Summary: First Longin domain of FUZ, MON1 and HPS1
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First Longin domain of FUZ, MON1 and HPS1 Provide feedback
This entry is specific to the first Longin domain of the HerMon (Hermansky-Pudlak syndrome and MON1-CCZ1) family, including protein sequences of FUZ, MON1 and HPS1 families [1,3,5]. The Mon1/Ccz1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking [2]. The Hps1/Hps4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules [3]. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [4,6].
Literature references
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Kinch LN, Grishin NV; , Protein Sci. 2006;15:2669-2674.: Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution. PUBMED:17075139 EPMC:17075139
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Kiontke S, Langemeyer L, Kuhlee A, Schuback S, Raunser S, Ungermann C, Kummel D;, Nat Commun. 2017;8:14034.: Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1. PUBMED:28051187 EPMC:28051187
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Gerondopoulos A, Langemeyer L, Liang JR, Linford A, Barr FA;, Curr Biol. 2012;22:2135-2139.: BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor. PUBMED:23084991 EPMC:23084991
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Gray RS, Abitua PB, Wlodarczyk BJ, Szabo-Rogers HL, Blanchard O, Lee I, Weiss GS, Liu KJ, Marcotte EM, Wallingford JB, Finnell RH;, Nat Cell Biol. 2009;11:1225-1232.: The planar cell polarity effector Fuz is essential for targeted membrane trafficking, ciliogenesis and mouse embryonic development. PUBMED:19767740 EPMC:19767740
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Sanchez-Pulido L, Ponting CP;, Bioinformatics. 2019 Sep 28. pii: 5575; [Epub ahead of print]: Hexa-Longin domain scaffolds for inter-Rab signalling. PUBMED:31562761 EPMC:31562761
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Toriyama M, Lee C, Taylor SP, Duran I, Cohn DH, Bruel AL, Tabler JM, Drew K, Kelly MR, Kim S, Park TJ, Braun DA, Pierquin G, Biver A, Wagner K, Malfroot A, Panigrahi I, Franco B, Al-Lami HA, Yeung Y, Choi YJ, Duffourd Y, Faivre L, Riviere JB, Chen J, Liu KJ, Marcotte EM, Hildebrandt F, Thauvin-Robinet C, Krakow D, Jackson PK, Wallingford JB;, Nat Genet. 2016;48:648-656.: The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery. PUBMED:27158779 EPMC:27158779
This tab holds annotation information from the InterPro database.
InterPro entry IPR043972
This entry represents the first Longin domain found in FUZ, MON1 and HPS1 proteins.
Longin domains are evolutionarily conserved regions widely distributed among eukaryotes, involved in membrane dynamic regulation and exhibit similarities in primary sequence and secondary structure. Longin-like domains are found in FUZ and related proteins, such as the MON1 and HPS1 proteins [ PUBMED:17075139 , PUBMED:23084991 , PUBMED:31562761 ]. The MON1/CCZ1 complex (MC1) is the GDP/GTP exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 during vesicular trafficking [ PUBMED:28051187 ]. The HPS1/HPS4 complex (BLOC-3) is a Rab32 and Rab38 GEF and is required for biogenesis of melanosomes and platelet dense granules [ PUBMED:23084991 ]. Inturned (INTU) and Fuzzy (FUZ) proteins interact as members of the ciliogenesis and planar polarity effector (CPLANE) complex that controls recruitment of intraflagellar transport machinery to the basal body of primary cilia [ PUBMED:19767740 , PUBMED:27158779 ]. Structurally, these domains are composed of an alpha/beta fold which contains five anti-parallel beta-strands organised as a central beta-sheet and around it, two alpha-helices [ PUBMED:31562761 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | vesicle-mediated transport (GO:0016192) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan PF (CL0431), which has the following description:
The families here all show the Profilin-like fold, and represent both the Profilin (actin-binding protein) (55770) and the Roadblock/LC7 domain-type (103196) superfamilies.
The clan contains the following 21 members:
Clat_adaptor_s FNIP_N Fuz_longin_1 Fuz_longin_2 Fuz_longin_3 Intu_longin_1 Intu_longin_2 Intu_longin_3 LAMTOR5 Longin Longin_2 MAPKK1_Int Nyv1_N Profilin Robl_LC7 Sedlin_N SLM4 SRP-alpha_N SRX Sybindin uDENNAlignments
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Seed (38) |
Full (2704) |
Representative proteomes | UniProt (4756) |
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RP15 (457) |
RP35 (1126) |
RP55 (2138) |
RP75 (2926) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (38) |
Full (2704) |
Representative proteomes | UniProt (4756) |
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RP15 (457) |
RP35 (1126) |
RP55 (2138) |
RP75 (2926) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
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Curation
Seed source: | Luis Sanchez-Pulido |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 38 |
Number in full: | 2704 |
Average length of the domain: | 123.10 aa |
Average identity of full alignment: | 30 % |
Average coverage of the sequence by the domain: | 20.24 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 125 | ||||||||||||
Family (HMM) version: | 2 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Fuz_longin_1 domain has been found. There are 2 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 sequence.
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