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Database: UniProt
Entry: I3NGC0_ICTTR
LinkDB: I3NGC0_ICTTR
Original site: I3NGC0_ICTTR 
ID   I3NGC0_ICTTR            Unreviewed;      1696 AA.
AC   I3NGC0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Unc-13 homolog A {ECO:0000313|Ensembl:ENSSTOP00000023417.2};
GN   Name=UNC13A {ECO:0000313|Ensembl:ENSSTOP00000023417.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000023417.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000023417.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AGTP01071336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01071337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01071338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01071339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01071340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSSTOT00000027458.2; ENSSTOP00000023417.2; ENSSTOG00000026062.2.
DR   eggNOG; KOG1011; Eukaryota.
DR   GeneTree; ENSGT00940000161905; -.
DR   HOGENOM; CLU_018378_0_0_1; -.
DR   Proteomes; UP000005215; 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:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:UniProt.
DR   CDD; cd20859; C1_Munc13-2-like; 1.
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; 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:SF1; PROTEIN UNC-13 HOMOLOG A; 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:UP000005215};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..97
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          554..604
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          660..784
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1094..1237
FT                   /note="MHD1"
FT                   /evidence="ECO:0000259|PROSITE:PS51258"
FT   DOMAIN          1346..1504
FT                   /note="MHD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51259"
FT   DOMAIN          1518..1645
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          185..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..367
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1696 AA;  192387 MW;  A292DA1661265F72 CRC64;
     PSLSLSTVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL
     TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQVIMADSEI CGTKDPTFHR
     ILLDTRFELP LDIPEEEARY WAKKLEQLNT LRDQDEYSFH DEQDKPLPVP SSQCCNWNYF
     GWGEQNDDPD SAVDDRDSDY RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD
     SMHSYEEFSE ARVLSPTGSS HYASSGELSQ GSSQLSEDFD PDEQSLQGSE LEDERDRDSY
     HSCHSSVSYH KDSPRWDQDE EDLEEDLEED LEEDLEEDLE DEELPEEEEE EEEEEEEVEE
     EEEVYVQQES VAAEPKDFKR LSHPPAAPEK EDKAPTLPTE APDVPKATSK PPTPEEVPGA
     PEPEPPKAEE SFRPREDEEG QEGQDSMSRA KANWLRAFNK VRMQLQEARG EGEMSKSLWF
     KGGPGGGLII IDSMPDIRKR KPIPLVSDLS LVQSRKAGIT SALASSTLNN EELKNHVYKK
     TLQALIYPIS CTTPHNFEVW TATTPTYCYE CEGLLWGIAR QGMRCTECGV KCHEKCQDLL
     NADCLQRAAE KSSKHGAEDR TQNIIMVLKD RMKIRERNKP EIFELIQEIF AVTKTAHTQQ
     MKAVKQSVLD GTSKWSAKIS ITVVCAQGLQ AKDKTGSSDP YVTVQVGKTK KRTKTIYGNL
     NPVWEENFHF ECHNSSDRIK VRVWDEDDDI KSRVKQRFKR ESDDFLGQTI IEVRTLSGEM
     DVWYNLDKRT DKSAVSGAIR LHISVEIKGE EKVAPYHVQY TCLHENLFHF VTDVQNNGVV
     KIPDAKGDDA WKVYYDETAQ EIVDEFAMRY GVESIYQAMT HFACLSSKYM CPGVPAVMST
     LLANINAYYA HTTASTNVSA SDRFAASNFG KERFVKLLDQ LHNSLRIDLS MYRNNFPASS
     PERLQDLKST VDLLTSITFF RMKVQELQSP PRASQVVKDC VKACLNSTYE YIFNNCHELY
     SREYQTDPAK KGEVPPEEQG PSIKNLDFWS KLITLIVSII EEDKNSYTPC LNQFPQELNV
     GKISAEVMWN LFAQDMKYAM DEHDKHRLCK SADYMNLHFK VKWLYNEYVA ELPAFKDRVP
     EYPAWFEPFV IQWLDENEEV SRDFLHGALE RDKKDGFQQT SEHALFSCSV VDVFSQLNQS
     FEIIKKLECP DPQIVGHYMR RFAKTISNVL LQYADIISKD FASYCSKEKE KVPCILMNNT
     QQLRVQLEKM FEAMGGKELD AEASDILKEL QVKLNNVLDE LSRVFATSFQ PHIEECVKQM
     GDILSQVKGT GNVPASACSS VAQDADNVLQ PIMDLLDSNL TLFAKICEKT VLKRVLKELW
     KLVMNTMEKT IVLPPLTDQT GTLLRKHGKG LEKVMRGTQM IFNAAKELGQ LSKLKDHMVR
     EEAKSLTPKQ CAVVELALDT IKQYFHAGGV GLKKTFLEKS PDLQSLRYAL SLYTQATDLL
     IKTFVQTQGA QGSGVEDPVG EVSVHVELFT HPGTGEQKVT VKVVAANDLK WQTSGIFRPF
     IEVNIIGPQL SDKKRKFATK SKNNSWAPKY NESFQFTLSA DAGPECYELQ VCVKDYCFAR
     EDRTVGLAVL QLRELAQRGS AACWLPLGRR IHMDDTGLTV LRILSQRSND EVAKEFVKLK
     SDTRSAEEGG GAAPAP
//
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