GenomeNet

Database: UniProt
Entry: Q8K093
LinkDB: Q8K093
Original site: Q8K093 
ID   TRHDE_MOUSE             Reviewed;        1025 AA.
AC   Q8K093;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   26-NOV-2014, entry version 102.
DE   RecName: Full=Thyrotropin-releasing hormone-degrading ectoenzyme;
DE            Short=TRH-DE;
DE            Short=TRH-degrading ectoenzyme;
DE            EC=3.4.19.6;
DE   AltName: Full=Pyroglutamyl-peptidase II;
DE            Short=PAP-II;
DE   AltName: Full=TRH-specific aminopeptidase;
DE   AltName: Full=Thyroliberinase;
GN   Name=Trhde;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Specific inactivation of TRH after its release.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Release of the N-terminal pyroglutamyl group
CC       from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly
CC       tetrapeptides.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; BC032288; AAH32288.1; -; mRNA.
DR   CCDS; CCDS24175.1; -.
DR   RefSeq; NP_666353.1; NM_146241.2.
DR   UniGene; Mm.445550; -.
DR   ProteinModelPortal; Q8K093; -.
DR   SMR; Q8K093; 136-1019.
DR   MEROPS; M01.008; -.
DR   PhosphoSite; Q8K093; -.
DR   PaxDb; Q8K093; -.
DR   PRIDE; Q8K093; -.
DR   Ensembl; ENSMUST00000061632; ENSMUSP00000057449; ENSMUSG00000050663.
DR   GeneID; 237553; -.
DR   KEGG; mmu:237553; -.
DR   UCSC; uc007hat.2; mouse.
DR   CTD; 29953; -.
DR   MGI; MGI:2384311; Trhde.
DR   eggNOG; COG0308; -.
DR   GeneTree; ENSGT00760000119082; -.
DR   HOGENOM; HOG000106482; -.
DR   HOVERGEN; HBG095698; -.
DR   InParanoid; Q8K093; -.
DR   KO; K01306; -.
DR   OMA; FDECGAS; -.
DR   OrthoDB; EOG754HNR; -.
DR   PhylomeDB; Q8K093; -.
DR   TreeFam; TF300395; -.
DR   ChiTaRS; Trhde; mouse.
DR   NextBio; 383404; -.
DR   PRO; PR:Q8K093; -.
DR   Bgee; Q8K093; -.
DR   CleanEx; MM_TRHDE; -.
DR   ExpressionAtlas; Q8K093; baseline and differential.
DR   Genevestigator; Q8K093; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_N.
DR   InterPro; IPR015570; TRH-DE.
DR   PANTHER; PTHR11533; PTHR11533; 1.
DR   PANTHER; PTHR11533:SF40; PTHR11533:SF40; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Aminopeptidase; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein;
KW   Protease; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN         1   1025       Thyrotropin-releasing hormone-degrading
FT                                ectoenzyme.
FT                                /FTId=PRO_0000095119.
FT   TOPO_DOM      1     40       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     41     61       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     62   1025       Extracellular. {ECO:0000255}.
FT   REGION      405    409       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    442    442       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       441    441       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       445    445       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       464    464       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   SITE        528    528       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   MOD_RES      30     30       Phosphothreonine; by PKC. {ECO:0000255}.
FT   CARBOHYD     90     90       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    161    161       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    176    176       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    223    223       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    606    606       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    635    635       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    650    650       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    664    664       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    685    685       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    801    801       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    907    907       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     68     68       Interchain. {ECO:0000250}.
SQ   SEQUENCE   1025 AA;  117458 MW;  0990B2A78A13B8AB CRC64;
     MGEDDAALRA SGRGLSDPWA DSVGVRPRTT ERHIAVHKRL VLAFAVSIVA LLAVTMLAVL
     LSLRFDECGA SAAMPGTDGG LGGFPERDSN SSFPGSARRN HHAGGESSQR ESGEVGTPGT
     PSAQPPSEEE REQWQPWTQL RLSGHLKPLH YNLMLTAFME NFTFSGEVNV EIACRNATRY
     VVLHASRVAV EKVQVAEDRA FGAVPVAGFF LYPQTQVLVV VLNRTLDAQR HYNLKIIYNA
     LIENELLGFF RSSYVIHGER RFLGVTQFSP THARKAFPCF DEPIYKATFK ISIKHQATYL
     SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAICNF TYRETTTKSG VVVRLYARPD
     AIRRGSGDYA LHITKRLIEF YEDYFKVPYS LPKLDLLAVP KHPYAAMENW GLSIFVEQRI
     LLDPSVSSIS YLLDVTMVIV HEICHQWFGD LVTPVWWEDV WLKEGFAHYF EFVGTDYLYP
     AWNMEKQRFL TDVLHEVMLL DGLASSHPVS QEVLRATDID RVFDWIAYKK GAALIRMLAN
     FMGHSVFQRG LQDYLTIHKY GNAARNDLWN TLSEALRRNG KYVNIQEVMD QWTLQMGYPV
     ITILGNTTAE NRILITQQHF IYDIGAKTKA LQLQNSSYLW QIPLTIVVGN RSHVSSEAII
     WVSNKSEHHR IAYLDRGSWI LGNINQTGYF RVNYDLRNWR LLIDQLIRNH EVLSVSNRAA
     LIDDAFSLAR AGYLPQNIPL EIIRYLSEEK DFLPWHAASR ALYPLDKLLD RMENYNIFNE
     YILKQVATTY IKLGWPRNNF NGSLVQASYQ HEELRREVIM LACSFGNKHC HQQASTLISD
     WISSNRNRIP LNVRDIVYCT GVSLLDEDVW EFIWMKFHST TAVSEKKILL EALTCSDDRN
     LLSRLLNLSL NSEVVLDQDA IDVIIHVARN PHGRDLAWKF FRDKWKILNT RYGEALFMNS
     KLISGVTEFL NTEGELKELK NFMKSYDGVA SASFSRAVET VEANVRWKRF YQDELFQWLG
     KAMRH
//
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