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Database: UniProt
Entry: A0A2K5C411_AOTNA
LinkDB: A0A2K5C411_AOTNA
Original site: A0A2K5C411_AOTNA 
ID   A0A2K5C411_AOTNA        Unreviewed;       978 AA.
AC   A0A2K5C411;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=TLL1 {ECO:0000313|Ensembl:ENSANAP00000003446.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000003446.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000003446.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|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   AlphaFoldDB; A0A2K5C411; -.
DR   Ensembl; ENSANAT00000021085.1; ENSANAP00000003446.1; ENSANAG00000019560.1.
DR   GeneTree; ENSGT00940000157225; -.
DR   Proteomes; UP000233020; Unplaced.
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; 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};
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:UP000233020};
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          113..312
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          314..426
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          427..539
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          539..580
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          583..695
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          695..735
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          739..851
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          852..968
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         205
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         209
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         215
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"
SQ   SEQUENCE   978 AA;  110730 MW;  0CED0A199570E3D4 CRC64;
     SRDRATALQP GDRETLTRKE KSIFWGDIAL DDEDLNIFQI DSTIDLTQNP FGNLGHTTGG
     LGDHAMSKKR GALYQLIEKI RRIGFGLEQN NTVKGKVPLQ FSGQNEKNRV PRAATSRSER
     IWPGGVIPYV IGGNFTGSQQ AMFKQAMRHW EKHTCMTFIE RSDEESYIVF THRPCGCCSY
     VGRRGNGPQA ISIGKNCDKF GIVVHELGHV IGFWHEHTRP DRDNHVTIIR ENIQPGQEYN
     FLKMEPGEVN SLGERYDFDS IMHYARNTFS RGMFLDTILP SRDDNGIRPA IGQRTRLSKG
     DIAQARKLYR CPACGETLQE SNGNLSSPGF PNGYPSYTHC IWRVSVTPGE KIVLNFTTMD
     LYKSSLCWYD YIEVRDGYWR KSPLLGRFCG DKVPEVLTST DSRMWIEFRS SSNWVGKGFA
     AVYEAICGGE IRKNEGQIQS PNYPDDYRPM KECVWKITVS EGYHVGLTFQ SFEIEKHDNC
     VYDHLEVRDG TSENSPLIGR FCGHEKPEDV RSTSNTLWMK FFSDGTVNKA GFAANFFKEE
     DECAKPDRGG CEQRCLNTLG SYQCTCEPGY ELGPNRRSCE AACGGLLTKL NGTITTPGWP
     KEYPPNKNCV WQVIAPTQYR ISVKFEFFEL EGNEVCKYDY VEIWSGLTSE SKLHGKFCGA
     EVPEVITSQF NSMRIEFKSD NTVSKKGFKA QFFSDKDECS KDNGGCQHEC VNTMGSYMCQ
     CRSGFVLHEN KHDCKEAECE QKIHSPTGLI TSPNWPDKYP SRKECTWEIS ATPGHRIKLA
     FSEFEIEQHQ ECAYDHLEVF DGETEKSPIL GRLCGNNIPD PLVATGNKMF VRFVSDASVQ
     RKGFQAMHST ECGGQLKAES KPRDLYSHAQ FGDNNYPGQV DCEWLLVSER GSRLELSFQT
     FEVEEEADCG YDYVELFDGF DSTAVGLGRF CGSGPPEEIY SIGDAVLIHF HTDDTINKKG
     FHIRYKSIRY PDTTHTKK
//
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