ID G1PPR7_MYOLU Unreviewed; 683 AA.
AC G1PPR7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Thimet oligopeptidase {ECO:0000256|ARBA:ARBA00039633};
DE EC=3.4.24.15 {ECO:0000256|ARBA:ARBA00039079};
GN Name=THOP1 {ECO:0000313|Ensembl:ENSMLUP00000013017.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013017.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013017.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000013017.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues at
CC P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15
CC residues.; EC=3.4.24.15; Evidence={ECO:0000256|ARBA:ARBA00036235};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; AAPE02042119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02042120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PPR7; -.
DR STRING; 59463.ENSMLUP00000013017; -.
DR Ensembl; ENSMLUT00000014311.2; ENSMLUP00000013017.2; ENSMLUG00000014305.2.
DR eggNOG; KOG2089; Eukaryota.
DR GeneTree; ENSGT00950000183171; -.
DR HOGENOM; CLU_001805_2_1_1; -.
DR InParanoid; G1PPR7; -.
DR OMA; KNFQSAM; -.
DR TreeFam; TF300459; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF50; THIMET OLIGOPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 223..671
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 683 AA; 77920 MW; 95F8D1F610DBE4AF CRC64;
VACTADVLDK AAPCSVVNYL RWDLNAQQIA ELTAELMEQT KCVYDQVGSL KFEDVSYEST
LKALADVEVS YTVQRNILDF PQHVSPSKDI RTASTEADKK LSEFDVEMSM RQDVYQRIVW
LQEKVQKDSL RPEAVRYLER LIKLGRRNGL HLPEETQEKI KGIKKKLSLL CIDFNKNLNE
DTTFLPFTRE ELGGLPEDFL NSLEKTEDEK FKVTLKYPHY FPLLKKCHVP ETRRKVEEAF
NCRCKEENCA ILRELVTLRA QKSSLLGFGT HADYVLEMNM AKTSQTVATF LDELAQKLKP
LGEQERAVIL ELKKAECEKR GLDFDGRINA WDMRYYMNQV EETCYSVDQN LLKEYFPMQV
VTRGLLGIYQ ELLGLTFDLE EHAAVWHEDV KLYSVRDTAS GTVIGKFYLD LYPREGKYGH
AACFGLQPGC LRQDGSRQIA IAAMVANFTK PTPDAPSLLQ HDEVETYFHE FGHVMHQLCS
QAEFAMFSGT HVERDFVEAP SQMLENWVWE KEPLLRMSQH YRTGSAIPQE LLEKLIKSRQ
ANTGLFNLRQ IVLAKVDQAL HTQKAAEPAE EYSRLCQEIL GVPATPGTNM PATFGHLAGG
YDAQYYGYLW SEVYSMDMFH TRFKQEGVLN GKVGLDYRSC ILRPGGSEDA SVMLKLFLGR
DPKQDAFLLS KGLQVEGSKL LAC
//
