GenomeNet

Database: UniProt
Entry: G3T1C0_LOXAF
LinkDB: G3T1C0_LOXAF
Original site: G3T1C0_LOXAF 
ID   G3T1C0_LOXAF            Unreviewed;      1022 AA.
AC   G3T1C0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   05-JUN-2019, entry version 65.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=TLL2 {ECO:0000313|Ensembl:ENSLAFP00000006852};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000006852, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000006852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006852};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S.,
RA   Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000006852}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006852};
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001199-2,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001199-
CC       2, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   RefSeq; XP_003409259.1; XM_003409211.2.
DR   STRING; 9785.ENSLAFP00000006852; -.
DR   MEROPS; M12.018; -.
DR   Ensembl; ENSLAFT00000008168; ENSLAFP00000006852; ENSLAFG00000008166.
DR   GeneID; 100673280; -.
DR   KEGG; lav:100673280; -.
DR   CTD; 7093; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000160572; -.
DR   InParanoid; G3T1C0; -.
DR   KO; K13047; -.
DR   OMA; SSMFLRF; -.
DR   OrthoDB; 170905at2759; -.
DR   TreeFam; TF314351; -.
DR   Proteomes; UP000007646; 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:InterPro.
DR   GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   Pfam; PF07645; EGF_CA; 1.
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; SSF49854; SSF49854; 5.
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   Complete proteome {ECO:0000313|Proteomes:UP000007646};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00601599};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00438935};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973787};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2,
KW   ECO:0000256|RuleBase:RU361183, ECO:0000256|SAAS:SAAS00973795};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS01068076};
KW   Protease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Repeat {ECO:0000256|SAAS:SAAS00792548};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973802}.
FT   SIGNAL        1     32       {ECO:0000256|RuleBase:RU361183}.
FT   CHAIN        33   1022       Metalloendopeptidase.
FT                                {ECO:0000256|RuleBase:RU361183}.
FT                                /FTId=PRO_5005131921.
FT   DOMAIN      358    470       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      471    583       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      583    624       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      627    739       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      739    779       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      783    895       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      896   1012       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   REGION       93    144       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3T1C0}.
FT   COMPBIAS    105    123       Polar. {ECO:0000256|MobiDB-lite:G3T1C0}.
FT   ACT_SITE    250    250       {ECO:0000256|PIRSR:PIRSR001199-1}.
FT   METAL       249    249       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       253    253       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       259    259       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
SQ   SEQUENCE   1022 AA;  115180 MW;  9BA24753B02883FF CRC64;
     MRRATALGAL GPLLLPPMLL LLLLPLPRGA EGFGERSDAA SDYWTPEDEE GAEQQLEHYH
     DPCKAAVFWG DIALDEDDLK LFHIDKARDW AKQPMEKMEP STGGLEEQPS ESWPNTTAMN
     TSSEEAKKDG KENTTLPQSP GTLNAVAETF SHRVRRATTS RTERIWPGGV IPYVIGGNFT
     GSQRAIFKQA MRHWEKHTCV TFIERTEEES FIVFSYRTCG CCSYVGRRGG GPQAISIGKN
     CDKFGIVAHE LGHVVGFWHE HTRPDRDQHV TIIRENIQPG QEYNFLKMEA GEVSSLGETY
     DFDSIMHYAR NTFSRGVFLD TILPRRDDNG VRPTIGQRVR LSQGDIAQAR KLYKCPACGE
     TLQDTTGNFS APGFPNGYPS YSHCVWRISV TPGEKIILNF TSMDLFKSRL CWYDYVEVRD
     GYWRKAPLLG RFCGDKVPEP LISTDSRLWV EFRSSSNILG KGFFAEYEAT CGGDINKDAG
     QIQSPNYPDD YRPSKECVWR ITVSEGFHVG LTFQAFEIER HDSCAYDYLE IRDGLTEEST
     LIGHFCGYEK PEDVKSSSNR MWMKFVSDGS INKAGFAANF FKEVDECSWP DHGGCEQRCV
     NTLGSYKCAC DPGYELKADK KACEVACGGF ISKLNGTITS PGWPKEYPTN KNCVWQVVAP
     VQYRISLQFE VFELEGNDVC KYDFVEVRSG LSQDARLHGK FCGSETPDVI TSQSNNMRVE
     FKSDNTVSKR GFRAHFFSDK DECATDNGGC QHECVNTFGS YLCRCRNGYR LHENGLDCKE
     AGCEHRLSSA EGTLASPNWP DKYPSRRECT WNISSTAGHR VKLTFNEFEI EQHQECAYDH
     LEMYDGPDSL APILGRFCGS KKPAPVVASS SSLFLRFHSD ASVQRKGFQA VHSTECGGRL
     KAEVQTKELY SHAQFGDNNY PSQARCDWVI VAEDGYGVEL IFRTFEVEEE ADCGYDYMEA
     YDGYDSTAPR LGRFCGSWPL EEIYSAGDSL MIRFHTDDTI NKKGFHARYT STKFQDALHM
     KK
//
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