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Q10836 (TRHDE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyrotropin-releasing hormone-degrading ectoenzyme

Short name=TRH-DE
Short name=TRH-degrading ectoenzyme
EC=3.4.19.6
Alternative name(s):
Pyroglutamyl-peptidase II
Short name=PAP-II
TRH-specific aminopeptidase
Thyroliberinase
Gene names
Name:Trhde
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specific inactivation of TRH after its release.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer; disulfide-linked. Ref.2

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

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

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Thyrotropin-releasing hormone-degrading ectoenzyme
PRO_0000095120

Regions

Topological domain1 – 4040Cytoplasmic Potential
Transmembrane41 – 6121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain62 – 1025964Extracellular Potential
Region405 – 4095Substrate binding By similarity

Sites

Active site4421Proton acceptor By similarity
Metal binding4411Zinc; catalytic By similarity
Metal binding4451Zinc; catalytic By similarity
Metal binding4641Zinc; catalytic By similarity
Site5281Transition state stabilizer By similarity

Amino acid modifications

Modified residue301Phosphothreonine; by PKC Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Glycosylation6351N-linked (GlcNAc...) Potential
Glycosylation6501N-linked (GlcNAc...) Potential
Glycosylation6641N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation8011N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential
Disulfide bond68Interchain Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q10836 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4024EB262608D16B

FASTA1,025117,287
        10         20         30         40         50         60 
MGEDDAALRA SGRGLSDPWA DSVGVRPRTT ERHIAVHKRL VLAFAVSIVA LLAVTMLAVL 

        70         80         90        100        110        120 
LSLRFDECGA SAAMPGTDGG LGGFPERGGN SSYPGSARRN HHAGEESSQR EIGEVGTAGT 

       130        140        150        160        170        180 
PSAHPPSEEE QEQWQPWTQL RLSGHLKPLH YNLMLTAFME NFTFSGEVNV EIACQNATRY 

       190        200        210        220        230        240 
VVLHASRVAV EKVQVAEDRA FGAVPVAGFF LYPQTQVLVV VLNRTLDAQR HYNLKIIYNA 

       250        260        270        280        290        300 
LIENELLGFF RSSYVIHGER RFLGVTQFSP THARKAFPCF DEPIYKATFK ISIKHQATYL 

       310        320        330        340        350        360 
SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAICNF TYRETTTKSG VVVRLYARPD 

       370        380        390        400        410        420 
AIRRGSGDYA LHITKRLIEF YEDYFKVPYS LPKLDLLAVP KHPYAAMENW GLSIFVEQRI 

       430        440        450        460        470        480 
LLDPSVSSIS YLLDVTMVIV HEICHQWFGD LVTPVWWEDV WLKEGFAHYF EFVGTDYLYP 

       490        500        510        520        530        540 
SWNMEKQRFL TDVLHEVMLL DGLASSHPVS QEVLRATDID KVFDWIAYKK GAALIRMLAN 

       550        560        570        580        590        600 
FMGHSVFQRG LQDYLTIHKY GNAARNDLWN TLSEALKRNG KYVNIQEVMD QWTLQMGYPV 

       610        620        630        640        650        660 
ITILGNMTAE NRILITQQHF IYDIGAKTKA LQLQNSSYLW QIPLTIVVGN RSHVSSEAII 

       670        680        690        700        710        720 
WVSNKSEHHR ITYLDKGSWI LGNINQTGYF RVNYDLRNWR LLIDQLIRNH EVLSVSNRAG 

       730        740        750        760        770        780 
LIDDAFSLAR AGYLPQNIPL EIIRYLSEEK DFLPWHAASR ALYPLDKLLD RMENYNIFNE 

       790        800        810        820        830        840 
YILKQVATTY SKLGWPKNNF NGSVVQASYQ HEELRREVIM LACSFGNKHC HQQASTLISD 

       850        860        870        880        890        900 
WISSNRNRIP LNVRDIVYCT GVSLLDEDVW EFIWMKFHST TAVSEKKILL EALTCSDDRN 

       910        920        930        940        950        960 
LLSRLLNLSL NSEVVLDQDA IDVIIHVARN PHGRDLAWKF FRDKWKILNT RYGEALFMNS 

       970        980        990       1000       1010       1020 
KLISGVTEFL NTEGELKELK NFMKSYDGVA SASFSRAVET VEANVRWKRL YQDELFQWLG 


KAMRH 

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References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80535 mRNA. Translation: CAA56675.1.
PIRI59331.
UniGeneRn.23393.

3D structure databases

ProteinModelPortalQ10836.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007461.

Protein family/group databases

MEROPSM01.008.

PTM databases

PhosphoSiteQ10836.

Proteomic databases

PaxDbQ10836.
PRIDEQ10836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD728895. Trhde.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
HOVERGENHBG095698.
InParanoidQ10836.
PhylomeDBQ10836.

Gene expression databases

GenevestigatorQ10836.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR015570. Peptidase_M1_TRH-DE.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF40. PTHR11533:SF40. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ10836.

Entry information

Entry nameTRHDE_RAT
AccessionPrimary (citable) accession number: Q10836
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries