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Database: UniProt
Entry: G3PMN7_GASAC
LinkDB: G3PMN7_GASAC
Original site: G3PMN7_GASAC 
ID   G3PMN7_GASAC            Unreviewed;      1606 AA.
AC   G3PMN7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Unc-13 homolog Ba (C. elegans) {ECO:0000313|Ensembl:ENSGACP00000018868.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018868.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000018868.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000018868.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 69293.ENSGACP00000018868; -.
DR   Ensembl; ENSGACT00000018906.1; ENSGACP00000018868.1; ENSGACG00000014286.1.
DR   eggNOG; KOG1011; Eukaryota.
DR   GeneTree; ENSGT00940000165775; -.
DR   InParanoid; G3PMN7; -.
DR   OMA; HERHKLC; -.
DR   TreeFam; TF312844; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000014286; Expressed in camera-type eye and 2 other cell types or tissues.
DR   GO; GO:0098793; C:presynapse; IEA:UniProt.
DR   GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   CDD; cd08394; C2A_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   PANTHER; PTHR10480; PROTEIN UNC-13 HOMOLOG; 1.
DR   PANTHER; PTHR10480:SF14; PROTEIN UNC-13 HOMOLOG B-LIKE; 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   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..97
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          488..538
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          594..719
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1022..1165
FT                   /note="MHD1"
FT                   /evidence="ECO:0000259|PROSITE:PS51258"
FT   DOMAIN          1267..1405
FT                   /note="MHD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51259"
FT   DOMAIN          1438..1561
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          191..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1606 AA;  182732 MW;  44AC5284B2617869 CRC64;
     VFSLCLPVKK AKLHGPPDKF NAYVTLKVQN VKSTTVTVRG DQPCWEQDFM FEINHLESGL
     VVELWNKGLI WDTMIGTALI PLDSIGQSDE EGPGHWTSLD SEVLMREDEI CGTSNPTPHQ
     VLLDTRFELP FDIPEDEAQY WSGKLDRINT MRIHDEYPLQ EEVRRGRMAS VPSQCCSWSY
     FGWNDQQTLD DHDSAVDDRD SDYRSETGSR PPRFHNTPQT NSSVHQYPVG RRAQHPTPSG
     EADSIRSYEL DYREIRRPSR QSKKAHLLEA MNPSKSLKTN PLGLERAQKQ NDSHQETKTS
     YSAHESIDLS NRGESPERQN PLLVTYLDAE EEAGEQQVEK EQNAPPEPGS NKDLKDSLVI
     SPQPTETKVC FFEDGPPPCS PSKVRWLKAY NKVRVRLLES RDQGGDPSKH PWAKPGRGNT
     PFGIDSMPDL RKRRPIPLVS ELSMIQTRKA GLAHTLSTRT SLKDEELKNH VYKKTLQSLI
     YPISCTTPHN FEVWTATTPT YCHECEGLLW GIARQGMRCA ECGVKVHEKC QELLNADCLQ
     RAAEKSSKTG AEDRTQHIIM AMKDRMKIRE RNKPEIFEEI RKVFNAPRVI HVQHMKTVKQ
     SVLDGTSKWS AKIAINAVVS AQGLQAKDRT GSSDPYVTIQ VGKTKKRTKT IYGNLNPVWE
     EKFSFECHNS SDRIKLRVWD EDDDIKSRVK QRLKRESDDF LGQSIIEVRT LSGEMDVWYN
     LDVVDKSAVS GAIRLQISVE IEGEEKVAPY HVQYTCLHEN MFHFSTDVEG GGVVKIPAAH
     GDDAWKVYYD EVKQDIVDEF AMRYGIESIY QAMTHFSCLS SKYMLSGVPA VMSTLLANIN
     AFYAHPTAST NVSAPARFAA SNFGRDRFVK LLDQLHNSLR IDLSMYRNNF PASSKPRLHD
     LKSTVDLLTS ITFFRMKVWE LQSPPRAAHV VDCFKPRLTS PYEFFNTCLE LFNRQFPTRR
     STEQEEQGPS IQNLDFWPKL ITLMVSIIEE DKNSYTPIIN QFPQELDVGK VSTEVMWRLF
     AQDMKYALTE HEKHKLCKTA DYMNLHFKVK WLYNEYVKDL PTFTDAVPEY PAWFLPFVLA
     WLAENEDVSM EFMHGALERD KREGFQQTSE HALFSSSVVD IFTQLNQSFE IIKKLDCPDP
     AVVAQYNRRF AKIFNLHLTL FLCSLSLSFK TESKKEKLPC MFRRNRAQLP RLRTRRFAAS
     HVRELDTEAA DILNELQVKL NTHLDNFSIV FAKSFQARIN SCMRQMAEIL YQIKGPPNHS
     TAEADADNML RPLMEFLDGN LSIFADICEK TVLKRILKDL WKTVLSSLEK SIVLPQSNDS
     LGAQLLTAAK GLSNLKSLQG GGEAKTLTPK QCIIIDAGLE TIKQYFHAGG NGLKKTFVEK
     SPELASLRYA LSLYSQSTDA LIKTFVTTQH SQVHDGMGIR ITGSEKIRPD RGPGVEKPIG
     EAVLQIDMML GKERKVSVRV IAVNDMKWQT SGMFRPFVDV SMVGPFLADK KRKFTTKSKN
     NSWSAKFNEA FQFVLGKESP DCYELQVTVK DYCFGRADRV VGVAVLQLRD VADRKSCVCW
     CPLGPRVHTD ETGLTVMRIL SQRPADEVAK EVVRLKAETR PAEEGR
//
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