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Database: UniProt
Entry: A0A0V0U8A9_9BILA
LinkDB: A0A0V0U8A9_9BILA
Original site: A0A0V0U8A9_9BILA 
ID   A0A0V0U8A9_9BILA        Unreviewed;      1096 AA.
AC   A0A0V0U8A9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX47497.1};
GN   Name=ADAM28 {ECO:0000313|EMBL:KRX47497.1};
GN   ORFNames=T05_9701 {ECO:0000313|EMBL:KRX47497.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47497.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX47497.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX47497.1};
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
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRX47497.1}.
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DR   EMBL; JYDJ01000042; KRX47497.1; -; Genomic_DNA.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; 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   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 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   Complete proteome {ECO:0000313|Proteomes:UP000055048};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Integrin {ECO:0000313|EMBL:KRX47497.1};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    764    788       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      237    439       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      445    533       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      675    712       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DISULFID    505    525       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    702    711       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1096 AA;  122837 MW;  A4B0C20F5BA8C533 CRC64;
     MEKLISRRFV SFWESDYLKN LQFIENRSKL QQLRKHPVEC MEEFFKMDSW NKELFEHLVD
     DFEIVYPVQL RDRGRVGIDT QNYLFDNSTI HFERCSFVIK TSYGRWRIHV QLNDVLIQPA
     AKYVRYLKLD SPSETNGRSL PNCYYHGQVH GQPKSKVSLS TCFGLRGSIV MENQTFIIIP
     LKGGDLSRRH PHVFARLKWD DEASCGNTDN TEWSRKRFHR RRPHRRKLRR DVEKEVKYIE
     LGLFVDRKLH DFLNVGYREM TSYFLEAVNA VDLAFQQLNT RVSLVYFEIW TTENKIGVQR
     EILPSLMNFI QFSSYEFYNG PFDLALLLTV ADLMTSEMMS AADTVCSARA AGMIKVADKF
     QPYYLSLLMA HAIGHISGMS HDDSEFDCTN GENFIGIMNN VVSMTSKKNR RVYQFTECNK
     HDYLELIRSG QGRCLFNFPL QNNALTLCGN KVVDPGEFCD CGSVEECDSV DPCCDAVTCT
     LRADAQCAEG VCCEKCKFIT NRTLCRPSRD ECDVPEYCSG LSGNCPSDSY KPNGAACGIN
     RLGICYGGQC RQSDSECQRI WGPNASAADP ACFKKFNTLG IDFGHCGVNE NNKPLPCTEN
     NAMCGLLFCK GGQEVPNFSL YFKTEFTENG SVYECKVFID NKSPVNYSLI PDGSRCGKSE
     ACISQNCVPL RNIYQHVDCP TTNTALFCSG HGICTNLNIC HCDAGWTGHD CSVKANFTFE
     MLSIGESAFS EHGGSSFYGD SEMPVAVSFP DTFPSGDSSK LDTYAMLIIL GCVAIGMILM
     LALLLLCYRR RANFSKKTKI PTSEKCDFEK ESNSSTETGQ RSIRFGPSRT YKCADEVMTT
     NKRRTLDQIR ECDERESLSA KSRESANSAE RVTLTMNRLP SRVILKNGPQ SFTCERTAPE
     WRALLAANRP YDAGYDIEPP YQQSATVGRY VGVNGGGCWT ASDDGRCPLQ TPNSARLTRG
     GLYESFNSKQ PRLNQTTAAI VSPYMYVRNR SLLKASPAAL DSFSNANNNG CCSPSRSRGA
     DLAAYAVSPA DKQQLSQTRC STSPCNSTCS SSRGATMQQP KPLKLTNIEL LLKQLGGAAV
     LAEPSEDPTL PSRRLR
//
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