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Q10836

- TRHDE_RAT

UniProt

Q10836 - TRHDE_RAT

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Protein

Thyrotropin-releasing hormone-degrading ectoenzyme

Gene

Trhde

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi441 – 4411Zinc; catalyticPROSITE-ProRule annotation
Active sitei442 – 4421Proton acceptorPROSITE-ProRule annotation
Metal bindingi445 – 4451Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi464 – 4641Zinc; catalyticPROSITE-ProRule annotation
Sitei528 – 5281Transition state stabilizerBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: RGD
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. proteolysis Source: RGD
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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi728895. Trhde.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei41 – 6121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini62 – 1025964ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Thyrotropin-releasing hormone-degrading ectoenzymePRO_0000095120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphothreonine; by PKCSequence Analysis
Disulfide bondi68 – 68Interchain
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi650 – 6501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ10836.
PRIDEiQ10836.

PTM databases

PhosphoSiteiQ10836.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiQ10836. baseline and differential.
GenevestigatoriQ10836.

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)LengthDescriptionGraphical viewFeature identifierActions
Regioni405 – 4095Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
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. 1 hit.
PTHR11533:SF40. PTHR11533:SF40. 1 hit.
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 .
PIRi I59331.
UniGenei Rn.23393.

3D structure databases

ProteinModelPortali Q10836.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000007461.

Protein family/group databases

MEROPSi M01.008.

PTM databases

PhosphoSitei Q10836.

Proteomic databases

PaxDbi Q10836.
PRIDEi Q10836.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 728895. Trhde.

Phylogenomic databases

eggNOGi COG0308.
HOGENOMi HOG000106482.
HOVERGENi HBG095698.
InParanoidi Q10836.
PhylomeDBi Q10836.

Miscellaneous databases

PROi Q10836.

Gene expression databases

ExpressionAtlasi Q10836. baseline and differential.
Genevestigatori Q10836.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR015570. TRH-DE.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
PTHR11533:SF40. PTHR11533:SF40. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of a cDNA encoding an ectoenzyme that degrades thyrotropin-releasing hormone."
    Schauder B., Schomburg L., Koehrle J., Bauer K.
    Proc. Natl. Acad. Sci. U.S.A. 91:9534-9538(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Pituitary.
  2. "Analysis of the thyrotropin-releasing hormone-degrading ectoenzyme by site-directed mutagenesis of cysteine residues. Cys68 is involved in disulfide-linked dimerization."
    Papadopoulos T., Heuer H., Bauer K.
    Eur. J. Biochem. 267:2617-2623(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BOND.

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 26, 2014
This is version 123 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

External Data

Dasty 3