CTX_SEPES
ID CTX_SEPES Reviewed; 1052 AA.
AC B2DCR8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=SE-cephalotoxin;
DE Short=SE-ctx;
DE Flags: Precursor;
OS Sepia esculenta (Golden cuttlefish) (Diphtherosepion dabryi).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX NCBI_TaxID=31210;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-52; 941-947; 334-345 AND
RP 347-381, SUBUNIT, GLYCOSYLATION AT ASN-41 AND ASN-353, AND TOXIC DOSE.
RC TISSUE=Posterior salivary gland;
RX PubMed=18694775; DOI=10.1016/j.toxicon.2008.07.007;
RA Ueda A., Nagai H., Ishida M., Nagashima Y., Shiomi K.;
RT "Purification and molecular cloning of SE-cephalotoxin, a novel
RT proteinaceous toxin from the posterior salivary gland of cuttlefish Sepia
RT esculenta.";
RL Toxicon 52:574-581(2008).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18694775}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the salivary gland.
CC -!- TOXIC DOSE: LD(50) is 2 ug/kg against crabs.
CC {ECO:0000269|PubMed:18694775}.
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DR EMBL; AB363989; BAG24412.1; -; mRNA.
DR AlphaFoldDB; B2DCR8; -.
DR iPTMnet; B2DCR8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR039051; SE-CTX-like.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR40472; PTHR40472; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Secreted; Signal; Sushi; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..29
FT /evidence="ECO:0000269|PubMed:18694775"
FT /id="PRO_0000359437"
FT CHAIN 30..1052
FT /note="SE-cephalotoxin"
FT /id="PRO_0000359438"
FT DOMAIN 460..497
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 709..769
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 768..821
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 819..859
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT COILED 130..194
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18694775"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18694775"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 464..474
FT /evidence="ECO:0000250"
FT DISULFID 468..485
FT /evidence="ECO:0000250"
FT DISULFID 487..496
FT /evidence="ECO:0000250"
FT DISULFID 711..752
FT /evidence="ECO:0000250"
FT DISULFID 739..767
FT /evidence="ECO:0000250"
FT DISULFID 780..814
FT /evidence="ECO:0000250"
FT DISULFID 784..820
FT /evidence="ECO:0000250"
FT DISULFID 795..804
FT /evidence="ECO:0000250"
FT DISULFID 829..847
FT /evidence="ECO:0000250"
FT DISULFID 841..858
FT /evidence="ECO:0000250"
SQ SEQUENCE 1052 AA; 120495 MW; 86E4400BF7EA24D5 CRC64;
MMGTSRCVIL LFALLLWAAN AAPPEIHTTR PNVPEEIKRP NSTEIETPAV KQLETPSIFL
LTTLEVAEAD VDSTLETMKD RNKKNSAKLS KIGNNMKSLL SVFSVFGGFL SLLSVVTTTS
DLQVISDMFT GVNRKLDQIN DKLDKLDNSV ELQGLLTNYI PWQYSVKNGI EKLIETYKKM
VEETDMNKRR LMAENFILFF ENNQIESNIN NLIKLTTTTD AVHQNMLFNE LLDEAGCDII
RLTRIYMHVR RIFYQGTQLV LAYNSFKQMD PPEMKKYLNA LIFIRNMYQS RVWHCKETTI
AQSKKDIKDI VKTNAKFGIT TVLRKINSEL SRKYPWYSWS IVTVKKMLAN QRNSTLGNQF
YEMEAVGPHG SNFVVIWQGF KEHSQCEDIQ KANTIAVLTI CKSCHQSHVF TPSNMLNKNT
CPNNQYPQVK AFIDRREPFR DEIQRKKSDV FWVAAGFKAP GNPCNHGCNG HGECKVVPYT
DQFQCFCHGN YEGKMCQKKI QMKRDISKLI SDLQTGYKNA FNVPSLTNIL IQGENLAKQL
KKMIQRIDNQ FELTHILVKY ISDLQKLDYI LKISFNYSKK KITVDAFSRR MKAFLSLNPV
DFIFQQLSNA ILAEGFTDIQ GKDFFNTFKR MIASNRDACT APYGNEATIL LERLSRLDLT
AAESILAYYS FESNYLNPAN MKRMLENAKQ LVRDSKRRMR SYARYWERTS CPPLNVTHLT
QTGCGALLSF EGMKVKLSCD GGRAAVPQNI ECVNVNGNLQ WSATPKCESS WSRWSKWSAC
ASTCGNATQS RRRRCLGQSE SEKCIGPSKQ VRKCFVEDCC QEKYGKFKCD NNKCISLSRV
CDGNDDCRNA EDESKSRCKY LRSGDRIALR NMAYSQEWLS VQYTDAVQAD LYYGRAYLNH
CIKGDHVTSS EWNSCAGQSL LIYGNYENGK IGKAIRFGDK IAMYYRKTNY HYRWFICYPT
YCMTYTCPKK AGSFTFGPNG GCDEYEFYII NYNDKLSRDP VKPGDVITLA NNRGSVKGNG
YNRNININDC TVKRAQDDRI ECNANAWQIF IK