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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

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi441 – 4411Zinc; catalytic By similarity
Active sitei442 – 4421Proton acceptor By similarity
Metal bindingi445 – 4451Zinc; catalytic By similarity
Metal bindingi464 – 4641Zinc; catalytic By similarity
Sitei528 – 5281Transition state stabilizer By similarity

GO - Molecular functioni

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

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 – 4040Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei41 – 6121Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini62 – 1025964Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. 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 ectoenzyme
PRO_0000095120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphothreonine; by PKC Reviewed prediction
Disulfide bondi68 – 68Interchain1 Publication
Glycosylationi90 – 901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi161 – 1611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi339 – 3391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi606 – 6061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi635 – 6351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi650 – 6501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi664 – 6641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi685 – 6851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi801 – 8011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi907 – 9071N-linked (GlcNAc...) Reviewed prediction

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

GenevestigatoriQ10836.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007461.

Structurei

3D structure databases

ProteinModelPortaliQ10836.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni405 – 4095Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

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

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MGEDDAALRA SGRGLSDPWA DSVGVRPRTT ERHIAVHKRL VLAFAVSIVA     50
LLAVTMLAVL LSLRFDECGA SAAMPGTDGG LGGFPERGGN SSYPGSARRN 100
HHAGEESSQR EIGEVGTAGT PSAHPPSEEE QEQWQPWTQL RLSGHLKPLH 150
YNLMLTAFME NFTFSGEVNV EIACQNATRY VVLHASRVAV EKVQVAEDRA 200
FGAVPVAGFF LYPQTQVLVV VLNRTLDAQR HYNLKIIYNA LIENELLGFF 250
RSSYVIHGER RFLGVTQFSP THARKAFPCF DEPIYKATFK ISIKHQATYL 300
SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAICNF TYRETTTKSG 350
VVVRLYARPD AIRRGSGDYA LHITKRLIEF YEDYFKVPYS LPKLDLLAVP 400
KHPYAAMENW GLSIFVEQRI LLDPSVSSIS YLLDVTMVIV HEICHQWFGD 450
LVTPVWWEDV WLKEGFAHYF EFVGTDYLYP SWNMEKQRFL TDVLHEVMLL 500
DGLASSHPVS QEVLRATDID KVFDWIAYKK GAALIRMLAN FMGHSVFQRG 550
LQDYLTIHKY GNAARNDLWN TLSEALKRNG KYVNIQEVMD QWTLQMGYPV 600
ITILGNMTAE NRILITQQHF IYDIGAKTKA LQLQNSSYLW QIPLTIVVGN 650
RSHVSSEAII WVSNKSEHHR ITYLDKGSWI LGNINQTGYF RVNYDLRNWR 700
LLIDQLIRNH EVLSVSNRAG LIDDAFSLAR AGYLPQNIPL EIIRYLSEEK 750
DFLPWHAASR ALYPLDKLLD RMENYNIFNE YILKQVATTY SKLGWPKNNF 800
NGSVVQASYQ HEELRREVIM LACSFGNKHC HQQASTLISD WISSNRNRIP 850
LNVRDIVYCT GVSLLDEDVW EFIWMKFHST TAVSEKKILL EALTCSDDRN 900
LLSRLLNLSL NSEVVLDQDA IDVIIHVARN PHGRDLAWKF FRDKWKILNT 950
RYGEALFMNS KLISGVTEFL NTEGELKELK NFMKSYDGVA SASFSRAVET 1000
VEANVRWKRL YQDELFQWLG KAMRH 1025
Length:1,025
Mass (Da):117,287
Last modified:November 1, 1996 - v1
Checksum:i4024EB262608D16B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80535 mRNA. Translation: CAA56675.1.
PIRiI59331.
UniGeneiRn.23393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80535 mRNA. Translation: CAA56675.1 .
PIRi I59331.
UniGenei Rn.23393.

3D structure databases

ProteinModelPortali Q10836.
ModBasei 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

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: September 3, 2014
This is version 120 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

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