ID M3YS15_MUSPF Unreviewed; 963 AA.
AC M3YS15;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=TLL1 {ECO:0000313|Ensembl:ENSMPUP00000014125.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000014125.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000014125.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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; AEYP01096997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01096998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01096999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01097000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01097001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01097002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01097003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01097004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012904923.1; XM_013049469.1.
DR AlphaFoldDB; M3YS15; -.
DR STRING; 9669.ENSMPUP00000014125; -.
DR Ensembl; ENSMPUT00000014350.1; ENSMPUP00000014125.1; ENSMPUG00000014233.1.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000157225; -.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; M3YS15; -.
DR OMA; VWKIMVS; -.
DR OrthoDB; 2873870at2759; -.
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: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; PTHR24251:SF37; CUB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 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; 1.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001199-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 98..297
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 299..411
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 412..524
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 568..680
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 680..720
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 724..836
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 837..953
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 190
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 194
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 200
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 160..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 162..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 963 AA; 109235 MW; C853702BED83F429 CRC64;
MMGGQSQSVF WGDIALDDED LSIFQIDRTI DLTQNPFGLG HTTGGFGDHG MSKKRGALYQ
LIDRIRRIGS GLEQNSTVKG KVPLKFSGQN EKNRVPRAAT SRTERIWPGG VIPYVIGGNF
TGSQRAMFKQ AMRHWEKHTC VTFIERSDEE SYIVFTYRPC GCCSYVGRRG NGPQAISIGK
NCDKFGIVVH ELGHVIGFWH EHTRPDRDNH VTIIRENIQP GQEYNFLKME PGEVNSLGER
YDFDSIMHYA RNTFSRGMFL DTILPSRDDN GIRPAIGQRT RLSKGDIAQA RKLYRCPACG
ETLQESNGNL SSPGFPNGYP SYTHCIWRIS VTPGEKIVLN FTTMDLYKSS LCWYDYIEVR
DGYWRKSPLL GRFCGDKFPE VLTSTDSRMW IEFRSSSNWV GKGFAAVYEA ICGGEIRKNE
GQIQSPNYPD DYRPMKECVW KITVSEDYYV GLTFQAFEIE RHDNCAYDYL EVRDGTSENS
PLIGRFCGYD KPEDIRSTSN TLWMKFVSDG TVNKAGFAAN FFKEEDECAK PDRGGCEQRC
LNTLGSYQCA CEPGYELGPD KRSCEAACGG LLTKLNGTIT TPGWPKEYPP NKNCVWQVVA
PTQYRISMKF EFFELEGNEV CKYDYVEIWS GLSSESKLHG KFCGAEVPDV ITSQFNNMRI
EFRSDNTVSK KGFKAHFFSD KDECSKDNGG CQHECVNTMG SYMCQCRNGF VLHENKHDCK
EAECEQKIHS PNGFITSPNW PDKYPSRKEC TWEISTTPGH RIKLAFSEFE IEQHQECAYD
HLEVFDGETE KSPILGRLCG NKIPEPLVAT GSKMFVRFVS DASVQRKGFQ ATHSTECGGR
LKADPKPRDL YSHAQFGDNN YPGQVDCEWL LVSERGFRLE LSFQIFEVEE EADCGYDYVE
LFDGLDSTAV GLGRFCGSGP PEEIYSIGDA VLIHFHTDDT INKKGFHIRY KSIRYPDTMH
TKK
//
