ID H0WT91_OTOGA Unreviewed; 893 AA.
AC H0WT91;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=TLL2 {ECO:0000313|Ensembl:ENSOGAP00000005350.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000005350.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000005350.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAQR03047664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03047665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03047666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WT91; -.
DR STRING; 30611.ENSOGAP00000005350; -.
DR Ensembl; ENSOGAT00000005985.2; ENSOGAP00000005350.2; ENSOGAG00000005983.2.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000160572; -.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; H0WT91; -.
DR OMA; WTKQTVG; -.
DR TreeFam; TF314351; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF34; CUB AND SUSHI DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF14670; FXa_inhibition; 2.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 27..227
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 229..341
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 342..454
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 454..495
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 498..610
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 610..650
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 654..766
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 767..883
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 90..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 92..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 893 AA; 100209 MW; 6A0BEADBBAE9A5FA CRC64;
GEENATLSHS PGTSNTAAGS SSSRVRRATT SRTERIWPGG VIPYVIGGNF TGHQRAIFKQ
AMRHWEKHTC VTFIERTDEE SFIVFSYRTC GCCSYVGRRG GGPQAISIGK NCDKFGIVAH
ELGHVVGFWH EHTRPDRDQH VTIIRENIQP GQEYNFLKME AGEVSSLGET YDFDSIMHYA
RNTFSRGVFL DTILPRRDDN GIRPTIGQRV RLSQGDIAQA RKLYKCPACG ETLQDTTGNF
SAPGFPNGYP SYSHCVWRIS VTPGEKIVLN FTSMDLFKSR LCWYDYVEVR DGYWRKAPLL
GRFCGDKVPE PLTSTDSRLW VEFRSSSNIL GKGFFAVYEA TCGGDIVKDA GQIQSPNYPD
DYRPSKECVW RISVSEGFHV GLTFQAFEIE RHDTCAYDYL EIRDGPTEES ALIGHFCGYE
KPEDVKSSSN MLWMKFVSDG SVNKAGFAAN FFKEVDECSW PDHGGCEHRC VNTLGSYKCT
CDPGYELGAD KKTCEVACGG FITKLNGTIT SPGWPKEYPT NKNCVWQVVA PVQYRISLQF
EAFELEGNDV CKYDFVEVRS GLSPDASLHG KFCGSETPEV ITSQSNNMRV EFKSDNTVSK
RGFRAHFFSD KDECAEDNGG CQHECVNTFG SYLCRCRNGY RLHDNGRDCK EAGCAHKISS
TEGTLASPNW PDKYPSRREC TWNISSTAGH RVKLTFNEFE IEQHQECAYD HLEMYDGPDS
LAPILGRFCG SKKPDPVVAS GSSLFLRFYS DASVQRKGFQ AVHSTECGGR LKAEVQTKEL
YSHAQFGDNN YPSQARCDWV IVAEDGFGVE LIFRTFEVEE EAECGYDYME AFDGYDSSAP
RLGRFCGSGP LEEIYSAGDS LMIRFHTDDT ISKKGFHARY TSTKFQDALH MKK
//
