ID E3LW70_CAERE Unreviewed; 1053 AA.
AC E3LW70;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=CRE-UNC-71 protein {ECO:0000313|EMBL:EFO83641.1};
GN Name=Cre-unc-71 {ECO:0000313|EMBL:EFO83641.1};
GN ORFNames=CRE_02845 {ECO:0000313|EMBL:EFO83641.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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}.
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DR EMBL; DS268417; EFO83641.1; -; Genomic_DNA.
DR RefSeq; XP_003111780.1; XM_003111732.1.
DR AlphaFoldDB; E3LW70; -.
DR STRING; 31234.E3LW70; -.
DR EnsemblMetazoa; CRE02845.1; CRE02845.1; WBGene00063439.
DR GeneID; 9811110; -.
DR KEGG; crq:GCK72_010958; -.
DR CTD; 9811110; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_291906_0_0_1; -.
DR InParanoid; E3LW70; -.
DR OMA; VNNRMTP; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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 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; IPR013111; EGF_extracell.
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:SF248; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN UNC-71; 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.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 745..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 233..433
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 439..526
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 663..700
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 183..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 498..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 690..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1053 AA; 116611 MW; ABDBEC48D00F35E1 CRC64;
MFSVDIRQTT ANKAFMETMS PDGYEVVHPF QIRDKNERIG IDTRNYFLKA QEHYSHVTIV
IRSNQLGRLK LVLERNNFIF LNQTAFHKLD ADGERVLQNR VENCYYQGTV GGEESSFVAL
SSCNGLRGVI SFANGTTYGI WPLDGGDRNS RRHPHILYKS EWTKEAKCGS SMAHAVGQRI
RRGAEPDLEG AEPKQKKHKH RKHHRRHMKD EEEEEDELKI RVANRRDASK RTKYVEVALI
ADYEFMKQRG LHDMDAISYM LESLNIADSM LSRDLNIRLS AVYVELWSDV QRIDLWEDIE
RTLSGVVDYA AGHIYHIQKD ASILFTAGSF ANQEVSNAAI RSICTARSAV IVRAIEPFAT
HWNGELVAQS VGHLLGLEHD TTACSCEPSP ECVMRQQPGR VGAPFSWQFS KCSVARMHGI
WQDGNIQCLL NKPFQVSELR ECGNGIVDGS EECDCGTREN CNDPCCDPLT CTLRPHAQCA
AHHKCCHRCE LRKAGETCRS SQSPCDVAES CDGKSGDCPP DGHLIDGTVC GNDGQCWRGN
CSDSHQQCQK LWGREARVAE EVCFEQNTKG AEYANCGMQS DGSYHPCQLE DTKCGTLHCH
SGSLTPTDST LKAFTFHFTQ NAQQIQCKSI AGSLSGLIQD GTNCGSGKVC VAGSCVEMSS
VSSGTACPTN NLALLCSGHG HCTTTAKCVC FNGWTGNACD IRSNTSTYQG SMGFRDEDHE
QMGHGGARKT IMIPHLNIGT TLETAYLFGI LFGFGAFLLL CLVCLMLCYR RRSVVEIPKP
SDEKLEESPD RQIKFGNMPS YREEKRKRKS SKRIYGALNR ITEADERDST SLRSRDSAGS
QQLLDRNGQP VMAGIRDPYS TDHHIYAESV AASSSNRQFR GINSDGSYPL RSFGSWRSSA
PISPASSSGH LTDVSNATTP LRLNKIGKLL KTMQQSDDEA GSPFSDHSMQ FQNHQGIQNL
QSLQNLQNHS LLGRLDHGYT GEEELSAVEA DHDVGSNTES SRGCEDSSGG RDSGGWDPPS
LVNGSTSNNY NFRQSPSLFS DPFKLEMTNS MHN
//
