ID A0A0V0RS74_9BILA Unreviewed; 971 AA.
AC A0A0V0RS74;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KRX17345.1};
DE Flags: Fragment;
GN Name=ADAM12 {ECO:0000313|EMBL:KRX17345.1};
GN ORFNames=T07_9437 {ECO:0000313|EMBL:KRX17345.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX17345.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX17345.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX17345.1};
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:KRX17345.1}.
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DR EMBL; JYDL01000089; KRX17345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RS74; -.
DR Proteomes; UP000054630; 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; ADAM METALLOPROTEASE; 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|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Integrin {ECO:0000313|EMBL:KRX17345.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..364
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 370..458
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 606..638
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 828..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 279..359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 319..343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 321..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 430..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 610..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 628..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX17345.1"
SQ SEQUENCE 971 AA; 105904 MW; 17B5AF25DF6F2374 CRC64;
LYTVIATYLF VETALILCHK FCSTFTQPFI MKMMRFMYKS ASFKSQEICI LYEYMKSIIY
VNKLKDKLQT CLRRNNDHQL SLSFVGVRAI RRLALQVLAS GVAYCLCVIW RVMMMREWKT
GVRMLNCYRE EWSLGSSGRN SDLEQGNMDR TNVDKPKYYY RYLNDKPLFL ELAIVFDNSM
YEKFGRDKNA LKDRASQIAT LVNSLFQPVN IRVALVGVEI WSDKDAFPVR QLGEDALSNF
VHYRQHRLLY DMPNDVAVLI TNISFQNGVV GKALQSTLCS VRSSGAVVSD HSHDVLSVAI
TVAHEIGHNF GMEHDNATCE CPLHVCIMAP MSGASHTLHW SSCSLEYLSW SLKHGSETCL
QNEPTNIING PLCGNGFLEE GEQCDCGLPH ICDNPCCNPK TCKFNADATC ADGACCDLST
CQPKRVGTVC RHARGECDLS EHCDGKSEFC PNDTYKQDGT LCKSGETHCF HGDCKTLDDQ
CKLLWGESGR PANPLCYSMN SEGNVYGNCG VSRFNDTYTV CQPQNMKCGL LQCEHKNEKT
TFGSKSTVLS GSTVLRQGSN HFSCNTAMVD LGVDSSDPGL VPGGTFCGPG KMCANQKCVT
VSSILEINRC PNECNNVGVC NNLGHCYCDV GYGGIDCTIA GPGGSIDSGP ASAPGSIFPS
TAILVFIFVA LPALFAILTY LHRRGIFKAS SVRLLKTMPM KRKASRKSKL RKVSSWVTDG
TLNRPNGVCS NNAMAPSALS LPLFGQAPAK PFHNPTQLVS SVNALKPASK AQPPPCPPPS
GRLAGERIYV EMSPERTVPL QMEMTEKRNF VPQLKEALSV LPSPGVVIPQ RRAPAPPPPL
PPQPSVTSVA NSSSFVETCI SDVAPNHGFS GSSTTNSASA CHQKSDTKQV QVQAQAMTGA
CNKNAPRPTQ APPPPPVPAK PPKAAAECVE RSYDRIAGQT ENLATSQLST LPKTQSKVTQ
LAAKFDAMTG Q
//