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Q5RFL1

- TPP1_PONAB

UniProt

Q5RFL1 - TPP1_PONAB

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Protein

Tripeptidyl-peptidase 1

Gene
TPP1, CLN2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus By similarity.

Catalytic activityi

Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei272 – 2721Charge relay system By similarity
Active sitei276 – 2761Charge relay system By similarity
Active sitei475 – 4751Charge relay system By similarity
Metal bindingi518 – 5181Calcium By similarity
Metal bindingi519 – 5191Calcium; via carbonyl oxygen By similarity
Metal bindingi540 – 5401Calcium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Calcium; via carbonyl oxygen By similarity
Metal bindingi544 – 5441Calcium By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. peptidase activity Source: UniProtKB
  3. serine-type endopeptidase activity Source: InterPro
  4. serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. bone resorption Source: UniProtKB
  2. nervous system development Source: UniProtKB
  3. peptide catabolic process Source: UniProtKB
  4. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tripeptidyl-peptidase 1 (EC:3.4.14.9)
Short name:
TPP-1
Alternative name(s):
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
Short name:
TPP-I
Gene namesi
Name:TPP1
Synonyms:CLN2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Lysosome By similarity. Melanosome By similarity

GO - Cellular componenti

  1. lysosome Source: UniProtKB
  2. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarityAdd
BLAST
Propeptidei20 – 195176Removed in mature form By similarityPRO_0000027382Add
BLAST
Chaini196 – 564369Tripeptidyl-peptidase 1PRO_0000027383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 122 By similarity
Glycosylationi210 – 2101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi222 – 2221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi286 – 2861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi313 – 3131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi365 ↔ 527 By similarity
Glycosylationi443 – 4431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi523 ↔ 538 By similarity

Post-translational modificationi

Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity By similarity.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RFL1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 564366Peptidase S53Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004449.
InParanoidiQ5RFL1.
KOiK01279.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamiPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS51695. SEDOLISIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RFL1-1 [UniParc]FASTAAdd to Basket

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MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT    50
FALRQQNVER LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ 100
KWLLAAGAQK CHSVITQDFL TCWLSIRQAE LLLPGAEFHH YVGGPTETHV 150
VRSPHPYQLP QALAPHVDFV GGLHRFPPTS SLRQHPEPQV TGTVGLHLGV 200
TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN 250
FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 300
QEPFLQWLML LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR 350
GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFLEPFLTT 400
NEIVDYISGG GFSNVFPRPS YQEEAVTKFL SSSPHLPPSS YFNASGRAYP 450
DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGGILSLIN EHRILSGRPP 500
LGFLNPRLYQ QHGAGLFDVT HGCHESCLDE EVEGQGFCSG PGWDPVTGWG 550
TPNFPALPKT LLNP 564
Length:564
Mass (Da):61,238
Last modified:December 21, 2004 - v1
Checksum:i381FDB588837B0F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857144 mRNA. Translation: CAH89446.1.
RefSeqiNP_001124619.1. NM_001131147.1.
UniGeneiPab.9208.

Genome annotation databases

GeneIDi100440001.
KEGGipon:100440001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857144 mRNA. Translation: CAH89446.1 .
RefSeqi NP_001124619.1. NM_001131147.1.
UniGenei Pab.9208.

3D structure databases

ProteinModelPortali Q5RFL1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100440001.
KEGGi pon:100440001.

Organism-specific databases

CTDi 1200.

Phylogenomic databases

HOVERGENi HBG004449.
InParanoidi Q5RFL1.
KOi K01279.

Family and domain databases

Gene3Di 3.40.50.200. 1 hit.
InterProi IPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view ]
Pfami PF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view ]
SMARTi SM00944. Pro-kuma_activ. 1 hit.
[Graphical view ]
SUPFAMi SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEi PS51695. SEDOLISIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiTPP1_PONAB
AccessioniPrimary (citable) accession number: Q5RFL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 57 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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