ID E2AWT7_CAMFO Unreviewed; 1051 AA.
AC E2AWT7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Tolloid-like protein 2 {ECO:0000313|EMBL:EFN62057.1};
GN ORFNames=EAG_04191 {ECO:0000313|EMBL:EFN62057.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62057.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL443425; EFN62057.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AWT7; -.
DR STRING; 104421.E2AWT7; -.
DR MEROPS; M12.011; -.
DR InParanoid; E2AWT7; -.
DR OMA; NHQECIY; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
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; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
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 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, ECO:0000256|PROSITE-
KW ProRule:PRU00059};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 292..352
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 369..485
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 486..599
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 599..639
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 642..759
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 759..799
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 803..915
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 916..1032
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 486..513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 1051 AA; 120007 MW; C58EBEB9B4ED8AA7 CRC64;
MKNEVSHIDS EIKTVPTSRL ALRHDFMKQR YIILDEWREQ KLNKSYLEEL EKYREEILKE
GLQVEEEGLT EILQFKSEHD VNKQVFNEHN DAVVKKKSES IDRNQYSMGG ESDGFSFNDR
SDDTNPAVKN EGLVFRLESS TQASKKKYFE RQARRQISRT VLISESVKAR HPTHDMPLEF
STSTAFTTEP SKYVGRVYTD NIKETFNAQT ELNTQNPSNR RRRRHHRKRI LGRRSHHHCN
RRTHDFITDA SDEVISAHDR RLRSIEFYNM DHKPKLINKH GTKHFSSRIR RAATARKERV
WDHGVIPYEI DGNFSGAHKA LFKQAMRHWE NFTCVKFVER VSREHPNYIL FTERPCGFIQ
LSKPIFAECG RTFQENSGIF ASPNYPNNSP PTDGERCEWR ITATHGERIV LNITFLDIFK
SNYCRSDYLE IRDGYWHKSR VLGRYCGSGK MHEPIVSSGS RMLVTYVISS KQSGHRGFTA
SYEAVCGGDV ELDGIGHLES PNYPEEYQSS KECVWKLSVP QDYQVALKFQ SFEIENHDNC
VYDYVEVRDG HDNDSPLIGV YCGYKIPPDI KSVGNKLLVK FVSDGSVQKA GFSATFMKEF
DECILTDHGC EHNCTNTLGG YECSCKIGYE LHSDGKHCED ACGGFFNGSN GTITSPSFPE
AYPGNKNCVW EIVAPSQYRI TLNFTHFDLE GNNVYQEECE YDSVEVASKL GDDVLRKHGI
FCGARLPSLI TSEGNFMRIT FTSDNSVQKS GFAAIFFTDM DECASNNGGC QHECKNTIGS
YQCSCHNGFT LHENGHDCKE GGCKYEIIAP VGTITSPNYP DYYPGRKDCV WHFTTKPGHR
IKLVFKVFEM ESHQECAYDH IVIYDGDSPD SLTLGRFCGT KEPHPILATG NQMYMVFKSD
ASVQRKGFLA THSTACGGHL MATDRVKHLY SHAKYGYHNY DHNTDCDWII EAPLGKNVHL
SFHSFQLEYE TECGYDFVEV FSGLDVSSPP YGRFCGNSNT TDFISMNEAL LVRFRTDDTI
SSKGFIAIFV AIDRQDSEEN FGGEDDEEQN L
//
