ID F1KQ46_ASCSU Unreviewed; 1828 AA.
AC F1KQ46;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phorbol ester/diacylglycerol-binding protein unc-13 {ECO:0000313|EMBL:ADY40000.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40000.1};
RN [1] {ECO:0000313|EMBL:ADY40000.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JI164064; ADY40000.1; -; mRNA.
DR GO; GO:0098793; C:presynapse; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR CDD; cd08394; C2A_Munc13; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR CDD; cd08395; C2C_Munc13; 1.
DR Gene3D; 1.10.357.50; -; 1.
DR Gene3D; 1.20.58.1100; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR PANTHER; PTHR10480; PROTEIN UNC-13 HOMOLOG; 1.
DR PANTHER; PTHR10480:SF12; UNC-13, ISOFORM E; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 3.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..106
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 705..755
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 811..935
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1224..1367
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1470..1626
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1641..1768
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 168..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..167
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 179..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1828 AA; 209171 MW; 36F9FE5D535C5B04 CRC64;
MFERRNCSSM ITVNVSVKKA RLQGSQDEFH SYVVVKLQNV KSTTVAVKGN QPCWEQEFIF
ETNRLDNGMM LELWNKGVLW DKLIGVHYIP LTSVQYSSAP GSGKWLQVDQ ELETRNGHTV
GTSRPTGHSL LVDVRFELPF DAQGSDAEEL QAKLQALNQL IEVNDQLPHP RAPFTHSGIS
EDSDYTSDVS FPIHHQPNSS VHQWDSHLHP NRHSRQYDHM PQQFDRTLQA SYEDEEDAYH
QRYYDGESDA TQRAADDNND AYGYNENEHD YASESRSSSR GHEQYSRNTL RQYEPMHEHG
YTTDTYDEFE NRSSSRQQQD SDASHTSTAY ARRKRCKIFS YDSEYYQPVS YDTDAHVDEY
YHAGTSYDHY DGRHYHEDRF CERPDWDQQN SDWTEEQEPL SYNSRPQPPH PIVSPSTSRH
FRDEDDEQTW PATTQQDNQS SVTSHYDVPP SESERDTYSH GEHGDTYAAE SDETHFISDS
HVSSSNQSTL LVNGSVGGGY LKRHDVQQQQ IQRNESLEKR PTESLGNADI LPPPTTAHQL
KDEDMTLGTP TSSAAESFEC RQSQPQQQQQ KRDERPLDNK PESTTTTMNN AEVAVSEKRN
YREMWHWAYK ETCKELGIKS TFFDAGATDS ASSAFYKSID AMPNMNVSRT KKTIPLVSEL
TMLTKRAQAG LANAAKTTFG DEELKMHVYR KTLQALIYPI SCTTPHNFVM TNFQTPTWCY
ECEGLLWGLA RQGLKCTECG VKVHDKCREL LSADCLQRAA EKSSKHGEGD RAQNLIAVIR
DRMKIQERNK PEIFETIRTI FNIDERTQQE TLKQVKTSIL EGSSKWSAKI ALTVRCAQGL
IAKDKTGKSD PYVTAQVGKV KKRTRTIHQE LNPVWNEQFF FECHNSTDRV KVRVWDEDND
LKSKLRQKLT RESDDFLGQA IIEVRTLSGE MDVWYNLEKR TDKSAVSGAI RLQISVEIKG
EEKLAPYHIQ YTCLHEHLFQ HHCTEQDEVR LPEAKGDDSW KVYFDDTGQE IVDEFAMRYG
IESIYQAMTH FACLCTRYMC PRVPAVLSTL LANINAYYAH TTATSAVSAS DRFSASNFGK
DRFVKLLDQL HNSIRIDLSM YRKYFPSSSR EKLADLKSTV DLLTSITFFR MKVLELASPP
RASNVVRECA KACMQATYQL MFESCCEDGG PSADSVKFWF DFLDYMMRVI EDDKHIYTPV
LNQFPQELNI GNLSAATLWQ LYKTDLQMAL EEHAASKKCS TPEYMNLYFK VKGFYFKYVA
DMPQYKASIP EFPAWFIPFV MDWLNENDEH SMDILRNAYN RDKSDNFPQT SEHTKFSNSV
VDVFTQLNEA LKLLKQMDCP NPEVYADMMK RFSKTLNKVL LAYADMVQKD FGKFVSNEKL
ACILMNNVQQ LRVQLEKIYE NMGGTSLDSA ANTVLTNLQK KLNTVLDKLA GQFAESLIPK
IHEQMNTLGS ILCKIKGPQL QKSQLVGEVD AVLEPLMELL EDKLQQYASE CEKTVLKYLL
KELWKITITS MEKIVVLPPL DNKALLKQLP NAKIGDVTKL MSTHLKDVKS MSSVKEMMDM
ARECERSLTP KQCTVLDAAL DAIKECFHAG GQGLKKSFFE KSPELQSLKY ALSLYTQTTE
QLIKTFIATQ KQQDLPSQEQ PVGEVSVQVD LFSHPGTGEQ KVTVKILAAN DLRWQTASVF
KPFVEVHLVG PHLADKKRKM ATKSKAGNWA PKFNETFHFF LGNEGEPEHY ELMFQVKDYC
FAREDRIVGV GVLQLANVVE QGSCACWVQL GRRFHIDETG LILLRILSQR QTDEIAREFV
RLKSECRFET ESTLAASVSS QQITSRLT
//
