ID C3ZEU6_BRAFL Unreviewed; 867 AA.
AC C3ZEU6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=BRAFLDRAFT_120123 {ECO:0000313|EMBL:EEN49252.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN49252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49252.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49252.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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:PRU00121}.
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DR EMBL; GG666612; EEN49252.1; -; Genomic_DNA.
DR RefSeq; XP_002593241.1; XM_002593195.1.
DR AlphaFoldDB; C3ZEU6; -.
DR eggNOG; KOG3714; Eukaryota.
DR eggNOG; KOG4157; Eukaryota.
DR InParanoid; C3ZEU6; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00108; KR; 2.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 3.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR10127:SF780; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 3.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57440; Kringle-like; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 3.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 40..249
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 300..380
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 718..801
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 809..867
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT REGION 517..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 409..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 416..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 428..443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 867 AA; 96717 MW; 59C8BDF55D49FE5A CRC64;
MDSFQLTVRK AAVLVLIIVA CIATVTELGS EPTFKRPKRK AIRDLRLRWP GGTIPYIMGD
SLSHRDRSYI AEAMEKWHQH SCARFKPYSR KLASYLGHHD HIIFYKGIGC LSDVGRLLER
DQQVVSINDA CLFATSNPVG VILHELGHVL GLYHEHSRPD RDEFVDILVN NIRPGEEYNF
QKMSSSDINL YNIPYDYMSI MHYYNTEWTV RADLQTIVTK DTKYQYFIGH KQALSFYDIK
TVNLLYGCGD KCPAMDCPEE AFVAYNCSCM CNDIHDYSAV FSCPERTLKE VHLSLRQARM
CYHGHGSDYR GTVAVTDAGE PCLKWSEATY RQFNTYNYPV GYHGLGDHNY CRNPAGRILK
KPWCYVNSDN SWGYCDVQEC REVYSPVQPT IPARPAVPAR PPTPKPTQCK STEFRCTDGT
CIPTAYRCDR DNDCKDNSDE LGCVYDTCPP LNIQADVMIS NCESGKPQLR GKVCRVLCLV
GSGPGETIIS TTCQSDGKWS APKGKLVCEK PENPIIPATR PKQSLTTPAP NKPTAAVVTT
QKPPRMTTKM PEKKPSATTK PTPKTCQDLV VPADVTTSCD ADKNEIGTVC LLKCSAGDGQ
SITKCLPDGS WSIPKENLDC PRVHVQTTQK PTVSPTEKPA EKPTEKPTAK PTQKQTVKPT
QKPTVKPTEK PTVKPTPKPT VKPTPKPTVK PTVKPIVRPI GTPKPTPQPT QKPLPPGDCY
TGDGSSYRGF KSTTTDGRAC LKWSDAKYQY YNTLRFTAGQ YGIGYHNYCR NPAGVETEPW
CYYINPATRR VTWSHCGAQQ CGGERITLKC AVRDSTGYRG TQDVTMHGDK CLNWSTTTNR
QFSTQTYPNG EGGIGNHNYC RNPTDKG
//
