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 01-MAY-2013, entry version 87.
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 (By
CC similarity).
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: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
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DR EMBL; BC032288; AAH32288.1; -; mRNA.
DR IPI; IPI00169524; -.
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; ENSGT00620000087820; -.
DR HOGENOM; HOG000106482; -.
DR HOVERGEN; HBG095698; -.
DR InParanoid; Q8K093; -.
DR KO; K01306; -.
DR OMA; FTYRETT; -.
DR OrthoDB; EOG4NZTSG; -.
DR NextBio; 383404; -.
DR ArrayExpress; Q8K093; -.
DR Bgee; Q8K093; -.
DR CleanEx; MM_TRHDE; -.
DR Genevestigator; Q8K093; -.
DR GermOnline; ENSMUSG00000050663; Mus musculus.
DR GO; GO:0016021; C:integral to 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR024571; DUF3358.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_N.
DR InterPro; IPR015570; Peptidase_M1_TRH-DE.
DR PANTHER; PTHR11533; PTHR11533; 1.
DR PANTHER; PTHR11533:SF40; PTHR11533:SF40; 1.
DR Pfam; PF11838; DUF3358; 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 (Potential).
FT TRANSMEM 41 61 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 62 1025 Extracellular (Potential).
FT REGION 405 409 Substrate binding (By similarity).
FT ACT_SITE 442 442 Proton acceptor (By similarity).
FT METAL 441 441 Zinc; catalytic (By similarity).
FT METAL 445 445 Zinc; catalytic (By similarity).
FT METAL 464 464 Zinc; catalytic (By similarity).
FT SITE 528 528 Transition state stabilizer (By
FT similarity).
FT MOD_RES 30 30 Phosphothreonine; by PKC (Potential).
FT CARBOHYD 90 90 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 176 176 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 223 223 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 339 339 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 606 606 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 635 635 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 650 650 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 664 664 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 685 685 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 801 801 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 907 907 N-linked (GlcNAc...) (Potential).
FT DISULFID 68 68 Interchain (By similarity).
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
//
