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Q8C1A5

- THOP1_MOUSE

UniProt

Q8C1A5 - THOP1_MOUSE

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Protein
Thimet oligopeptidase
Gene
Thop1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi473 – 4731Zinc; catalytic By similarity
Active sitei474 – 4741 By similarity
Metal bindingi477 – 4771Zinc; catalytic By similarity
Metal bindingi480 – 4801Zinc; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: MGI
  3. peptide binding Source: Ensembl

GO - Biological processi

  1. intracellular signal transduction Source: MGI
  2. peptide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thimet oligopeptidase (EC:3.4.24.15)
Gene namesi
Name:Thop1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1354165. Thop1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Thimet oligopeptidase
PRO_0000319044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-acetyllysine By similarity
Modified residuei278 – 2781Phosphotyrosine1 Publication
Modified residuei538 – 5381N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8C1A5.
PaxDbiQ8C1A5.
PRIDEiQ8C1A5.

2D gel databases

REPRODUCTION-2DPAGEQ8C1A5.

PTM databases

PhosphoSiteiQ8C1A5.

Expressioni

Gene expression databases

BgeeiQ8C1A5.
CleanExiMM_THOP1.
GenevestigatoriQ8C1A5.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi206040. 2 interactions.
IntActiQ8C1A5. 1 interaction.
MINTiMINT-4128941.

Structurei

3D structure databases

ProteinModelPortaliQ8C1A5.
SMRiQ8C1A5. Positions 24-677.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ8C1A5.
KOiK01392.
OrthoDBiEOG7SR4KW.
PhylomeDBiQ8C1A5.
TreeFamiTF300459.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C1A5-1 [UniParc]FASTAAdd to Basket

« Hide

MKPPAACAGD VVDAASPAST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR    50
VGAQNFEDVS YESTLKALAD VEVTYTVQRN ILDFPQHVSP CKDIRAASTE 100
ADKKLSEFDV EMSMRQDVYQ RVVWLQEKTP KNSLKPEAAR YLERLIKLGR 150
RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK NLNEDTTFLP FTREELGGLP 200
EDFLSSLEKA EDGKLKVTLK YPHYFPLLKK CHVPETRRLL EEAFNCRCKE 250
ENCAILKELV SLRAQKSSLL GFHTHADYVL EMNMAKTSQT VATFLDELAQ 300
KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR 350
VDQNLLKEYF PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR 400
DAASGEEIGK FYLDLYPREG KYGHAACFGL QPGCLRQDGS RQLAVAAMVA 450
NFTKPTPDAP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF 500
VEAPSQMLEN WVWEKEPLMR MSQHYRTGSE APQDLLEKLI KSRQANAGLF 550
NLRQIVLAKV DQVLHTQTDA DPAEEYARLC QEILGVPATP GTNMPATFGH 600
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG 650
SEDASAMLKQ FLGRDPKQDA FLLSKGLQVE GSEAPAC 687
Length:687
Mass (Da):78,026
Last modified:March 1, 2003 - v1
Checksum:i362D899CE5101662
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321N → D in AAG35061. 1 Publication
Sequence conflicti132 – 1321N → D in AAH31722. 1 Publication
Sequence conflicti193 – 1942RE → KK in AAG35061. 1 Publication
Sequence conflicti205 – 2051S → I in AAG35061. 1 Publication
Sequence conflicti529 – 5291S → G in AAG35061. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF314187 mRNA. Translation: AAG35061.1.
AK028609 mRNA. Translation: BAC26031.1.
BC031175 mRNA. Translation: AAH31175.1.
BC031722 mRNA. Translation: AAH31722.1.
CCDSiCCDS24042.1.
RefSeqiNP_073144.3. NM_022653.4.
UniGeneiMm.26995.

Genome annotation databases

EnsembliENSMUST00000005057; ENSMUSP00000005057; ENSMUSG00000004929.
GeneIDi50492.
KEGGimmu:50492.
UCSCiuc007gfv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF314187 mRNA. Translation: AAG35061.1 .
AK028609 mRNA. Translation: BAC26031.1 .
BC031175 mRNA. Translation: AAH31175.1 .
BC031722 mRNA. Translation: AAH31722.1 .
CCDSi CCDS24042.1.
RefSeqi NP_073144.3. NM_022653.4.
UniGenei Mm.26995.

3D structure databases

ProteinModelPortali Q8C1A5.
SMRi Q8C1A5. Positions 24-677.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206040. 2 interactions.
IntActi Q8C1A5. 1 interaction.
MINTi MINT-4128941.

Protein family/group databases

MEROPSi M03.001.

PTM databases

PhosphoSitei Q8C1A5.

2D gel databases

REPRODUCTION-2DPAGE Q8C1A5.

Proteomic databases

MaxQBi Q8C1A5.
PaxDbi Q8C1A5.
PRIDEi Q8C1A5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005057 ; ENSMUSP00000005057 ; ENSMUSG00000004929 .
GeneIDi 50492.
KEGGi mmu:50492.
UCSCi uc007gfv.2. mouse.

Organism-specific databases

CTDi 7064.
MGIi MGI:1354165. Thop1.

Phylogenomic databases

eggNOGi COG0339.
GeneTreei ENSGT00550000074738.
HOGENOMi HOG000245985.
HOVERGENi HBG000238.
InParanoidi Q8C1A5.
KOi K01392.
OrthoDBi EOG7SR4KW.
PhylomeDBi Q8C1A5.
TreeFami TF300459.

Miscellaneous databases

NextBioi 307472.
PROi Q8C1A5.
SOURCEi Search...

Gene expression databases

Bgeei Q8C1A5.
CleanExi MM_THOP1.
Genevestigatori Q8C1A5.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTHOP1_MOUSE
AccessioniPrimary (citable) accession number: Q8C1A5
Secondary accession number(s): Q8K0J9, Q8K2D4, Q9EPX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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