ID W5MWI7_LEPOC Unreviewed; 1403 AA.
AC W5MWI7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Calcium dependent secretion activator {ECO:0000313|Ensembl:ENSLOCP00000012746.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012746.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012746.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01020715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000012770.1; ENSLOCP00000012746.1; ENSLOCG00000010394.1.
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00590000083094; -.
DR InParanoid; W5MWI7; -.
DR OMA; LYQCTCL; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000010394; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0045921; P:positive regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro.
DR CDD; cd01234; PH_CADPS; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR033227; CAPS.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12166; CALCIUM-DEPENDENT SECRETION ACTIVATOR; 1.
DR PANTHER; PTHR12166:SF6; CALCIUM-DEPENDENT SECRETION ACTIVATOR 1; 1.
DR Pfam; PF06292; MUN; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transport {ECO:0000256|ARBA:ARBA00022927}.
FT DOMAIN 346..464
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 487..590
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 980..1156
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 160164 MW; 161846D7283333D1 CRC64;
MLDPSSSEEE SDEIVEEESK EVMAPPAGAR LSPSRTSESS GGLQPSSRSS SVRPSSPSPS
VVSEKEKEEM EKMQKEEEER KKKLQLYVFV MRCIAYPFNA KQPTDMARRQ QKISKQQLQT
VKDRFQAFLN GETQIVADEA FINAVQSYYE VFLKSDRVAR MVQSGGFSAN DSREVFKKHI
EKRVRSLPEI DGLSKETVLS SWMAKFDAIY RGEEDPRKQQ ARMTASAASE LILSKEQLYE
MFQQILGIKK FEHQLLYNAC QLDNPDEQAA QIRRELDGRL QMADQIARER KFPKFVSKEM
ENMYIEELKS SVNLLMANLE SMPVSKGGSE FKLQKLKRSH NTSIIDMGEE NENQLSKSDV
VLSFTLEVVI MEVQGLKSLA PNRIVYCTME VEGGEKLQTD QAEASKPTWG TQGDFTTTHP
LPAVKVKLFT ESTGVLALED KELGRVVLHP TPNSPKQSEL HKMTVSKNCP DQDLKIKLAI
RMDKPQNMKH CGYLWAIGKN VWKRWKKRFF VLVQVSQYTF AMCSYREKKA EPQELLQLDG
YTVDYTDPQP GLEGGRAFFN AVKEGDTVIF ASDDEQDRIL WVQAMYRATG QSHKPVPPTQ
VQKLNAKGGN APQLDAPISQ FYADRAQKHG MDEFISANPC NFDHNSLFEM VQRLTLDHRL
NDSYSCLGWF SPGQVFVLDE YCARNGVRGC HRHLCYLNDL LERAENGAMI DPTLLHYSFA
FCASHVHGNS QKMPDLLGGL HNTEAEGDKS QSPSVVEPEG NSKKDFKKDS KKKRDSKTQQ
APEPKRPDGI GTVTVEEKER FEEIKERLRL LLENQITHFR YCFPFGRPEG ALKATLSLLE
RVLMKDIVTP VPPEEVKAVI RKCLEQAALV NYTRLSEYAK VEGKKREMYE HPVFCLASQV
MDLTIQNQKD PENVGRLVTP AKKLEDTIRL AELVIEVLQQ NEEHHAEAAV TSTGDQTGAF
AWWSDLMVEH AETFLSLFAV DMDAALEVQP PDTWDSFPLF QLLNDFLRTD YNLCNGKFHK
HLQDLFAPLV VRYVDLMESS IAQSIHRGFE RESWEPVKSL TSNLPNVNLP NVNLPKVPNL
PVNLPQMPSF STPSWMAAIY DSDNGSGTSE DLFWKLDALQ TFIRDLHWPE EEFAKHLESR
LKLMSSDMIE SCVKRTRVAF EAKLQKTSRT TDFRVPQSIC TMFNVMVDAK AQSAKLCSME
MGQEFVKEWR QYHSQIDNLI EETVKEMITL LVAKFVTILE SVLAKLSRYD EGTLFSSFLS
FTVKAASKYV DVPKPGMDVA DAYVTFVRHS QDILREKVNE EMYIERLFDQ WYTSTMNLIG
TWLTDRMDLQ LHVYQLKILI RIVKKKYRDF RLQGVLDSTL NSKMYETVRN RLTLEEATAS
VREGGGMQGI TMKDSDEEDE EDD
//
