ID A0A0V0YGR7_TRIPS Unreviewed; 1756 AA.
AC A0A0V0YGR7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phorbol ester/diacylglycerol-binding protein unc-13 {ECO:0000313|EMBL:KRX99291.1};
GN Name=unc-13 {ECO:0000313|EMBL:KRX99291.1};
GN ORFNames=T4E_5965 {ECO:0000313|EMBL:KRX99291.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX99291.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX99291.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX99291.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX99291.1}.
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DR EMBL; JYDU01000015; KRX99291.1; -; Genomic_DNA.
DR Proteomes; UP000054815; Unassembled WGS sequence.
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; 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; 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 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..88
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 593..643
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 707..831
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1138..1281
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1392..1548
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1566..1693
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 198..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 291..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 199591 MW; 0B93669112F83925 CRC64;
MIFELNFLDE VHSYVTLKLQ NVKSTTVAVK GSEPCWEQEF IFETERLDLG LIFELWSQGV
LWDKLMGVYF MPLTSVHYSN VAGTGKWLQL FSEVETKNGE VVGHRGQTSH LLLADVRFEL
PLEFNDEEAQ ILQQKLEALN RMDEEISTAQ LQMKRAQFNR SGISEDSDYT SDISFPVHLN
NSSAHQFGSH LRTCCKSTDN AEQPSSVRMS LEDERDYATS SNKNAEEQSS FEYQYYDEQH
LGEPQSPSSV SRVNYNSTDV HDNSCHANDK PNNFDSKNCH PEVNTAAKRR ANLRASKERT
YSSEHEVSDH MSPCSDSEPL FYNSRPNDRH RSKKATVWDD DFFVDKPCNL SHGIYSDSFG
DSICRNSISR KGSNSSSMSS QQNFGTLLKS KCSDSHPMVS PQTSLESAST HTVKTGFGSK
DESSVLKQQP CDGLVNTASS LINSTVEQST SVRPFDSVTN DTSASKPSED TCLQALNGSE
INIPSVNQEM SNAKKRWVTA FRRICEQLGP KESFLESSPK TYDFYTSIDA MPNIALLKKK
SVPLVSELTM ATKRAQAGLA SAACTTFGNE ELKMRVYRKT LQALIYPISV STPHNFQVWT
ATSPTYCYEC EGLLWGLARQ GLRCSECGVK CHEKCKDLLS ADCLQRAAEK SSKHSGSGDR
AQSIISAMKD RMKIQERNKA EVFEYIRHLH FAYRRVFDVD KKMHHEAMKQ VKQCILEGTA
KWSAKIAITV ICAQGLSAKD KTGKSDPYVT VQVGKVKKRT RTIHQELNPF WSEKFYFECH
NSTDRVKVRV WDEDNDLKSK LRQKLTRESD DFLGQTIIEV RTLSGEMDVW YNLEKRTDKS
AVSGAIRLQI NVEIKGEEKV APYHDQYTCL HEHIFNYYCS KEMGQLKLPD ARGDESWKVY
FDEIGQEIVD EFAMRYGIES IYQAMIHFAC LCTKYMCQGV PAVISTLLAN INAYYAHTTA
TSAVSASDRF AASNFGKDRF VKLLDQLHNS LRIDISMYRN NFPASNAGKL QDLKSTVDLL
TSITFFRMKV LELTSPPRAS TVVRECATAC IKSTYQFLFE NCYELFQREF EGNQALTTNP
ELVGPSTDSV EFWHKMIALM ISVIEEDRNI YTPVLNQFPQ ELNIGQLSAA TMWSQYTIDL
KLALEEHSEQ RKCKSSDYMN LYFKVKWFYN NYVSDIPPYK GTIPEFPVWF IPFVMQWLNE
NDEISMDFLR GAFERDKKDN YPQSSEHTLF SNSVVDVFTQ LNQGLDVLRK MDCPDPDVYG
DMMKRFSKTV NKVLLAYADM VQKDFSRYVG NEKLVKFHLK QACILMNNVQ QLRVQLEKMY
ESMGGAMLDQ DAQQVLKGLQ SKLNNVLEGL THVFAASLES NIYDSTVKLG NLLMRVKGGG
QVQKSQVTAE ADLILEPLMD LLDVSLTQYA QQCEKTVLKK LLKELWRITI SCMEKLVVLP
VFPDRNLLKQ LPNAKIGDMS KLLSNHLKEV KNISSVKEVM DLARESDRSL TPKQCTVLDA
SLDTVKSYFH AGGSGLKKSF LEKSAEYQSL KYALSLYTQT TDQLIKTFIA LQKEQGQYDS
PSQEEPVGEV SVQVDLFTHP GTGEHKVTVK ILAANDLRWQ TTGVFRPFIE VHIVGPNQAD
KKRKFATKTK TNNWAPKFNE VFYFILGNED ELENYELIFQ AKDYCFARED RLIGVGVLQL
RSFAEHGSCA CWVQLGRRQY IDDTGLILLR ILSQRHYDEI AKQFVKLKTE SRYESELHTT
GSSFQLDKLS ANSTAG
//
