ID A0A026VWG5_OOCBI Unreviewed; 1311 AA.
AC A0A026VWG5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein {ECO:0000313|EMBL:EZA48108.1};
GN ORFNames=X777_14217 {ECO:0000313|EMBL:EZA48108.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA48108.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA48108.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KK107681; EZA48108.1; -; Genomic_DNA.
DR OMA; TTSDRYK; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 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; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:EZA48108.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1311
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001545273"
FT TRANSMEM 792..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..473
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 478..566
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 714..751
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 865..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1007
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 538..558
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 741..750
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1311 AA; 146235 MW; 198DF61C6CE64DF3 CRC64;
MFWLHCGLFV LVIAVPGFIS SLADTTSKRE ADYTLDDSFW NEDTPIGEAE RLLREYRQNQ
ELVSNIGGNF YQIIYPVQLR HHEKMGISTR EVGVSKFPQR GYGDGGYQNS RSRGRTGRHF
HRTSLLIKAF NHKFRLDLEL NTQLLAPNLM QKDFLTGNAE QTSKQEIEHC YYHGTVRDYP
GASAAFHTCN GVSGVIHLGN ETFVIHPFYG GDLSKHPHII FEARTKANKG CANSANNERR
VKSRRQKHIL GLPKTTSDRY KRDVREATKY IETAIIIDKA MFDKRNGSTR AEVVHDAIQV
ANIADLYFRT LNTRVSVVYI ETWKGSNQAD IDKGIDIDLA LINLNDYTMR RMYQLAQDTT
QLLTNYIYIY ICIYIAVPAT VCSQKSVGIS VDLNTYEPHL LAGTMAHMIG HNIGMSHDDG
RNDCNCRDWH GCIMAQSIVG LENVQPYKFS ECSKSDYIEA LKSGHGYCLF NKPNELEIRR
CGNRVIDEGE ECDCGTLDEC HELDPCCDPI TCKLRTEAEC ATGPCCSDCK LRVRGVVCRE
STNECDLPEV CTGDSGQCPP DVYKKNGNPC SNIAGYCFNG VCPALDLQCE QVWGYGGIAA
DKQCFEQFNS KGSINGHCGT DSSGHFIKCE AENVHCGSLQ CQQGSKQPVI DGMKDYYSRT
IISIKSQEYE CKATTGKVEG SDMPGWGLVR DGTSCGDNLI CVNQTCTSLF PHIDQGKCPS
NHDNSECSGN GVCTNVNKCY CFPGWSGPDC SIEQYIPTMS PTTSSPEVVG KADPKLEKKE
TPYENYHGSN TVFLVGMLMS VVGGVFVVFA LMALCYRRKS TVQKYDLPYS KKPPQKSYSG
VSGNHHAEAA ALETVNKILT FGRMPQYRDK PQPKRHGVEE EDGGTGAEEV VSFIDLPPNN
LTKLPEKGIL KKHGGYGLGA GAIEHVERTL NQLNGYHEDI LEVLKNAASR RDLAGTPSGS
SNLLDDDVLR KSLAEVGWHP DVYHKDTDGQ DNGIDNGQED EEEDVELQPP CGTIRIRTLE
DLIRQLEHRA TARPYLPGQM SPSGSEEIRM SEGEPDRHYR IDSSVCSESS QGSRRCSRGR
DEDASRFVYG RYRQPTSRSP YGNHQHTHQH SHQIHPEDEG IYETADPDRG SNTRGETPDC
ESDAFIQAQQ QVARWTSEDG GGVQHRPPQQ PPPPPAMQLP VQQQAQQQQQ QSQQQPQQLQ
QQQQHQLPVE QLPIKQRGYY PSPPTENSLD VGNNAEAESA QSQQQQQTLS DVRGIDVNHL
PNIKKCPLDD NFSLDCNIMN NGSPKELTTN NNSDNENTAL LPPTHFPEYK H
//
