ID E3NPV1_CAERE Unreviewed; 941 AA.
AC E3NPV1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFO83337.1};
GN ORFNames=CRE_12410 {ECO:0000313|EMBL:EFO83337.1};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; DS269423; EFO83337.1; -; Genomic_DNA.
DR RefSeq; XP_003089569.1; XM_003089521.1.
DR AlphaFoldDB; E3NPV1; -.
DR STRING; 31234.E3NPV1; -.
DR MEROPS; S01.B69; -.
DR EnsemblMetazoa; CRE12410.1; CRE12410.1; WBGene00073665.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_315286_0_0_1; -.
DR InParanoid; E3NPV1; -.
DR OMA; GPYLNND; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF10; SERINE PROTEASE 56; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 206..278
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 329..409
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 574..692
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 689..937
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 224..263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 314..329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 542..560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 554..569
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 941 AA; 104550 MW; 59B0740C38C23694 CRC64;
MKNSRIFDDI LEVRSQNGLF FPLCSKSFHQ KYGEQACSLT SSTFSSHSIV PLQQYTYSIG
CTSSVCFTFL SAFCKTGIKV FCSSSLCSPG TLQLGNKCIS ISTVPVQGYS EAKDYCSPFS
LISSLKPSEI ESIRDTILPF SLTDSRLFFT SGLRQGSTWK WANGDTVEQE ISGNGRCLSY
QSGSLVASDC DSEGYVFCES GRECIGKNRE YSGTSNKTSN GINCLMWNDP SVLFQRDVEL
EILNHNFCRF IEQDGKKSAT PVCYTKPNQL SECNIPNCPE SLNDAIQLES GDSCTIGSFS
CDNGSKCISE KFQCDYEMDC IDGTDEQNCE DYLQYYELIG AYRLIENIIE VWTFIPHVQG
CARKCRESLL MCEAFSYEPK TQTCLLTDTS QTYSSLARKT TSLYYRRRFS SKDVLFEVDN
KTLYATKLSK KGRVCNENFS REKLSSICRI LGFGDPIYVE GSLQSELSLV RLPHSLPSSD
SLSSVSQAAV SSITALRLPA WNLNCLREPN CTSTIISTCQ PIRILKFTLN RYRCSQCQEA
ACSDGSCIRF RQLCDGNVDC ESGDDEGDCA AKSFRLTNGT DTRGYLEVLF RAKWEPLCAD
HIDEKRANSV CYSMRLGERG SVLYTNSSLL SGFDVICDPD CILRRSTSCT RHARISCTSE
NGVSSISQCG LRYVEVNARD AARSRIARVV GGFETIPGAF PWTAALRNKA TKAHHCGASV
LDKTHLITAA HCFEEDERVS SYEIVVGEWD NNRTDGHEQV FDLQRIHYYP LYKGNRNSIN
LAFSLFSDIF SHDIAILEIP YPGIEFNEYV QPICLPSKDF VYTPGRQCVV SGWGSMGLHY
AQRLQAALIP IIDRFDCVNS SQIYTSMSRS AFCAGYLEGG IDSCQGDSGG PFACRREDGA
FVLAGVISWG DGCAQKKQPG IYTMVAPYLS WINAIVNGEN V
//
