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The lipocalin protein family: structural and sequence overview
Abstract
Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the fatty acid binding proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.
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“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [20]
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Cites
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,445
The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679
Self-citationThe PROSITE database, its status in 1999
Hofmann, K., Bücher, P., Falquet, L., & Bairoch, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.215 · Cited by 1,092
Green, N. M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)84259-j · Cited by 1,020
Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin
Brownlow, S., Morais-Cabral, J. H., Cooper, R. A., Flower, D. R., Yewdall, S. J., Polikarpov, I., North, A. C. T., & Sawyer, L. (1997) · Structure · doi:10.1016/s0969-2126(97)00205-0 · Cited by 714
Self-citationLipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L. J., Winter, N. S., Xu, Z., Bernlohr, D., Cowan, S. W., & Jones, A. T. (1994) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60639-7 · Cited by 483
Borgstahl, G. E. O., Williams, D. R., & Getzoff, E. D. (1995) · Biochemistry · doi:10.1021/bi00019a004 · Cited by 438
Harpaz, Y., & Chothia, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1312 · Cited by 435
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
Böcskei, Z., Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., & North, A. C. T. (1992) · Nature · doi:10.1038/360186a0 · Cited by 361
Self-citationStructure and sequence relationships in the lipocalins and related proteins
Flower, D. R., North, A. C. T., & Attwood, T. K. (1993) · Protein Science · doi:10.1002/pro.5560020507 · Cited by 342
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Ruiz, M., Sánchez, D., Correnti, C., Strong, R. K., & Ganfornina, M. D. (2013) · FEBS Journal · doi:10.1111/febs.12394 · Cited by 59
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Christoffersen, C., & Nielsen, L. B. (2013) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328361f6ad · Cited by 57
Schultz, L. W., Liu, L., Cegielski, M., & Hastings, J. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409335102 · Cited by 56
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Fang, W., Xu, L., Lu, X., Liao, L., Cai, W., Shen, Z., & Li, E. (2007) · Biochemical Journal · doi:10.1042/bj20060836 · Cited by 54
Cabré, A., Lázaro, I., Girona, J., Manzanares, J. M., Marimón, F., Plana, N., Heras, M., & Masana, L. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2007.094672 · Cited by 53
Strope, C. L., Abel, K., Scott, S., & Moriyama, E. N. (2009) · Molecular Biology and Evolution · doi:10.1093/molbev/msp174 · Cited by 52
Campanacci, V., Nurizzo, D., Spinelli, S., Valencia, C., Tegoni, M., & Cambillau, C. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00199-1 · Cited by 52
Li, Y., Jin, K., Bunker, E. N., Zhang, X., Luo, X., Liu, X., & Hao, B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708677115 · Cited by 52
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Di Grande, A., Giuffrida, C., Carpinteri, G., Narbone, G., Pirrone, G., Di Mauro, A., Calandra, S., Noto, P., Moli, C. L., Alongi, B., et al. (2009) · PubMed · Cited by 52
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Zhao, C., Hoeppner, A., Xu, Q.-Z., Gärtner, W., Scheer, H., Zhou, M., & Zhao, K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715495114 · Cited by 52
Wojnar, P., Lechner, M., & Redl, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210922200 · Cited by 52
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Li, J., Ram, G., Gast, K., Chen, X., Barasch, K., Mori, K., Schmidt-Ott, K. M., Wang, J., Kuo, H.-C., Savage‐Dunn, C., et al. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00260.2004 · Cited by 52
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Jachimska, B., Świątek, S., Loch, J. I., Lewiński, K., & Luxbacher, T. (2018) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2018.01.010 · Cited by 51
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Soni, S. S., Pophale, R., & Ronco, C. (2011) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2011.664 · Cited by 50
Juul‐Madsen, H. R., Viertlboeck, B. C., Härtle, S., Smith, A. L., & Göbel, T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-396965-1.00007-8 · Cited by 58
Bastos, R. G., Ueti, M. W., Guerrero, F. D., Knowles, D. P., & Scoles, G. A. (2009) · Parasites & Vectors · doi:10.1186/1756-3305-2-57 · Cited by 49
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Wang, B., Kou, S., Lin, Z., & Shi, J. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118160 · Cited by 49
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Salier, J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00144-8 · Cited by 49
Stepanenko, O. V., Marabotti, A., Kuznetsova, I. М., Константинович, Т. К., Fini, C., Varriale, A., Staiano, M., Rossi, M., & D’Auria, S. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21658 · Cited by 48
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Grolli, S., Merli, E., Conti, V., Scaltriti, E., & Ramoni, R. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05510.x · Cited by 47
Assumpção, T. C. F., Eaton, D. P., Pham, V. M., Francischetti, I. M. B., Aoki, V., Filho, G. H., Rivitti, E. A., Valenzuela, J. G., Diaz, L. A., & Ribeiro, J. M. C. (2012) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.2012.11-0690 · Cited by 47
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Chruszcz, M., Kapingidza, A. B., Dolamore, C., & Kowal, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208276 · Cited by 48
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Goss, R. (2003) · Planta · doi:10.1007/s00425-003-1044-1 · Cited by 46
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Pickel, B., Pfannstiel, J., Steudle, A., Lehmann, A., Gerken, U., Pleiss, J., & Schaller, A. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08580.x · Cited by 45
Roli, L., Pecoraro, V. L., & Trenti, T. (2017) · The International Journal of Biological Markers · doi:10.5301/jbm.5000245 · Cited by 45
Parker, C. L., & Sodetz, J. M. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(02)00121-9 · Cited by 45
Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla
Earhart, C. A., Vetting, M. W., Gosu, R., Michaud‐Soret, I., QUE, L. J., & Ohlendorf, D. H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.221 · Cited by 45
Tan, Y. W., Chan, S. L., Ong, T. C., Yit, L. Y., Tiong, Y. S., Chew, F. T., Sivaraman, J., & Mok, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807209200 · Cited by 44
Attardo, G. M., Güz, N., Strickler-Dinglasan, P., & Aksoy, S. (2006) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2006.07.007 · Cited by 44
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Tromelin, A., Andriot, I., & Guichard, É. (2006) · Elsevier eBooks · doi:10.1533/9781845691400.2.172 · Cited by 44
Oba, Y., Shimasaki, Y., Oshima, Y., Satone, H., Kitano, T., Nakao, M., Kawabata, S., & Honjo, T. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm119 · Cited by 44
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Ganfornina, M. D., Sánchez, D., Pagano, A., Tonachini, L., DESCALZI‐CANCEDDA, F., & Martı́nez, S. (2004) · Developmental Dynamics · doi:10.1002/dvdy.20193 · Cited by 44
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Parker, M., Houston, S., Pětrošová, H., Lithgow, K., Hof, R., Charmaine, W., Wei-Chien, K., Lin, Y., Moriarty, T. J., Ebady, R., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005919 · Cited by 43
Reis, C. V., de Andrade, S. A., Ramos, O. H. P., Ramos, C. R. R., Ho, P. L., Batista, I. D. F. C., & Chudzinski‐Tavassi, A. M. (2006) · Biochemical Journal · doi:10.1042/bj20060325 · Cited by 43
Diarrassouba, F., Liang, L., Remondetto, G. E., & Subirade, M. (2013) · Food Research International · doi:10.1016/j.foodres.2013.03.025 · Cited by 42
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di Masi, A., Trezza, V., Leboffe, L., & Ascenzi, P. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.02.049 · Cited by 45
Zhang, Y., Qiao, S.-K., Wang, R., & Guo, X. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.04.018 · Cited by 41
Ramoni, R., Stefano Bellucci, A., Grycznyski, I., Grycznyski, Z., Grolli, S., Staiano, M., Bellis, G. D., Micciulla, F., Pastore, R., Tiberia, A., et al. (2007) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/19/39/395012 · Cited by 42
Assumpção, T. C. F., Alvarenga, P. H., Ribeiro, J. M. C., Andersen, J. F., & Francischetti, I. M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.152835 · Cited by 41
Huang, Q., Liao, X., Yang, X., Luo, Y., Lin, P., Zeng, Q.-H., Bai, H., Jiang, B., Pan, Y., Zhang, F., et al. (2020) · Plant Biotechnology Journal · doi:10.1111/pbi.13533 · Cited by 41
Shimasaki, Y., Oshima, Y., Yokota, Y., Kitano, T., Nakao, M., Kawabata, S., Imada, N., & Honjo, T. (2002) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5620210616 · Cited by 41
Liu, X., Li, Y., Chen, S., Yang, J., Jing, J., Li, J., Wu, X., Wang, J., Wang, J., Zhang, G., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154756 · Cited by 41
Rodríguez-Amigo, B., Delcanale, P., Rotger, G., Juárez‐Jiménez, J., Abbruzzetti, S., Summer, A., Agut, M., Luque, F. J., Nonell, S., & Viappiani, C. (2014) · Journal of Dairy Science · doi:10.3168/jds.2014-8691 · Cited by 40
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Matz, J. M., Drepper, B., Blum, T. B., van Genderen, E., Burrell, A., Martin, P., Stach, T., Collinson, L., Abrahams, J. P., Matuschewski, K., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001153117 · Cited by 40
Immonen, A. K., Farci, S., Taivainen, A. H., Partanen, J., Pouvelle‐Moratille, S., Närvänen, A. T. O., Kinnunen, T. T., Saarelainen, S. A., Rytkönen-Nissinen, M. A., Maillère, B., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.6.3614 · Cited by 40
Unno, K., Sumiyoshi, A., Konishi, T., Hayashi, M., Taguchi, K., Muguruma, Y., Inoue, K., Iguchi, K., Nonaka, H., Kawashima, R., et al. (2020) · Nutrients · doi:10.3390/nu12010174 · Cited by 39
Schwarz, A., Helling, S., Collin, N., Teixeira, C., Medrano-Mercado, N., Hume, J. C. C., Assumpção, T. C. F., Marcus, K., Stephan, C., Meyer, H. E., et al. (2009) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000532 · Cited by 39
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Ribeiro, J. M. C., Assumpção, T. C. F., & Francischetti, I. M. B. (2012) · Psyche A Journal of Entomology · doi:10.1155/2012/470436 · Cited by 39
Retinol-binding protein 2 (RBP2): biology and pathobiology
Blaner, W. S., Brun, P., Calderon, R. M., & Golczak, M. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1768207 · Cited by 41
El-Halfawy, O. M., Klett, J., Ingram, R. J., Loutet, S. A., Murphy, M. E. P., Martín‐Santamaría, S., & Valvano, M. A. (2017) · mBio · doi:10.1128/mbio.00225-17 · Cited by 40
Fan, L., Xie, P., Wang, Y., Liu, X., Li, Y., & Zhou, J. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.05.033 · Cited by 38
Valashedi, M. R., Roushandeh, A. M., Tomita, K., Kuwahara, Y., Pourmohammadi-Bejarpasi, Z., Kozani, P. S., Sato, T., & Roudkenar, M. H. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120704 · Cited by 38
Esposito, V., Musi, V., de Chiara, C., Veggi, D., Serruto, D., Scarselli, M., Kelly, G. P., Pizza, M., & Pastore, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.289314 · Cited by 38
Carel, C., Marcoux, J., Réat, V., Parra, J., Latgé, G., Laval, F., Demange, P., Burlet-Schiltz, O., Milon, A., Daffé, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617888114 · Cited by 36
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Buarque, D. S., Braz, G. R. C., Martins, R. M., Tanaka-Azevedo, A. M., Gomes, C. M., Oliveira, F. A., Schenkman, S., & Tanaka, A. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061203 · Cited by 37
Mauchamp, B., Royer, C., Garel, A., Jalabert, A., Rocha, M. D., Grenier, A.-M., Labas, V., Vinh, J., Mita, K., Kadono‐Okuda, K., et al. (2006) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2006.05.006 · Cited by 37
Identification of the bovine α1-acid glycoprotein in colostrum and milk
Ceciliani, F., Pocacqua, V., Provasi, E., Comunian, C., Bertolini, A., Bronzo, V., Moroni, P., & Sartorelli, P. (2005) · Veterinary Research · doi:10.1051/vetres:2005029 · Cited by 37
Binding of Zona Binding Inhibitory Factor-1 (ZIF-1) from Human Follicular Fluid on Spermatozoa
Chiu, P. C. N., Koistinen, R., Koistinen, H. K., Seppälä, M. T., Lee, C., & Yeung, W. S. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212086200 · Cited by 37
Emerging Concepts of Apolipoprotein D with Possible Implications for Breast Cancer
Søiland, H., Søreide, K., Janssen, E. A. M., Kørner, H., Baak, J. P. A., & Søreide, J. A. (2007) · Analytical Cellular Pathology · doi:10.1155/2007/487235 · Cited by 38
Acute phase lipocalin Ex‐FABP is involved in heart development and cell survival
Gentili, C., Tutolo, G., Zerega, B., Marco, E. D., Cancedda, R., & Cancedda, F. D. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20165 · Cited by 36
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Metadata
- Authors
- Flower, D. R., North, A. C. T., & Sansom, C. E.
- Affiliations
- Jenner Institute (GB)
- University of Leeds (GB)
- University of London (GB)
- Corresponding author
- Flower, Darren R.
- ORCID
- Flower, Darren R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 1482
- Issue
- 1-2
- Pages
- 9-24
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2038438679
- Cited by
- 868
- References
- 59
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 25 · 2023: 27 · 2022: 29 · 2021: 33 · 2020: 37 · 2019: 27 · 2018: 29 · 2017: 35 · 2016: 46 · 2015: 39 · 2014: 51 · 2013: 37 · 2012: 60
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- lipocalin, protein superfamilies, conserved motifs, fatty acid binding protein, avidin, metalloproteinase inhibitors, protein structure conservation
- MeSH terms
- Fatty Acid-Binding Protein 7, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Lactoglobulins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Sequence Homology, Amino Acid, Insect Proteins, Tumor Suppressor Proteins, Fatty Acid-Binding Proteins
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