ID A0A068Y1Y5_ECHMU Unreviewed; 1788 AA.
AC A0A068Y1Y5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Adam {ECO:0000313|EMBL:CDS36387.1};
GN ORFNames=EmuJ_000347500 {ECO:0000313|EMBL:CDS36387.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS36387.1};
RN [1] {ECO:0000313|EMBL:CDS36387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS36387.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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:PRU00276}.
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DR EMBL; LN902849; CDS36387.1; -; Genomic_DNA.
DR STRING; 6211.A0A068Y1Y5; -.
DR eggNOG; KOG3607; Eukaryota.
DR OMA; RQPEKGI; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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 InterPro; IPR006586; ADAM_Cys-rich.
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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1788
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009741457"
FT TRANSMEM 863..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..496
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 493..597
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 345..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..992
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1391
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 569..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 1788 AA; 194151 MW; 69987FBEB2F4699E CRC64;
MSYLAIFCVA VILCCTPLIL SITAQNTPES YLNSPSNHHS KLSSSFRIGC DCYSVPNCFT
NCSDVSGLLP QLQASSQFLQ SLPTPFCITR LEQLRKRGPK FDTSTANKRS YYSQAQFHLT
LLGHAEPIQI KIRKSSVFNG GEEYSTLFYR NRNGVVSEVE FTKSEDCFYT GEVESAPNAS
FVAVDTCSGL RGAIYYHNTT FVILPLPCPS CDPQTAPHIV LSWSSAPIAQ NASMRTFWKP
VDLMAMMQET VDQRLADLSS TVHTIWLEFI VDEKLLHQFS GKFTTTLRYV ASMVNLVNLH
FRDLPVQFHL LRTQIWNLGN LASIESSIKA TLNNFQRYRS EQSFGDKIGQ RRSRRDLDEG
ETNDPHSSSP QGVFKQPGSR KADITMLLTD SAEIDFVEKV DHLAIPGSIC TPRGTAIVRV
NVTDFELQVA TLVSKSIAEI LGIHSILCPE MYSCNENEVF SLGDISRLQL ALLSGMSACL
RSPNLQGREF LRPDTCGNGI IDRGEECEPY QQGLPIGLPH STDSGFNKSL NSPAFGCCDS
KTCLADVHAV CVEGGCCRGC RLVARGRLCR PARDQCDLPE FCSGSEAECP GDLYLENGMP
CKGEKNDFEE EALCYEGRCP TRSSHCKALW GPNARTADDY CYSTMNRNID SACGKGVVCE
EEDAMCGLLH CQNGSDEPLP VEARLLSFFN LRTQHEQQKI QCQYVASTRK FSYVPEGASC
NEGRFCFQKR CIKPTAIVVH SKCPKGPFSD LWGVSDGSND YIHPAVRGSL PTATATPINI
TCSGRGICTN GAFCLCPPRW HGPSCSQHQP SINPNASVTK PRVKVAYVSV YPDEDIASLI
WMYIQAMDKN AEGLVEPGSV NTVYLISILA AVIACVFLCL CGIIFLYRRR NFNSRGLRFG
AKSERCLSSP TNRFSPALFD SPLSKSSGTA TATTTAANSM DSMCLCNRNS RPSGASLDDM
ELHYHTLRSS CSRRHRHTAS SSSSKNRNRR QKRGGGASSG DSLQTGANGT VESGPELGRN
GEESVKDEGG NGVGKIKFGS MPSYREDKMK HAKDNATSTT ISDTAGISTI TDAVVTTTST
TNNLFQQQQP ALMDFSASWS LPPPPPPPFV VPAVCSVVAS PNPIFAGSSS PWMSTPQTPL
STSTNINTTT TTCANVICTD VGGMEVRVMS AQSSRKVMTT STISADEAET PQVTVIRENS
CRQPEKGILK NKHEGGGGVD MPDLPTSTNG EGGSKKQEHS LKRSGKKHYC SSPHFSGTTS
STSSSSTSTT GSQSLSASST GSSSSSLSSV SYCSTSRATD DTNSTNFVAS AMNSGEEEEG
GVMDMVSDSG STCSTALETG EEERKMGGRE CRHKNHRQHK SQCKKKSSHR QHSHAHSHHR
RHSHSHHRRS QRSSSTGGDT SAANTSTPPT TTTASTSSTS SPCHRRCHRR RRTGVSRRYR
FSSEDAESSI GGQNHKVPTI LCNAEQQTDE ISLARAMGAI FPTPQKDLRS PSPLKDLQNS
NSSNLQQQQQ LSSDVIDEED SEWEEVECTG GSDCEECRKN AAISWNSSAV PPTPPSAGGL
LSRQYKLPSP PPLPPVIVTS TPYYCTTQLS SQSDIDPYYQ PPIDDTDSFV AGKPGLVSHR
KYPGHAEEDD GLISSRGTQG GLTLTSSLNA PSDCYMTRDS DGLTRKTSPA VPYVSRHNYN
GSDSDFSLST SVKKSPTLGH TVDWLSSGNS SQIGGLSNHV SATVAATAHQ WLDMAESDAS
SLPDASCDLV HLAQLSHAAR MNPNLSDLAR QQERIRLGTE APFYSKQP
//
