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Q8C1A5 (THOP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thimet oligopeptidase

EC=3.4.24.15
Gene names
Name:Thop1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length687 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments By similarity.

Catalytic activity

Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 687687Thimet oligopeptidase
PRO_0000319044

Sites

Active site4741 By similarity
Metal binding4731Zinc; catalytic By similarity
Metal binding4771Zinc; catalytic By similarity
Metal binding4801Zinc; catalytic By similarity

Amino acid modifications

Modified residue2571N6-acetyllysine By similarity
Modified residue2781Phosphotyrosine Ref.4
Modified residue5381N6-acetyllysine By similarity

Experimental info

Sequence conflict1321N → D in AAG35061. Ref.1
Sequence conflict1321N → D in AAH31722. Ref.3
Sequence conflict193 – 1942RE → KK in AAG35061. Ref.1
Sequence conflict2051S → I in AAG35061. Ref.1
Sequence conflict5291S → G in AAG35061. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C1A5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 362D899CE5101662

FASTA68778,026
        10         20         30         40         50         60 
MKPPAACAGD VVDAASPAST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR VGAQNFEDVS 

        70         80         90        100        110        120 
YESTLKALAD VEVTYTVQRN ILDFPQHVSP CKDIRAASTE ADKKLSEFDV EMSMRQDVYQ 

       130        140        150        160        170        180 
RVVWLQEKTP KNSLKPEAAR YLERLIKLGR RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK 

       190        200        210        220        230        240 
NLNEDTTFLP FTREELGGLP EDFLSSLEKA EDGKLKVTLK YPHYFPLLKK CHVPETRRLL 

       250        260        270        280        290        300 
EEAFNCRCKE ENCAILKELV SLRAQKSSLL GFHTHADYVL EMNMAKTSQT VATFLDELAQ 

       310        320        330        340        350        360 
KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR VDQNLLKEYF 

       370        380        390        400        410        420 
PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR DAASGEEIGK FYLDLYPREG 

       430        440        450        460        470        480 
KYGHAACFGL QPGCLRQDGS RQLAVAAMVA NFTKPTPDAP SLLQHDEVET YFHEFGHVMH 

       490        500        510        520        530        540 
QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEKEPLMR MSQHYRTGSE APQDLLEKLI 

       550        560        570        580        590        600 
KSRQANAGLF NLRQIVLAKV DQVLHTQTDA DPAEEYARLC QEILGVPATP GTNMPATFGH 

       610        620        630        640        650        660 
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG SEDASAMLKQ 

       670        680 
FLGRDPKQDA FLLSKGLQVE GSEAPAC 

« Hide

References

« Hide 'large scale' references
[1]"The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation."
Tullai J.W., Cummins P.M., Pabon A., Roberts J.L., Lopingco M.C., Shrimpton C.N., Smith A.I., Martignetti J.A., Ferro E.S., Glucksman M.J.
J. Biol. Chem. 275:36514-36522(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Colon and Mammary tumor.
[4]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF314187 mRNA. Translation: AAG35061.1.
AK028609 mRNA. Translation: BAC26031.1.
BC031175 mRNA. Translation: AAH31175.1.
BC031722 mRNA. Translation: AAH31722.1.
RefSeqNP_073144.3. NM_022653.4.
UniGeneMm.26995.

3D structure databases

ProteinModelPortalQ8C1A5.
SMRQ8C1A5. Positions 24-677.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206040. 1 interaction.
IntActQ8C1A5. 1 interaction.
MINTMINT-4128941.

Protein family/group databases

MEROPSM03.001.

PTM databases

PhosphoSiteQ8C1A5.

2D gel databases

REPRODUCTION-2DPAGEQ8C1A5.

Proteomic databases

PaxDbQ8C1A5.
PRIDEQ8C1A5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005057; ENSMUSP00000005057; ENSMUSG00000004929.
GeneID50492.
KEGGmmu:50492.
UCSCuc007gfv.2. mouse.

Organism-specific databases

CTD7064.
MGIMGI:1354165. Thop1.

Phylogenomic databases

eggNOGCOG0339.
GeneTreeENSGT00550000074738.
HOGENOMHOG000245985.
HOVERGENHBG000238.
InParanoidQ8C1A5.
KOK01392.
OrthoDBEOG7SR4KW.
PhylomeDBQ8C1A5.
TreeFamTF300459.

Gene expression databases

BgeeQ8C1A5.
CleanExMM_THOP1.
GenevestigatorQ8C1A5.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307472.
PROQ8C1A5.
SOURCESearch...

Entry information

Entry nameTHOP1_MOUSE
AccessionPrimary (citable) accession number: Q8C1A5
Secondary accession number(s): Q8K0J9, Q8K2D4, Q9EPX1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot