Summary: AN1-like Zinc finger
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AN1 zinc finger Edit Wikipedia article
Solution structure of the zf-an1 domain from arabiopsis thaliana f5o11.17 protein
In molecular biology, the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1 SWISSPROT, a ubiquitin-like protein in Xenopus laevis. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.
Certain stress-associated proteins (SAP) contain AN1 domain, often in combination with A20 zinc finger domains (SAP8) or C2H2 domains (SAP16). For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. The interact of Znf216 with IKK-gamma and RIP is mediated by the A20 zinc-finger domain, while its interaction with TRAF6 is mediated by the AN1 zinc-finger domain; therefore, both zinc-finger domains are involved in regulating the immune response. The AN1 zinc finger domain is also found in proteins containing a ubiquitin-like domain, which are involved in the ubiquitination pathway. Proteins containing an AN1-type zinc finger include:
- Ascidian posterior end mark 6 (pem-6) protein .
- Human immunoglobulin mu binding protein 2 (SMUBP-2), mutations in which cause muscular atrophy with respiratory distress type 1.
AN1-type zinc finger domains are widely present across diverse euryarchaeota and thaumarchaeota, where they are often fused to membrane-associated peptidase domains such as the rhomboid family serine peptidase, transglutaminase-like thiol peptidases of the papain fold, and Zn-dependent metallopeptidases. Archaeal AN1 domains are also linked to transmembrane helices, and domains such as DNAJ and SCP/PR1. These fusions suggest membrane-associated roles for AN1 domain containing proteins in archaea, such as in proteolytic processing of polypeptides and in regulating protein folding or stability. The architectural syntax is remarkably similar to that of the prokaryotic B-box zinc finger and LIM domains. 
- Linnen JM, Bailey CP, Weeks DL (June 1993). "Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins". Gene 128 (2): 181â8. doi:10.1016/0378-1119(93)90561-G. PMID 8390387.
- Vij S, Tyagi AK (December 2006). "Genome-wide analysis of the stress associated protein (SAP) gene family containing A20/AN1 zinc-finger(s) in rice and their phylogenetic relationship with Arabidopsis". Mol. Genet. Genomics 276 (6): 565â75. doi:10.1007/s00438-006-0165-1. PMID 17033811.
- Huang J, Teng L, Li L, Liu T, Li L, Chen D, Xu LG, Zhai Z, Shu HB (April 2004). "ZNF216 Is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation". J. Biol. Chem. 279 (16): 16847â53. doi:10.1074/jbc.M309491200. PMID 14754897.
- Satou Y, Satoh N (December 1997). "Posterior end mark 2 (pem-2), pem-4, pem-5, and pem-6: maternal genes with localized mRNA in the ascidian embryo". Dev. Biol. 192 (2): 467â81. doi:10.1006/dbio.1997.8730. PMID 9441682.
- Duan W, Sun B, Li TW, Tan BJ, Lee MK, Teo TS (October 2000). "Cloning and characterization of AWP1, a novel protein that associates with serine/threonine kinase PRK1 in vivo". Gene 256 (1-2): 113â21. doi:10.1016/S0378-1119(00)00365-6. PMID 11054541.
- Liepinsh E, Leonchiks A, Sharipo A, Guignard L, Otting G (February 2003). "Solution structure of the R3H domain from human Smubp-2". J. Mol. Biol. 326 (1): 217â23. doi:10.1016/S0022-2836(02)01381-5. PMID 12547203.
- Burroughs AM, Iyer LM, Aravind L (July 2011). "Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system". Mol Biosyst. 7 (1): 2261–77. doi:10.1039/C1MB05061C. PMID 21547297.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
AN1-like Zinc finger Provide feedback
Zinc finger at the C-terminus of An1 Q91889 a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000058
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1 SWISSPROT, a ubiquitin-like protein in Xenopus laevis [PUBMED:8390387]. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.
Certain stress-associated proteins (SAP) contain AN1 domain, often in combination with A20 zinc finger domains (SAP8) or C2H2 domains (SAP16) [PUBMED:17033811]. For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. The interact of Znf216 with IKK-gamma and RIP is mediated by the A20 zinc-finger domain, while its interaction with TRAF6 is mediated by the AN1 zinc-finger domain; therefore, both zinc-finger domains are involved in regulating the immune response [PUBMED:14754897]. The AN1 zinc finger domain is also found in proteins containing a ubiquitin-like domain, which are involved in the ubiquitination pathway [PUBMED:8390387]. Proteins containing an AN1-type zinc finger include:
- Ascidian posterior end mark 6 (pem-6) protein [PUBMED:9441682].
- Human AWP1 protein (associated with PRK1), which is expressed during early embryogenesis [PUBMED:11054541].
- Human immunoglobulin mu binding protein 2 (SMUBP-2), mutations in which cause muscular atrophy with respiratory distress type 1 [PUBMED:12547203].
More information about these proteins can be found at Protein of the Month: Zinc Fingers [PUBMED:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Author:||Bateman A, SMART|
|Number in seed:||181|
|Number in full:||1823|
|Average length of the domain:||42.70 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||20.23 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the zf-AN1 domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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