ID A0A4X2L5Z6_VOMUR Unreviewed; 1016 AA.
AC A0A4X2L5Z6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=TLL1 {ECO:0000313|Ensembl:ENSVURP00010017100.1};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010017100.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010017100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSVURP00010017100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A4X2L5Z6; -.
DR STRING; 29139.ENSVURP00010017100; -.
DR Ensembl; ENSVURT00010019437.1; ENSVURP00010017100.1; ENSVURG00010013083.1.
DR GeneTree; ENSGT00940000157225; -.
DR OMA; VWKIMVS; -.
DR Proteomes; UP000314987; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 FunFam; 2.10.25.10:FF:000022; Metalloendopeptidase; 2.
DR FunFam; 2.60.120.290:FF:000004; Metalloendopeptidase; 1.
DR FunFam; 2.60.120.290:FF:000007; Metalloendopeptidase; 1.
DR FunFam; 2.60.120.290:FF:000009; Metalloendopeptidase; 1.
DR FunFam; 2.60.120.290:FF:000011; Metalloendopeptidase; 1.
DR FunFam; 3.40.390.10:FF:000004; Metalloendopeptidase; 1.
DR FunFam; 2.60.120.290:FF:000005; Procollagen C-endopeptidase enhancer 1; 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; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_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:SF45; METALLOENDOPEPTIDASE; 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; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
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|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01211}; Reference proteome {ECO:0000313|Proteomes:UP000314987};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 26..1016
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5021511735"
FT DOMAIN 151..350
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 352..464
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 465..577
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 577..618
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 621..733
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 733..773
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 777..889
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 890..1006
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 244
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 243
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 247
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 253
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 213..235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 215..216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 1016 AA; 115258 MW; D2830E8C1536BBCD CRC64;
MRRMGMEMLS QRLVLWLLAS ALIYGGEMRV SSGFDYDYTY AFHEEDKIET LDYKDPCKAA
VFWGDIALDD EDLRIFPIDR TIDVTQNSFE KLGRITGGLG DHGVSEKRGV LYQLIDRIRR
FGSGLEQNNT AIGKASVKFS GQNEKNRVPR AATSRTERIW PGGVIPYLIG GNFTGSQRAM
FKQAMRHWEK HTCVTFIERS DEESYIVFTY RPCGCCSYVG RRGNGPQAIS IGKNCDKFGI
VVHELGHVIG FWHEHTRPDR DKHVTIIREN IQPGQEYNFL KMEPGEVNSL GESYDFDSIM
HYARNTFSRG MFLDTILPSR DDNGIRPAIG QRTRLSKGDI AQARKLYRCP ACGETLQEST
GNFSSPGFPN GYPSYTHCIW RISVTPGEKI VLNFTTMDLY KSSLCWYDYI EVRDGYWRKS
PLLGRFCGDK LPEVLTSTDS RMWIEFRSSS NWVGKGLAAV YEAICGGEIH KNEGQIQSPN
YPDDYRPMKE CVWKIIASEN YNVGLTFQAF EIERHDSCAY DYLEIRDGSS ENSPLIGRFC
GYDKPEDIRS TSNTLWMKFV SDGTVNKAGF AANFFKEEDE CAKPDNGGCE QRCVNTLGSY
HCACEPGYEL GTDKRSCEAA CGGLLTKLNG TITTPGWPKE YPPNKNCIWQ VVAPTQYRIS
MKFEFFELEG NEVCKYDYVE IRSGLSSDSK LHGKFCGAEV PEMITSQFNN MRIEFKSDNT
VSKKGFRAHF FSDKDECSKD NGGCQHECIN TVGSYVCQCR NGFVLHENKH DCKEAECEEK
IHSPNGVITS PNWPDKYPSR KECTWEISTT PGHRVKLAFS EFEIEQHQEC AYDHLEVFDG
ETEKSPILGR LCGNKMPDPL VATGNKMFLR FVSDASVQRK GFQAQHSTEC GGPLKAESNP
RDLYSHAQFG DNNYPVQVHC EWLLMSERGS SVELSFQTFE VEEEADCGYD YVQLFDGHDS
TARNLGRFCG SGPPEEIYSS GDAILIYFHT DDTINKKGFH IRYKSRKYSA TAHTKK
//
