ID A0A0V0Y270_TRIPS Unreviewed; 1192 AA.
AC A0A0V0Y270;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KRX94235.1};
DE Flags: Fragment;
GN Name=ADAM28 {ECO:0000313|EMBL:KRX94235.1};
GN ORFNames=T4E_8851 {ECO:0000313|EMBL:KRX94235.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94235.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX94235.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94235.1};
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:KRX94235.1}.
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DR EMBL; JYDU01000075; KRX94235.1; -; Genomic_DNA.
DR STRING; 6337.A0A0V0Y270; -.
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 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:KRX94235.1};
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 858..882
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..596
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 766..803
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 894..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..908
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 793..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX94235.1"
FT NON_TER 1192
FT /evidence="ECO:0000313|EMBL:KRX94235.1"
SQ SEQUENCE 1192 AA; 132155 MW; 86CBF0BF5269EDDC 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 YCSGLSGSVS
LLCGFNELEL FGGLFCPSDS YKPNGAACGI NRLGICYGGQ CRQSDSECQR IWGPNASAAD
PACFKKFNTL GIDFGHCGVN ENNKPLPCTE NNAMCGLLFC KGGQEIPNFS LYFKTEFTEN
GSVYECKVFI DNKSPVNYSL IPDGSRCGKS EACISQNCVP LRNIYQHVDC PTTNTALFCS
GHGICTNLNI CHCDAGWTGR DCSVKLNFTF EMLSIGQSAV SEHGSFYGDS EMPVAVSFPD
TFPSGVSDVS DSSKLDTYAM LIILGCVAIG MILMLALLLL CYRRRANFSK KSKTPTSEKC
DFEKESNSST ETGQRSIRFG PSRTYKCADE VMTTNKRRTL DQIRECDERE SLSAKSRESG
NSTERVTLTM NRLPSRGILK NGPQSFTCER TAPEWRALLA ANRPCDNGYD SEPPYQQSST
FGRYVGVNGS GXXXXXXXXX VAVGPPAMMT PNSARLTRGG LYESFNSKQP RLNQTTAAIV
SPYMYVRNRS LLKASPATLD SFSSNNGCCS PSRSRGADLA AYAVSPAEKQ LPTTRCSTSP
CNSTCSSSRG ATMQQPKPLK LTNIELLLKQ LDGAAVLAEP SEDQSLSSRR LS
//
