Thyrotropin-releasing hormone-degrading ectoenzyme - Rattus norvegicus (Rat)

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Q10836 (TRHDE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Traceable author statement PubMed 11856362. Source: RGD
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aminopeptidase activity Traceable author statement PubMed 11856362. Source: RGD metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1025

Thyrotropin-releasing hormone-degrading ectoenzyme

PRO_0000095120

Regions

Topological domain

40

Cytoplasmic Potential

Transmembrane

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

964

Extracellular Potential

Region

5

Substrate binding By similarity

Sites

Active site

1

Proton acceptor By similarity

Metal binding

1

Zinc; catalytic By similarity

Metal binding

1

Zinc; catalytic By similarity

Metal binding

1

Zinc; catalytic By similarity

Site

1

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

1

Phosphothreonine; by PKC Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

Interchain Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q10836 [UniParc].

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

1,025

117,287

        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

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.
IPI	IPI00212649.
PIR	I59331.
UniGene	Rn.23393.
3D structure databases
ProteinModelPortal	Q10836.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000007461.
Protein family/group databases
MEROPS	M01.008.
PTM databases
PhosphoSite	Q10836.
Proteomic databases
PaxDb	Q10836.
PRIDE	Q10836.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	728895. Trhde.
Phylogenomic databases
eggNOG	COG0308.
HOGENOM	HOG000106482.
HOVERGEN	HBG095698.
InParanoid	Q10836.
OMA	FTYRETT.
OrthoDB	EOG4NZTSG.
Gene expression databases
Genevestigator	Q10836.
GermOnline	ENSRNOG00000005278. Rattus norvegicus.
Family and domain databases
InterPro	IPR024571. DUF3358. IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. IPR015570. Peptidase_M1_TRH-DE. [Graphical view]
PANTHER	PTHR11533. PTHR11533. 1 hit. PTHR11533:SF40. PTHR11533:SF40. 1 hit.
Pfam	PF11838. DUF3358. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRHDE_RAT

Accession

Primary (citable) accession number: Q10836

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents