ID A0A493TIN4_ANAPP Unreviewed; 1023 AA.
AC A0A493TIN4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Thyrotropin releasing hormone degrading enzyme {ECO:0000313|Ensembl:ENSAPLP00000025500.1};
GN Name=TRHDE {ECO:0000313|Ensembl:ENSAPLP00000025500.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000025500.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000025500.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000025500.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR AlphaFoldDB; A0A493TIN4; -.
DR Ensembl; ENSAPLT00000046425.1; ENSAPLP00000025500.1; ENSAPLG00000004571.2.
DR GeneTree; ENSGT00940000155878; -.
DR Proteomes; UP000016666; Chromosome 1.
DR GO; GO:0016020; C:membrane; 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 CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF40; THYROTROPIN-RELEASING HORMONE-DEGRADING ECTOENZYME; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..352
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 389..590
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 677..1000
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 548
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1023 AA; 117759 MW; 5A8621B2B8205B8E CRC64;
MALEEKREKR PPVTPMMIEE EAALRNGSRG LPPGPWAEAA GPRPRTTERH IAVHKRLVLG
FAVSILALLA VTMVAVLLSV RFEECGAAAD GPPRVGGNGS LAGGARPPPR AGQPPGRPEP
EEQARGGEAT AAAAEEEEEE EEEEEEEWQR RRLLPPWARP RLPRHLRPLH YNLMLSAFME
NFTFCGEVNV QLEVRNASRY IVLHAHRMHI EAVRVAEDKL AGAVRVARSF LYPQTQVLVV
VLNRSLEVQR SYNLKIIYNA LIENELLGFF RSSYVLHGER RFLGVTQFSP THARKAFPCF
DEPIYKATFK ISIRHQATYI SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAVCNF
TYRETVTKSG VVVRLYARPD AIRRGSGDYA LNITRRLIEF YEDYFKVPYS LPKLDLLAVP
KHPYAAMENW GLSVFVEQRI LLDPSISSIS YLLDVTMVIV HELCHQWFGD LVTPVWWEDV
WLKEGFAHYF EFVGTDYLYP GWNMEKQRFL TDVLHEVMLL DGLASSHPVS QEVQQATDID
RVFDWIAYKK DYLTIHKYGN AARNDLWNTL SKALKRVGKS VNIQEVMDQW TLQMGYPVIT
ILGNETTDNV IVISQERFVY DSDAKTKDPD FGDNSYLWQI PLTIAVGNTS HISSEAIIWV
SNKSEHHRIP ALEEASWLLG NINQTGYFRV NYDVRNWRLL INQLTRNHEV ISVSNRAGLI
DDAFNLARAG YLPQNIPLEI IRYLSEEKDF LPWHAASRAL YPLDKLLDRT ESYNIFNEYI
LRQVASMYLK LGWPTNNLNK SLVQASYQHE ELRREVIMLA CSFGNKHCHQ QAATLISDWI
SSNRNRIPLN VRDIVYCTGV SLMDEDVWEF IWMKFHSTIA VSEKKILLEA LTCSDDRNLL
NRLLNLSLNS EVVLDQDAID VIIHVARNPH GRDLAWKFFR EKWKILNARY GEALFMNSKL
ISGVTEFLNT EEELRELKNF IKSYEEGTAA SFSRAVETVE ANVRWQRLYK EELFQWLRKS
LTH
//