Summary: Latexin
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This is the Wikipedia entry entitled "Latexin family". More...
Latexin family Edit Wikipedia article
Latexin | |||||||||
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![]() human carboxypeptidase a4 in complex with human latexin.
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Identifiers | |||||||||
Symbol | Latexin | ||||||||
Pfam | PF06907 | ||||||||
InterPro | IPR009684 | ||||||||
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In molecular biology, the latexin family is a family of proteins which family consists of several animal specific latexin and proteins related to latexin that belong to MEROPS proteinase inhibitor family I47, clan IH.[1]
Latexin, a protein possessing inhibitory activity against rat carboxypeptidase A1 (CPA1) and CPA2 (MEROPS peptidase family M14A), is expressed in a neuronal subset in the cerebral cortex and cells in other neural and non-neural tissues of rat.[2][3] OCX-32, the 32 kDa eggshell matrix protein, is present at high levels in the uterine fluid during the terminal phase of eggshell formation, and is localised predominantly in the outer eggshell. The timing of OCX-32 secretion into the uterine fluid suggests that it may play a role in the termination of mineral deposition.[4] OCX-32 protein possesses limited identity (32%) to two unrelated proteins: latexin and to a skin protein that is encoded by a retinoic acid receptor-responsive gene, TIG1. Tazarotene Induced Gene 1 (TIG1) is a putative transmembrane protein with a small N-terminal intracellular region, a single membrane-spanning hydrophobic region, and a large C-terminal extracellular region containing a glycosylation signal. TIG1 is up-regulated by retinoic acid receptor but not by retinoid X receptor-specific synthetic retinoids.[5] TIG1 may be a tumour suppressor gene whose diminished expression is involved in the malignant progression of prostate cancer.[6]
External links
References
- ^ Rawlings ND, Tolle DP, Barrett AJ (March 2004). "Evolutionary families of peptidase inhibitors". Biochem. J. 378 (Pt 3): 705–16. doi:10.1042/BJ20031825. PMC 1224039
. PMID 14705960.
- ^ Uratani Y, Takiguchi-Hayashi K, Miyasaka N, Sato M, Jin M, Arimatsu Y (March 2000). "Latexin, a carboxypeptidase A inhibitor, is expressed in rat peritoneal mast cells and is associated with granular structures distinct from secretory granules and lysosomes". Biochem. J. 346 (3): 817–26. doi:10.1042/0264-6021:3460817. PMC 1220918
. PMID 10698712.
- ^ Liu Q, Yu L, Gao J, Fu Q, Zhang J, Zhang P, Chen J, Zhao S (2000). "Cloning, tissue expression pattern and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor". Mol. Biol. Rep. 27 (4): 241–6. doi:10.1023/A:1010971219806. PMID 11455960.
- ^ Hincke MT, Gautron J, Mann K, Panheleux M, McKee MD, Bain M, Solomon SE, Nys Y (2003). "Purification of ovocalyxin-32, a novel chicken eggshell matrix protein". Connect. Tissue Res. 44 Suppl 1: 16–9. doi:10.1080/03008200390152025. PMID 12952168.
- ^ Nagpal S, Patel S, Asano AT, Johnson AT, Duvic M, Chandraratna RA (February 1996). "Tazarotene-induced gene 1 (TIG1), a novel retinoic acid receptor-responsive gene in skin". J. Invest. Dermatol. 106 (2): 269–74. doi:10.1111/1523-1747.ep12340668. PMID 8601727.
- ^ Jing C, El-Ghany MA, Beesley C, Foster CS, Rudland PS, Smith P, Ke Y (April 2002). "Tazarotene-induced gene 1 (TIG1) expression in prostate carcinomas and its relationship to tumorigenicity". J. Natl. Cancer Inst. 94 (7): 482–90. doi:10.1093/jnci/94.7.482. PMID 11929948.
This article incorporates text from the public domain Pfam and InterPro IPR009684
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Latexin Provide feedback
This family consists of several animal specific latexin proteins. Latexin is a carboxypeptidase A inhibitor and is expressed in a cell type-specific manner in both central and peripheral nervous systems in the rat [1].
Literature references
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Liu Q, Yu L, Gao J, Fu Q, Zhang J, Zhang P, Chen J, Zhao S; , Mol Biol Rep 2000;27:241-246.: Cloning, tissue expression pattern and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor. PUBMED:11455960 EPMC:11455960
This tab holds annotation information from the InterPro database.
InterPro entry IPR009684
This family consists of several animal specific latexin and proteins related to latexin that belong to MEROPS proteinase inhibitor family I47, clan I- [PUBMED:14705960].
Latexin, a protein possessing inhibitory activity against rat carboxypeptidase A1 (CPA1) and CPA2 (MEROPS peptidase family M14A), is expressed in a neuronal subset in the cerebral cortex and cells in other neural and non-neural tissues of rat [PUBMED:10698712, PUBMED:11455960]. OCX-32, the 32 kDa eggshell matrix protein, is present at high levels in the uterine fluid during the terminal phase of eggshell formation, and is localised predominantly in the outer eggshell. The timing of OCX-32 secretion into the uterine fluid suggests that it may play a role in the termination of mineral deposition [PUBMED:12952168]. OCX-32 protein possesses limited identity (32%) to two unrelated proteins: latexin and to a skin protein that is encoded by a retinoic acid receptor-responsive gene, TIG1. Tazarotene Induced Gene 1 (TIG1) is a putative 228 transmembrane protein with a small N-terminal intracellular region, a single membrane-spanning hydrophobic region, and a large C-terminal extracellular region containing a glycosylation signal. TIG1 is up-regulated by retinoic acid receptor but not by retinoid X receptor-specific synthetic retinoids [PUBMED:8601727]. TIG1 may be a tumour suppressor gene whose diminished expression is involved in the malignant progression of prostate cancer [PUBMED:11929948].
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 Cystatin (CL0121), which has the following description:
This superfamily includes cystatins and cathelicidins [1]. The cystatin superfamily comprises cysteine protease inhibitors that play key regulatory roles in protein degradation processes. The progenitor of this superfamily was most probably intracellular and lacked a signal peptide and disulfide bridges, much like the extant Giardia cystatin. A primordial gene duplication produced two ancestral eukaryotic lineages, cystatins and stefins. Stefins - included in Pfam:PF00031 - remain encoded by a single or a small number of genes throughout the eukaryotes, whereas the cystatins have undergone a more complex and dynamic evolution through numerous gene and domain duplications [2].
The clan contains the following 12 members:
Cathelicidins Cystatin DUF3889 FTP Latexin Monellin PP1 Spp-24 SQAPI Staphopain_pro YebF YPEBAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (20) |
Full (200) |
Representative proteomes | UniProt (290) |
NCBI (693) |
Meta (0) |
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RP15 (22) |
RP35 (58) |
RP55 (154) |
RP75 (199) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (20) |
Full (200) |
Representative proteomes | UniProt (290) |
NCBI (693) |
Meta (0) |
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RP15 (22) |
RP35 (58) |
RP55 (154) |
RP75 (199) |
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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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Trees
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
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_14203 (release 10.0) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Moxon SJ |
Number in seed: | 20 |
Number in full: | 200 |
Average length of the domain: | 187.60 aa |
Average identity of full alignment: | 43 % |
Average coverage of the sequence by the domain: | 86.20 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 217 | ||||||||||||
Family (HMM) version: | 12 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Peptidase_M14Structures
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 Latexin domain has been found. There are 3 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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