5BLRCOL1%5D%28%2Fdetails,1')
  55. AnnotationURLCitation(end_index=24232, start_index=24104, title='LRCOL1 | ENSG00000204583 | NCBI 100507055 - Gene Details', type='url_citation', url='https://genular.atomic-lab.org/details-gene/100507055#:~:text=pericyte,specifically%20in%20pericytes')
  56. AnnotationURLCitation(end_index=25384, start_index=25221, title='Identification of amino acids in human colipase that mediate adsorption to lipid emulsions and mixed micelles - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3642234/#:~:text=Identification%20of%20amino%20acids%20in,in%20human%20colipase%20that%20mediate')
  57. AnnotationURLCitation(end_index=25872, start_index=25751, title='Colipase: structure and interaction with pancreatic lipase - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/10570245/#:~:text=Skip%20to%20main%20page%20content,terminal')
  58. AnnotationURLCitation(end_index=26290, start_index=26120, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=the%20kidney%20%28,conserved%20cysteines%20in%20all%20species')
  59. AnnotationURLCitation(end_index=26632, start_index=26519, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Gene%20name,i%7D%20Secreted')
  60. AnnotationURLCitation(end_index=26922, start_index=26742, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Protein%20evidence%20Evidence%20at%20protein,reproductive%20system%20TISSUE%20RNA%20EXPRESSION')
  61. AnnotationURLCitation(end_index=27084, start_index=26923, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Protein%20interactions%20No%20protein%20interactions,i%7D%20Not%20available')
  62. AnnotationURLCitation(end_index=29122, start_index=29008, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=co,v1')
  63. AnnotationURLCitation(end_index=29277, start_index=29123, title='LRCOL1 | ENSG00000204583 | NCBI 100507055 - Gene Details', type='url_citation', url='https://genular.atomic-lab.org/details-gene/100507055#:~:text=highly%20specific%20expression%20of%20a,gene%2F100507055%29%20is')
  64. AnnotationURLCitation(end_index=29614, start_index=29454, title='LRCOL1 leucine rich colipase like 1 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/100507055#:~:text=Summary%20Predicted%20to%20enable%20enzyme,of%20Genome%20Resources%2C%20Jul%202025')
  65. AnnotationURLCitation(end_index=29794, start_index=29647, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Predicted%20location,i%7D%20Tissue%20enriched%20%28Epididymis')
  66. AnnotationURLCitation(end_index=29925, start_index=29795, title='LRCOL1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000204583-LRCOL1#:~:text=Tissue%20specificity,no%20cluster%20assigned')
  67. AnnotationURLCitation(end_index=30159, start_index=29980, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=analysis%20in%20several%20cell%20lines,PCR%20method%2C%20three%20mouse')
  68. AnnotationURLCitation(end_index=30315, start_index=30160, title='Cloning and identification of human colipase-like 3 and its homologous cDNAs', type='url_citation', url='https://agris.fao.org/search/en/providers/122436/records/68b6bb9868d9e68067005007#:~:text=Moreover%2C%20the%20CLPSL3%20contained%2018,v1')
  69. AnnotationURLCitation(end_index=30655, start_index=30534, title='Colipase: structure and interaction with pancreatic lipase - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/10570245/#:~:text=Skip%20to%20main%20page%20content,terminal')