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Database: UniProt
Entry: A0A0V0RS74_9BILA
LinkDB: A0A0V0RS74_9BILA
Original site: A0A0V0RS74_9BILA 
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
//
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