ID F4W9W1_ACREC Unreviewed; 952 AA.
AC F4W9W1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
DE Flags: Fragment;
GN ORFNames=G5I_02269 {ECO:0000313|EMBL:EGI69097.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI69097.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001809};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; GL888033; EGI69097.1; -; Genomic_DNA.
DR AlphaFoldDB; F4W9W1; -.
DR STRING; 103372.F4W9W1; -.
DR MEROPS; M12.322; -.
DR EnsemblMetazoa; XM_011070782.1; XP_011069084.1; LOC105154964.
DR eggNOG; KOG3658; Eukaryota.
DR InParanoid; F4W9W1; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR049038; ADAM10_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF3; KUZBANIAN-LIKE, ISOFORM A; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13574; Reprolysin_2; 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; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Integrin {ECO:0000313|EMBL:EGI69097.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 597..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..362
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 376..472
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 640..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI69097.1"
SQ SEQUENCE 952 AA; 105985 MW; 76ABAA062DC40BA5 CRC64;
VVQGVVTQDG LFDGSVVTRF EEYYIEPTSR YLNKNEDTSP PYHSIAYRTS DVTTPPHPLP
CASHQLHQER SLRDSFDRNY RYNNSQAFYE PLLGEHVALY SRENNARVLT LETNNDVEYT
DAVSGRDRIA RHLHKRATID PRKTTCMLYL QADHQFFARY GTEEACIEVM TRHVQRVNSI
YKHTDFNQDG RPDNISFMIK RVKVHSEDAL RDPHYRFPGN YGVEKYLELF SEEDYDAFCL
AYMFTYRDFE MGTLGLAWTG DLKNAGGVCE KNGHYRGSMK SLNTGIVTLL NYGKHVPPAV
SHVTLAHEIG HNFGSPHDPE QCTPGGEDGN FIMFARATSG DKRNNNRFSP CSLNAINPVL
NSKARSPKGC FTEPQVSLCG NGVVEEGEEC DCGWEEDCRD SCCYPQRRYP PPEETPCTLT
PRAVCSPSQG PCCTSECNLR FGDKCRDDNG CRDASFCDGR SPYCPPSINK PNKTICNREL
VCFMGECTGS ICLAYGLESC QCIPGPNDPP TKACELCCRL PGENQPCLSS FDWNSPPYDI
PDMFSKPGTP CNDYNGYCDV FQKCREVDPS GPLATLRKLL LSDESLATFR RWVAEHWYAA
ALIILAAISL LVASMRLLGK RPDLKLKSVT IIHSSTTETV RLPPEGTEGV TVHPPAVRAK
LPLSRKVREK RCHRKHKDGG HTDKSNNKDA KKKQNQQAKR SSTGQVDDFA RKRPAEVLTA
VTQENKRKKI TSVRDKGQGT SNNPGGGSSG DNDKRKRKKQ HRKEVIDYSA IQADKESETN
ADPKSKVRSW LLASSQCRPE TGARTNVNGM PKSKSTPVGL TASGGAVGSR VLKNSSNSLA
RKERARLQVV YKPPFRFSVK LRKSDKVAQA PATAVNHTNA NSRTAKLPRT GVLLRTAKRK
DRVRIGRARQ IAPTGIGNSG GDLPEPANSD LHTVPSDLEV LLSESEFLFS DT
//
