ID   UN13C_RAT               Reviewed;        2204 AA.
AC   Q62770;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Protein unc-13 homolog C;
DE   AltName: Full=Munc13-3;
GN   Name=Unc13c; Synonyms=Unc13h3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Telemenakis I., Brose N., Suedhof T.C.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 942-1634, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=7559667; DOI=10.1074/jbc.270.42.25273;
RA   Brose N., Hofmann K., Hata Y., Suedhof T.C.;
RT   "Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel
RT   family of C2-domain proteins.";
RL   J. Biol. Chem. 270:25273-25280(1995).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INTERACTION WITH SYNTAXIN 1; VAMP2 AND SNAP25.
RX   PubMed=9895278; DOI=10.1042/bj3370363;
RA   Augustin I., Betz A., Herrmann C., Jo T., Brose N.;
RT   "Differential expression of two novel Munc13 proteins in rat brain.";
RL   Biochem. J. 337:363-371(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-446; SER-450 AND
RP   SER-778, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May play a role in vesicle maturation during exocytosis as a
CC       target of the diacylglycerol second messenger pathway. May be involved
CC       in the regulation of synaptic transmission at parallel fiber - Purkinje
CC       cell synapses (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC   -!- SUBUNIT: Interacts with STX1A and/or STX1B1, VAMP2 and SNAP25.
CC       {ECO:0000269|PubMed:9895278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9895278}. Membrane
CC       {ECO:0000305|PubMed:9895278}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:9895278}. Presynaptic cell membrane
CC       {ECO:0000305|PubMed:9895278}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:9895278}. Note=Localized to presynaptic structures.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in brain, predominantly in
CC       the cerebellum. {ECO:0000269|PubMed:7559667,
CC       ECO:0000269|PubMed:9895278}.
CC   -!- DEVELOPMENTAL STAGE: First detected at birth, after which expression
CC       level is steadily increasing until it reaches a plateau at P15.
CC       {ECO:0000269|PubMed:9895278}.
CC   -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC       phospholipid binding.
CC   -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB39720.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U75361; AAB39720.1; ALT_INIT; mRNA.
DR   PIR; T42759; T42759.
DR   RefSeq; NP_775169.4; NM_173146.2.
DR   AlphaFoldDB; Q62770; -.
DR   SMR; Q62770; -.
DR   STRING; 10116.ENSRNOP00000010330; -.
DR   iPTMnet; Q62770; -.
DR   PhosphoSitePlus; Q62770; -.
DR   PaxDb; Q62770; -.
DR   PRIDE; Q62770; -.
DR   GeneID; 286931; -.
DR   KEGG; rno:286931; -.
DR   UCSC; RGD:628592; rat.
DR   CTD; 440279; -.
DR   RGD; 628592; Unc13c.
DR   eggNOG; KOG1011; Eukaryota.
DR   InParanoid; Q62770; -.
DR   OrthoDB; 117172at2759; -.
DR   PhylomeDB; Q62770; -.
DR   PRO; PR:Q62770; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0098793; C:presynapse; ISO:RGD.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0019905; F:syntaxin binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR   GO; GO:0031914; P:negative regulation of synaptic plasticity; ISO:RGD.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:RGD.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   GO; GO:0016081; P:synaptic vesicle docking; IBA:GO_Central.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR   GO; GO:0016082; P:synaptic vesicle priming; IMP:ParkinsonsUK-UCL.
DR   CDD; cd00029; C1; 1.
DR   CDD; cd04027; C2B_Munc13; 1.
DR   Gene3D; 2.60.40.150; -; 2.
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   InterPro; IPR027087; Unc13C.
DR   PANTHER; PTHR10480; PTHR10480; 3.
DR   PANTHER; PTHR10480:SF2; PTHR10480:SF2; 3.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF06292; MUN; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM01145; DUF1041; 1.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   SUPFAM; SSF57889; SSF57889; 1.
DR   PROSITE; PS50004; C2; 2.
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   1: Evidence at protein level;
KW   Calcium; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Exocytosis; Membrane; Metal-binding; Methylation; Phosphoprotein;
KW   Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT   CHAIN           1..2204
FT                   /note="Protein unc-13 homolog C"
FT                   /id="PRO_0000188580"
FT   DOMAIN          1193..1317
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          1627..1770
FT                   /note="MHD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT   DOMAIN          1876..2018
FT                   /note="MHD2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT   DOMAIN          2032..2159
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   ZN_FING         1087..1137
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          28..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          961..984
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        128..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1226
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1226
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         1297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         778
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1017
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K0T7"
SQ   SEQUENCE   2204 AA;  249136 MW;  13F1C251FA28E00E CRC64;
     MVASLFKSLI LAYIHKLCKG MFTKKLGNTT KKKENRQQNK DQDFPTAGHT KPPKLSNALK
     STVKKIAKCS STRNFSVEDE EGHKDFSLSP TFSYRVAIAN GLQTAVTNSD EDLLQELSSI
     ESSYSESFNE LRSSTENQVQ STHTMPVRRN RKSSSSLAPS EGSSDGERTL HTLKLGALRK
     LRKWKKSQEC VSSDSELSTV KKTWGIRSKS LDRTARNPKT NVLEPGFSSS GCISQTHDVM
     EMIFKELQGI SQIETELSEL RGHVNALKYS IDEISSSVEV VQSEIEQLRT GFVQARRETR
     DIHDYIKHLG HMGSKVSLRF LNVPEERHEY VESVVYQILV DKMGFSDVPN AIKIEFAQRI
     GQQRDCPNAK PRPILVYFET PQQRDSVLKK SYKLKGTGIA ISTDILTYDI RERKEKGVLP
     SSQTYESMDM KLSTPEPKAK KNAWLSPNDS DRELESDLSR SSYADSPAKG SSSKSSSKSH
     SARSKNKAAN SRTSQKSDYN KRPSKPPASE KPTPHYVEAT PLWHSQSDFF TPKLSRSESD
     FSKLCQSYSE DFSESQFFCR TNGSSLLSSS DRELWQRKQE GMTALYHSPQ DQGLDGNIPT
     VPGQGEIENT ETVDSGMSNS VVCASGDRSN YSGSQLSLHE DLSPWKEWNQ AGHGTDGLDS
     STQEPFDYDT NSLSDQQLDM SSKDLDDLGK CHSDLQDDSE SYDLTQDDNS SPCPGLDNEP
     QGQWVGQYDS YQKTNSNDLY PNQSHPSMMY RSQSELQSDD SEAAQPKSWH SRLSIDLSDK
     TFKFPKFGST LQRAKSALEV VWNKSTQSLS GCEDSGSSLM GRFRTLSQST ANESSTTLDS
     DIYTEPYYYK AEEEEDYCEP VADSETDYVE VMEQVLAKLE NRTSVTEVDE HIKEYDHPSY
     ETPYETPQDE GYDGQADDII SEGELETLNE PAVEMELVED ESQNLPVEPP EVMKPKRIRP
     SFKEAALRAY KKQMAELEEK ILAGDSSSVD EKARIVSGND LDASKFSALQ VFGGAGRGLY
     GIDSMPDLRR KKTLPIVRDV AMTLAARKSG LSLAMVIRTS LNNEELKMHV FRKTLQALIY
     PISSTTPHNF EVWTATTPTY CYECEGLLWG IARQGMKCLE CGVKCHEKCQ DLLNADCLQR
     AAEKSSKHGA EDKTQTIITA MKERMKIRER NRPEVFEVIQ EMFQISKEDF VQYTKAAKQS
     VLDGTSKWSA KITITVVSAQ GLQAKDKTGS SDPYVTVQVG KNKRRTKTIF GNLNPVWDEK
     FYFECHNSTD RIKVRVWDED DDIKSRVKQH FKKESDDFLG QTIVEVRTLS GEMDVWYNLE
     KRTDKSAVSG AIRLKINVEI KGEEKVAPYH IQYTCLHENL FHYLTEVKSN GSVKIPEVKG
     DEAWKVFFDD ASQEIVDEFA MRYGVESIYQ AMTHFSCLSS KYMCPGVPAV MSALLANINA
     FYAHTTVSTN VQVSASDRFA ATNFGREKFI KLLDQLHNSL RIDLSKYREN FPASNSERLQ
     DLKSTVDLLT SITFFRMKVL ELQSPPKASA VVKDCVRACL DSTYKYIFDN CHELYSQLID
     PSKKQDVPRE EQGPTTKNLD FWPQLITLMV TIIDEDKTAY TPVLNQFPQE LNMGKISAEI
     MWSLFALDMK YALEEHEKQR LCKSTDYMNL HFKVKWFYNE YVRELPAFKD AVPEYSLWFE
     PFVMQWLDEN EDVSMEFLHG ALGRDKKDGF QQTSDHALFS CSVVDVFAQL NQSFEIIKKL
     ECPNPEALSH LMRRFAKTIN KVLVQYAAIV SSDFSSYCDK ETVPCILMNN IQQLRVQLEK
     MFESMGGKEL DPEASTILKE LQIKLNGVLD ALSVTYGESF QLVIEECIKQ MGAELNQMRA
     NGNSAANKNN AAMDAEIVLR PLMDFLDKIL SLSAKICEKT VLKRVLKELW KLVLNKIEKQ
     IVLPPLTDQT GPQMIFIAAK ELGQLSKLKE HMIRDDAKGL TPRQCAIMEV VLATIKQYFH
     AGGNGLKKNF LEKSPDLHSL RYALSLYTQT TDALIKKFIE TQGSQSRSSK DAVGQISVHV
     DVTTTPGTGE HKVTVKVIAI NDLNWQTTTM FRPFVEVCML GPSLGDKKRK QGTKTKSNTW
     SPKYNETFQF ILGNENRPGA YELHLSVKDY CFAREDRIIG MTVIQLQNIA EKGSYGAWYP
     LLKNLSMDET GLTILRILSQ RTSDDVAKEF VRLKSETRSI DESA