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Protein

Thyrotropin-releasing hormone-degrading ectoenzyme

Gene

Trhde

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specific inactivation of TRH after its release.

Catalytic activityi

Release of the N-terminal pyroglutamyl group from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly tetrapeptides.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi441Zinc; catalyticPROSITE-ProRule annotation1
Active sitei442Proton acceptorPROSITE-ProRule annotation1
Metal bindingi445Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi464Zinc; catalyticPROSITE-ProRule annotation1
Sitei528Transition state stabilizerBy similarity1

GO - Molecular functioni

  • aminopeptidase activity Source: RGD
  • metalloaminopeptidase activity Source: GO_Central
  • peptide binding Source: GO_Central
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • cell-cell signaling Source: GO_Central
  • peptide catabolic process Source: GO_Central
  • proteolysis Source: RGD
  • regulation of blood pressure Source: GO_Central
  • signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyrotropin-releasing hormone-degrading ectoenzyme (EC:3.4.19.6)
Short name:
TRH-DE
Short name:
TRH-degrading ectoenzyme
Alternative name(s):
Pyroglutamyl-peptidase II
Short name:
PAP-II
TRH-specific aminopeptidase
Thyroliberinase
Gene namesi
Name:Trhde
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi728895. Trhde.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 40CytoplasmicSequence analysisAdd BLAST40
Transmembranei41 – 61Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini62 – 1025ExtracellularSequence analysisAdd BLAST964

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951201 – 1025Thyrotropin-releasing hormone-degrading ectoenzymeAdd BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30Phosphothreonine; by PKCSequence analysis1
Disulfide bondi68Interchain
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi176N-linked (GlcNAc...)Sequence analysis1
Glycosylationi223N-linked (GlcNAc...)Sequence analysis1
Glycosylationi339N-linked (GlcNAc...)Sequence analysis1
Glycosylationi606N-linked (GlcNAc...)Sequence analysis1
Glycosylationi635N-linked (GlcNAc...)Sequence analysis1
Glycosylationi650N-linked (GlcNAc...)Sequence analysis1
Glycosylationi664N-linked (GlcNAc...)Sequence analysis1
Glycosylationi685N-linked (GlcNAc...)Sequence analysis1
Glycosylationi801N-linked (GlcNAc...)Sequence analysis1
Glycosylationi907N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ10836.
PRIDEiQ10836.

PTM databases

iPTMnetiQ10836.
PhosphoSitePlusiQ10836.

Expressioni

Tissue specificityi

Predominantly expressed in brain and pituitary. Lower levels in lung and liver.

Gene expression databases

BgeeiENSRNOG00000005278.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007461.

Structurei

3D structure databases

ProteinModelPortaliQ10836.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni405 – 409Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG095698.
InParanoidiQ10836.
PhylomeDBiQ10836.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR015570. TRH-DE.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PTHR11533:SF40. PTHR11533:SF40. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDDAALRA SGRGLSDPWA DSVGVRPRTT ERHIAVHKRL VLAFAVSIVA
60 70 80 90 100
LLAVTMLAVL LSLRFDECGA SAAMPGTDGG LGGFPERGGN SSYPGSARRN
110 120 130 140 150
HHAGEESSQR EIGEVGTAGT PSAHPPSEEE QEQWQPWTQL RLSGHLKPLH
160 170 180 190 200
YNLMLTAFME NFTFSGEVNV EIACQNATRY VVLHASRVAV EKVQVAEDRA
210 220 230 240 250
FGAVPVAGFF LYPQTQVLVV VLNRTLDAQR HYNLKIIYNA LIENELLGFF
260 270 280 290 300
RSSYVIHGER RFLGVTQFSP THARKAFPCF DEPIYKATFK ISIKHQATYL
310 320 330 340 350
SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAICNF TYRETTTKSG
360 370 380 390 400
VVVRLYARPD AIRRGSGDYA LHITKRLIEF YEDYFKVPYS LPKLDLLAVP
410 420 430 440 450
KHPYAAMENW GLSIFVEQRI LLDPSVSSIS YLLDVTMVIV HEICHQWFGD
460 470 480 490 500
LVTPVWWEDV WLKEGFAHYF EFVGTDYLYP SWNMEKQRFL TDVLHEVMLL
510 520 530 540 550
DGLASSHPVS QEVLRATDID KVFDWIAYKK GAALIRMLAN FMGHSVFQRG
560 570 580 590 600
LQDYLTIHKY GNAARNDLWN TLSEALKRNG KYVNIQEVMD QWTLQMGYPV
610 620 630 640 650
ITILGNMTAE NRILITQQHF IYDIGAKTKA LQLQNSSYLW QIPLTIVVGN
660 670 680 690 700
RSHVSSEAII WVSNKSEHHR ITYLDKGSWI LGNINQTGYF RVNYDLRNWR
710 720 730 740 750
LLIDQLIRNH EVLSVSNRAG LIDDAFSLAR AGYLPQNIPL EIIRYLSEEK
760 770 780 790 800
DFLPWHAASR ALYPLDKLLD RMENYNIFNE YILKQVATTY SKLGWPKNNF
810 820 830 840 850
NGSVVQASYQ HEELRREVIM LACSFGNKHC HQQASTLISD WISSNRNRIP
860 870 880 890 900
LNVRDIVYCT GVSLLDEDVW EFIWMKFHST TAVSEKKILL EALTCSDDRN
910 920 930 940 950
LLSRLLNLSL NSEVVLDQDA IDVIIHVARN PHGRDLAWKF FRDKWKILNT
960 970 980 990 1000
RYGEALFMNS KLISGVTEFL NTEGELKELK NFMKSYDGVA SASFSRAVET
1010 1020
VEANVRWKRL YQDELFQWLG KAMRH
Length:1,025
Mass (Da):117,287
Last modified:November 1, 1996 - v1
Checksum:i4024EB262608D16B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80535 mRNA. Translation: CAA56675.1.
PIRiI59331.
UniGeneiRn.23393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80535 mRNA. Translation: CAA56675.1.
PIRiI59331.
UniGeneiRn.23393.

3D structure databases

ProteinModelPortaliQ10836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007461.

Protein family/group databases

MEROPSiM01.008.

PTM databases

iPTMnetiQ10836.
PhosphoSitePlusiQ10836.

Proteomic databases

PaxDbiQ10836.
PRIDEiQ10836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi728895. Trhde.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG095698.
InParanoidiQ10836.
PhylomeDBiQ10836.

Miscellaneous databases

PROiQ10836.

Gene expression databases

BgeeiENSRNOG00000005278.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR015570. TRH-DE.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PTHR11533:SF40. PTHR11533:SF40. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRHDE_RAT
AccessioniPrimary (citable) accession number: Q10836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 134 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.