Entry - *612846 - SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 7; SENP7 - OMIM

 
 
* 612846

SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 7; SENP7


Alternative titles; symbols

SUMO-SPECIFIC PROTEASE 7
KIAA1707


HGNC Approved Gene Symbol: SENP7

Cytogenetic location: 3q12.3     Genomic coordinates (GRCh38): 3:101,324,205-101,513,212 (from NCBI)


TEXT

▼ Description

The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; 601912) is required for many cellular processes. SUMO-specific proteases, such as SENP7, process SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also display isopeptidase activity for deconjugation of SUMO-conjugated substrates (Lima and Reverter, 2008).


▼ Cloning and Expression

By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2000) obtained a partial SENP7 clone, which they designated KIAA1707. RT-PCR ELISA detected SENP7 in all adult and fetal tissues examined and in all adult brain regions examined.

Lima and Reverter (2008) stated that the C-terminal catalytic domain of SENP7 lies between amino acids 662 and 984.


▼ Gene Function

Lima and Reverter (2008) showed that the isolated catalytic domains of SENP6 (605003) and SENP7 could not efficiently process SUMO1, SUMO2 (603042), and SUMO3 (602231) precursors. In contrast, SENP6 and SENP7 exhibited efficient SUMO deconjugation activity, with a preference for substrates containing SUMO2 or SUMO3 over substrates containing SUMO1. SENP6 and SENP7 showed higher rates for deconjugating di- or poly-SUMO2 and -SUMO3 than for deconjugating SUMO2- or SUMO3-conjugated RANGAP1 (602362). Lima and Reverter (2008) concluded that the high poly-SUMO2 and -SUMO3 chain deconjugation activities of SENP6 and SENP7 may reflect a preference for flexible isopeptide-linked substrates.


▼ Biochemical Features

Crystal Structure

Lima and Reverter (2008) solved the crystal structure of the SENP7 catalytic domain to 2.4-angstrom resolution. The primary sequence of SENP7 showed several substitutions and changes in charged residues compared with SENP2 (608261). SENP7 also has several unique secondary structural elements compared with SENP2, including a unique substrate-enzyme interface.


▼ Mapping

Hartz (2009) mapped the SENP7 gene to chromosome 3q12.3 based on an alignment of the SENP7 sequence (GenBank AF217504) with the genomic sequence (build 36.1).

▼ REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 6/11/2009.

  2. Lima, C. D., Reverter, D. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J. Biol. Chem. 283: 32045-32055, 2008. [PubMed: 18799455, images, related citations] [Full Text]

  3. Nagase, T., Kikuno, R., Hattori, A., Kondo, Y., Okumura, K., Ohara, O. Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7: 347-355, 2000. [PubMed: 11214970, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 6/11/2009
Edit History:
mgross : 06/11/2009

* 612846

SENTRIN-SPECIFIC PROTEASE FAMILY, MEMBER 7; SENP7


Alternative titles; symbols

SUMO-SPECIFIC PROTEASE 7
KIAA1707


HGNC Approved Gene Symbol: SENP7

Cytogenetic location: 3q12.3     Genomic coordinates (GRCh38): 3:101,324,205-101,513,212 (from NCBI)


TEXT

Description

The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; 601912) is required for many cellular processes. SUMO-specific proteases, such as SENP7, process SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also display isopeptidase activity for deconjugation of SUMO-conjugated substrates (Lima and Reverter, 2008).


Cloning and Expression

By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2000) obtained a partial SENP7 clone, which they designated KIAA1707. RT-PCR ELISA detected SENP7 in all adult and fetal tissues examined and in all adult brain regions examined.

Lima and Reverter (2008) stated that the C-terminal catalytic domain of SENP7 lies between amino acids 662 and 984.


Gene Function

Lima and Reverter (2008) showed that the isolated catalytic domains of SENP6 (605003) and SENP7 could not efficiently process SUMO1, SUMO2 (603042), and SUMO3 (602231) precursors. In contrast, SENP6 and SENP7 exhibited efficient SUMO deconjugation activity, with a preference for substrates containing SUMO2 or SUMO3 over substrates containing SUMO1. SENP6 and SENP7 showed higher rates for deconjugating di- or poly-SUMO2 and -SUMO3 than for deconjugating SUMO2- or SUMO3-conjugated RANGAP1 (602362). Lima and Reverter (2008) concluded that the high poly-SUMO2 and -SUMO3 chain deconjugation activities of SENP6 and SENP7 may reflect a preference for flexible isopeptide-linked substrates.


Biochemical Features

Crystal Structure

Lima and Reverter (2008) solved the crystal structure of the SENP7 catalytic domain to 2.4-angstrom resolution. The primary sequence of SENP7 showed several substitutions and changes in charged residues compared with SENP2 (608261). SENP7 also has several unique secondary structural elements compared with SENP2, including a unique substrate-enzyme interface.


Mapping

Hartz (2009) mapped the SENP7 gene to chromosome 3q12.3 based on an alignment of the SENP7 sequence (GenBank AF217504) with the genomic sequence (build 36.1).

REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 6/11/2009.

  2. Lima, C. D., Reverter, D. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J. Biol. Chem. 283: 32045-32055, 2008. [PubMed: 18799455] [Full Text: https://doi.org/10.1074/jbc.M805655200]

  3. Nagase, T., Kikuno, R., Hattori, A., Kondo, Y., Okumura, K., Ohara, O. Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7: 347-355, 2000. [PubMed: 11214970] [Full Text: https://doi.org/10.1093/dnares/7.6.347]


Creation Date:
Patricia A. Hartz : 6/11/2009

Edit History:
mgross : 06/11/2009



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: April 16, 2024