ID A0A0V1MQH6_9BILA Unreviewed; 968 AA.
AC A0A0V1MQH6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KRZ74065.1};
DE Flags: Fragment;
GN Name=ADAM12 {ECO:0000313|EMBL:KRZ74065.1};
GN ORFNames=T10_333 {ECO:0000313|EMBL:KRZ74065.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74065.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ74065.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74065.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRZ74065.1}.
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DR EMBL; JYDO01000055; KRZ74065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MQH6; -.
DR STRING; 268474.A0A0V1MQH6; -.
DR Proteomes; UP000054843; 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; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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; PF01421; Reprolysin; 1.
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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Integrin {ECO:0000313|EMBL:KRZ74065.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
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 TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..337
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 343..431
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 579..611
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 828..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 252..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 292..316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 294..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 403..423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 583..593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 601..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ74065.1"
SQ SEQUENCE 968 AA; 104293 MW; 5CEA141FBDF12AA7 CRC64;
LKDKFQTCLH RNNDHQLSLS FVGVRAIRRL ARQVLASGVA YCLCVICRVM IMCEWKSVRM
LNCYKEEVNI FLKSYSSSSS SSGGGGGGGK LVSISQQLNQ CMHRWSLGSS SRSSDLEQGN
MDRTNVDKPK YYYRYLNDKP LFLELAIVFD NSMYEKFGRD KNALKDRASQ IATLVNSLFQ
PMNIRVALVG VEIWSDKDAF PVRQLGEDAL SNFVHYRQHR LLYDMPNDVA VLITNISFQN
GVVGKALQST LCSVRSSGAV VSDHSHDVLS VAITVAHEIG HNFGMEHDNA TCECPLHVCI
MAPMSGASHT LHWSSCSLEY LSWSLKHGSE SCLQNEPINV INGPLCGNGF LEEGEQCDCG
LPHICDNPCC NPKTCKFNAD ATCANGACCD LTTCQPKGVG TVCRHARGEC DLTEHCDGKS
ELCPNDTYKH DGTLCRSGET HCFHGDCKTL DDQCKLLWGE SGRPANPLCY SMNSEGNVYG
NCGVNRFNDT YTVCQPQNMK CGLLQCEHKN EKTTFGSKST VLSGSTVLRQ GSNHFSCNTA
MVDLGVDSSD PGLVPGGTFC GPGKMCANQK CVTVSSVLEI NPCPNECNNA GVCNNLGHCY
CDVGYGGIDC TIAGPGGSID SGPASAPGSI FPSTAILVFI FVALPALFAI LTYLHRRGIF
KASSVRLLKT MPMKRKASRR SKLRKVSSWV TDGTLNHPNG VCNNNAMAPS ALSLPVGLPK
PPALSPPLPP QGPVKPKNVY DQDQLFGQAL AKPFSNATQP VSSVNALKQA GAQPPPCPPP
SGRLAGERIY VEMSPERTVP LQMEMTEKRN FVPQLKEALS VLPSPGVVIP QRRAPAPPPP
PSPPQPLPTS VASSSSFAEA CTSDVTPNHG FSGSSTSSVC QKSDTRQVEC KLQAMASACN
KNGTRPTQAP PPPPLPAKPK AALECVDRSY DRIAGQTENL ATSQLSTLPK SQSKVTQLAA
KFDAMTGQ
//
