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Database: UniProt
Entry: A0A195F586_9HYME
LinkDB: A0A195F586_9HYME
Original site: A0A195F586_9HYME 
ID   A0A195F586_9HYME        Unreviewed;      1302 AA.
AC   A0A195F586;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-JUN-2019, entry version 21.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:KYN35337.1};
GN   ORFNames=ALC56_10512 {ECO:0000313|EMBL:KYN35337.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN35337.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN35337.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN35337.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN35337.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KQ981820; KYN35337.1; -; Genomic_DNA.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078541};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Integrin {ECO:0000313|EMBL:KYN35337.1};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1302       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008271207.
FT   DOMAIN      270    474       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      480    568       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      716    753       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      764    784       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   REGION      903    926       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   REGION      987   1017       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   REGION     1036   1235       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   REGION     1277   1302       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS    770    784       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS    904    926       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS    999   1013       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS   1055   1069       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS   1114   1140       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS   1189   1203       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS   1213   1235       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   COMPBIAS   1277   1291       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A195F586}.
FT   DISULFID    540    560       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    743    752       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1302 AA;  145044 MW;  A414332E31A4FEF7 CRC64;
     MFWLHCGLFV LVIAVRGFIS SLADTTSKRE ADYTLDDSFW KEEETPAGEV ERLLHEYRQN
     QELIRNIGGH YYQIIYPVQL RHHEKMGIST REVGVPKFPQ RGYGDGGYQN SRGRLRTGRH
     FHRTSLLIKA FNHKFRLDLE LNTQLLAPNL IQKDFLAGNA EQMSKQEIEH CYYHGTVRDY
     PGASAAFHTC NGVSGVIHLG NETFVIHPFY GGDLSKHPHI IFEARTKVNK GCANSGNLEW
     RVKNRRQKHI FGLSETTSDR YKRDVREATK YIETAIIIDK AMFDKRNGST RAEVVHDAIQ
     VANIADLYFR TLNTRVSVVY IESWKGSNQA QIDNGIDIDQ ALLSFNDYTM RRMYQVAQDT
     TQLLTGETFS GGESGVAVPE TVCSQRSVGI SVDLNTYEPH LLAGTMAHMI GHNIGMSHDD
     GRNDCNCRDW HGCIMAQSIV GLENVQPYKF SECSKTDYIE ALKSGHGICL FNKPNELEIR
     RSCGNRVIDD GEQCDCGSIE ECKEYDPCCD PITCKLTTEA ECATGPCCSD CKLRARGVVC
     RESTNECDLP EMCTGDTGQC PPDVYKKNGN PCANNAGHCF NGICPALDLQ CEQVWGYGGI
     AADKECFEQF NSKGSINGHC GTDSSGHLIK CESENVRCGS LQCQQGSKQP VIDGMKDLHT
     RTIISIKNQE YECKATNGRV EGSDIPGMGL VRDGTSCGDN LICVNQTCTS LFPYIDQEKC
     PSNHDDKECS GNGVCTNVNK CHCFLGWSGP DCSIEQSIPT ALPTTSEPEV VHKPDSKLPE
     KKETPYENYH GSNTVFLVGM LMSVVGGVFV LFTLVALCYR SVVVHKNFSL CLRRKSTVQK
     YDPPYSKKPQ QKSYSGVSGN HHAEAAALDT VNKILTFGSM PQYSRGETQR VLFRHPNNVV
     TADGSRVKEH KPQPKRLGVE EEDGGLGGGA IEHVERTLNQ LNGYHEDILE VLKNAASRRD
     LVGTPSGSNL LDEDALRKSL AECGYPDMYR KDTDGQDNGI DNGQEEEEDD VELQPPCGTI
     RIRNLEDLIR QLEHRASARP YMTGQMSPSG SEEIRTSETE PDRHYRIDSS VCSESSQGRC
     SRGRDEDASR FVYGRYRQPT SRSPYGNHQH THQHSHQMHP EDEGIYETAD PDRGSNTRGE
     TPDCESDAFI QAQQQVARWT SEDGGGGGGG GVQHRPPQQP PPPPAMPVQQ QVQQQQHQLP
     VEQLPITQRG YYPSPPQIEN NLDAGSNAEV ESAQSQQQQT LSEVRGIDVN HTPNINKRPL
     DDNFSLDCNI MNNDSPKELI TNNTSDNENT ALLPPHFPEY KH
//
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