ID A0A0V0Y203_TRIPS Unreviewed; 1175 AA.
AC A0A0V0Y203;
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 28 {ECO:0000313|EMBL:KRX94237.1};
DE Flags: Fragment;
GN Name=ADAM28 {ECO:0000313|EMBL:KRX94237.1};
GN ORFNames=T4E_8851 {ECO:0000313|EMBL:KRX94237.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94237.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX94237.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94237.1};
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:KRX94237.1}.
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DR EMBL; JYDU01000075; KRX94237.1; -; Genomic_DNA.
DR Proteomes; UP000054815; 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 Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
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 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; PS00427; DISINTEGRIN_1; 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}; Integrin {ECO:0000313|EMBL:KRX94237.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
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 841..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 311..513
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 519..607
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 749..786
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 877..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 579..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 776..785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX94237.1"
FT NON_TER 1175
FT /evidence="ECO:0000313|EMBL:KRX94237.1"
SQ SEQUENCE 1175 AA; 130315 MW; 1521E59CB97B2C6C CRC64;
LLFAVCAVSV LALGRPAFFI QARFRCESYS TFCFNFGNSC SVCSSLPASL LCPNGTKSPV
GNRVSCLASS VGLIARLTNA FQGFQTGEGR PAGRNWIFGS CRVLDAKPSD IDQAMEEFFK
MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTVHFERCS FVIKTSYGRW
RIHVQLNDVL IQPAAKYMRY LKLDSPSETS GRSLPNCYYH GQVHGHPKSK VSLSTCFGLR
GSIIMENQTF IIIPLKGGDL SRRHPHVFVR LKWDDEASCG NTDDAEWSRK RFHRRRPHRR
KLRRDVEKEV KYIELGLFID RKLHDFLNVG YREMTSYFLE AVNAVDLAFQ QLNTRVSLVY
SEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC
SARAAGMIKV ADKFQPYYLS LLMAHAIGHI SGMSHDDSEF DCTNGENFIG IMNNVVSMTS
KKNRRVYQFT ECNKHDYLEL IRSGQGRCLF NYPLQNSALT LCGNKVVDPG EFCDCGSVEE
CDLIDPCCDA VTCTLRADAQ CAEGVCCEKC KFITNRTLCR PSRDECDVPE YCSGLSGSCP
SDSYKPNGAA CGINRLGICY GGQCRQSDSE CQRIWGPNAS AADPACFKKF NTLGIDFGHC
GVNENNKPLP CTENNAMCGL LFCKGGQEIP NFSLYFKTEF TENGSVYECK VFIDNKSPVN
YSLIPDGSRC GKSEACISQN CVPLRNIYQH VDCPTTNTAL FCSGHGICTN LNICHCDAGW
TGRDCSVKLN FTFEMLSIGQ SAVSEHGSFY GDSEMPVAVS FPDTFPSGVS DVSDSSKLDT
YAMLIILGCV AIGMILMLAL LLLCYRRRAN FSKKSKTPTS EKCDFEKESN SSTETGQRSI
RFGPSRTYKC ADEVMTTNKR RTLDQIRECD ERESLSAKSR ESGNSTERVT LTMNRLPSRG
ILKNGPQSFT CERTAPEWRA LLAANRPCDN GYDSEPPYQQ SSTFGRYVGV NGSGXXXXXX
XXXVAVGPPA MMTPNSARLT RGGLYESFNS KQPRLNQTTA AIVSPYMYVR NRSLLKASPA
TLDSFSSNNG CCSPSRSRGA DLAAYAVSPA EKQLPTTRCS TSPCNSTCSS SRGATMQQPK
PLKLTNIELL LKQLDGAAVL AEPSEDQSLS SRRLS
//
