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Q5RFL1

- TPP1_PONAB

UniProt

Q5RFL1 - TPP1_PONAB

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Protein

Tripeptidyl-peptidase 1

Gene

TPP1

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).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 systemBy similarity
Active sitei276 – 2761Charge relay systemBy similarity
Active sitei475 – 4751Charge relay systemBy similarity
Metal bindingi518 – 5181CalciumBy similarity
Metal bindingi519 – 5191Calcium; via carbonyl oxygenBy similarity
Metal bindingi540 – 5401Calcium; via carbonyl oxygenBy similarity
Metal bindingi542 – 5421Calcium; via carbonyl oxygenBy similarity
Metal bindingi544 – 5441CalciumBy 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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RFL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 peptidase S53 domain.Curated

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

« Hide

        10         20         30         40         50
MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT
60 70 80 90 100
FALRQQNVER LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ
110 120 130 140 150
KWLLAAGAQK CHSVITQDFL TCWLSIRQAE LLLPGAEFHH YVGGPTETHV
160 170 180 190 200
VRSPHPYQLP QALAPHVDFV GGLHRFPPTS SLRQHPEPQV TGTVGLHLGV
210 220 230 240 250
TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN
260 270 280 290 300
FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG
310 320 330 340 350
QEPFLQWLML LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR
360 370 380 390 400
GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFLEPFLTT
410 420 430 440 450
NEIVDYISGG GFSNVFPRPS YQEEAVTKFL SSSPHLPPSS YFNASGRAYP
460 470 480 490 500
DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGGILSLIN EHRILSGRPP
510 520 530 540 550
LGFLNPRLYQ QHGAGLFDVT HGCHESCLDE EVEGQGFCSG PGWDPVTGWG
560
TPNFPALPKT LLNP
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: October 29, 2014
This is version 59 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