ID T1IEU1_RHOPR Unreviewed; 991 AA.
AC T1IEU1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC014810-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC014810-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
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; ACPB03017714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03017715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03017716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACPB03017717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1IEU1; -.
DR STRING; 13249.T1IEU1; -.
DR EnsemblMetazoa; RPRC014810-RA; RPRC014810-PA; RPRC014810.
DR VEuPathDB; VectorBase:RPRC014810; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_005278_0_0_1; -.
DR InParanoid; T1IEU1; -.
DR OMA; TTSDRYK; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000015103; 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: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; 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; 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; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000015103};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 382..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 586..595
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 991 AA; 108399 MW; FF67CF7846CB4CD1 CRC64;
ITSKSFLFQE IEHCYYHGTV KDYPGATAAF HTCNGVSGVI HVGNETFVIQ PFYGGDLSKH
PHVIFESRIK TNKGCANAGN LEWRSFRRAK HLSNLVEAAN RRFRRDVAEA TKYIETALVI
DKAMFEKRNG STRAEVVHDA IQVANIADLY FRTLNTRVSV VYIETWQGAN QAVIDKTQDI
SRALLNFNDY TSRNLFHIDK DTAQLLTGEI FQGGEAGMSV PETVCTPKSV GISVDVNAYE
LYLLAGTMAH MIGHNIGMGH DGRREKCVCR DWHGCIMAQS IVGLENVQPY TFSECSRSDY
NSALRTGHGI CLLNKPNELE VRRTCGNNVV EEGEDCDCGM IPECQDIDPC CDPYTCKLKK
EAECASGPCC VACKLKKGGT VCREASNECD LPEHCTGEHG QCPLDVHKKN GNPCASESGY
CFNGICPTLD LQCKQIWGYD GVAGDIECYK QFNSKGSFSG HCGYDSDKKA FIKCDKENSR
CGSLQCQRGS SYPLVAGVDQ LYSRTIISTK GVEYECKATS GPVDQPDVPD LGLVRDGTPC
GENLICVNQT CTSIFPHMDQ GTCPSNHNKL ECSGNGVCTN VNKCYCFLGW SGPDCSIQVE
IIISPSPEAT AYPGSGQSQS DKADIEKQMN KKETPYENSH STNTVFLVGT LMSVVGGVFI
VFALSALCYR SVVVHKNFSL CLRRSTVPRM DPPYNKKPIV KGFGTSAQQT PEGAVAMSAP
NKLLGFGHIA GQRVLFRPNH MVPGGPASRF QEHKLQQMKR MGVGSGSEDD PGHSGEEETV
SFIDLPPNNL SKLPEKGILK KSCPYGGGGG SDDPCHKGSK WLDDTQSDAQ EMLSQSDNNL
TAEMISGGPI LEVERNLKTL NGYHEDILEA LRSAASRHHS GGPSSVTASS DDLLRRSLAA
AAALEAGYVR GSSQDKLCTD ASKYTVFSKS LVRNEEEDED VPPCGPIRIR NLEDLIRQLE
HKTTRHMSPS GSEDIRMSET EADRHYNRLD S
//
