ID A0A1D2NK55_ORCCI Unreviewed; 1343 AA.
AC A0A1D2NK55;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN ORFNames=Ocin01_01317 {ECO:0000313|EMBL:ODN05356.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN05356.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN05356.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05356.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN05356.1}.
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DR EMBL; LJIJ01000024; ODN05356.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2NK55; -.
DR OMA; WIDTHWY; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000094527; 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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
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:ODN05356.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..492
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 506..602
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 202..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 1343 AA; 147430 MW; 171E8AAEC5C3B1C9 CRC64;
MWSTFAKFFI LILYYSGTCL VILTVLSPHL LSNGSATEEV ASGGESPALR YFEPVFYSPS
EFISQHRRKK REIRNSESLR LNIASQSRNF RLNLIEDDSV FHPDAVIENS DGPIQYDTSR
VLVGHLDDEP GSLAHGVVSE DGFFDGTIST SCGSEYYVEP TKRYSLLNAN ASQGIIYEKG
AIEWPEEPPV CASHELHIKR REERMSSTAS TLDPDVRFNS KSNRSDFQHH HHDHHHQHHQ
SLASINKASF SFPTSKPHKR SKRYIVDPRK RACTLYLQAD YLFYRHFGSE EAAINMMARH
IQRVNEIYRT TDFDGDGVPD DISFMIKRIK VHTKNHTLDS SYRYNGEFQV IKFLELFSEG
DYDQFCLAYM FTFRDFEGGT LGLAWTGDLK NAGGVCERKG HFRGGLKSLN TGIITLLNYG
KIVLPAVSFV TLAHEIGHNF GSPHDPEGDK ECTPGGREGN YIMYARATAG DQKNNNRFSP
CSLRSIIPVL NSKARGTHGC FVEPQQAICG NREVEDGEEC DCGWEEDCAE PCCWPMKLRP
VRGEKPCTLK YGKDCSPSQG PCCTANCTLK IGDKCRDDNG CRHSAFCDGY MPNCPSSVHK
PNKTICHEEQ SVCFMGECTG SICLAYGLES CQCTPEPWES TSKYCELCCK LPGEGQPCLS
SYQWNEPPFD VPNLYSKPGS PCKNYTGYCD AYHVCREVDP SGPLATLRNL LLADEGLTAI
ADWIDTHWYA VLCFFVLLIL MMVLTAKLCG KRAKQRLRKI TVMHSNVEAI QIERSYWDEQ
GEHVVHPMAV RKKIPIRKKV REKNKTKKRS GSSKNKGDRP GKGVTGTLFK RKGRGERSKV
NSNHFANSSS SKTENGELPS NLNGDVQSPT SPIQSFNLVN LQANGGEGAC MPPPTGGVPI
YPHYMMPDSS TTNGIVGNSK IYNHNSCNNN IPSPGSSSSS GGFRTAQSPR SPITPGDNIN
DPLCAALVNH EPKTVILPAA GVRRKRSKHP DKKEKKSKQG KSQRSPSKRE SSKSASGKNH
SHHQPHHPSL QESGGITKRR SVKASTKEQK AAGDAVKPKK RIQVVFTPPF SLRVVQVVAG
GGERESHGKS SGNKSSSKQG GGTSASQPTT KHNSGSNNAI NSSSSNNANH ISNIVKKSES
EVPNKSAAAA NPISGERANN NISSVKNDLN SCGGGGVKHK LNGANDTQLS ASQMKQSCES
NNANPISPNK VSNKSANHQK SNKSGKVIKT KISGGGSPDS DNKNVDTGPG SKKESESKII
ENLTCSNENE GDGIKGKMGG ENKESNKNSQ GHIKAKVKSS GSFLQRRKQN LKARAGEKSE
LRVLIPPCNQ DEDDINSPIT PMS
//
