ID G1L0M7_AILME Unreviewed; 2174 AA.
AC G1L0M7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Unc-13 homolog C {ECO:0000313|Ensembl:ENSAMEP00000000429.2};
GN Name=UNC13C {ECO:0000313|Ensembl:ENSAMEP00000000429.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000000429.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000000429.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000000429.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSAMET00000000445.2; ENSAMEP00000000429.2; ENSAMEG00000000405.2.
DR GeneTree; ENSGT00940000155174; -.
DR HOGENOM; CLU_001304_2_0_1; -.
DR InParanoid; G1L0M7; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
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:0031914; P:negative regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
DR CDD; cd20859; C1_Munc13-2-like; 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; 2.
DR Gene3D; 3.30.70.1820; L1 transposable element, RRM domain; 1.
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:SF2; PROTEIN UNC-13 HOMOLOG C; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF06292; MUN; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 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 4: Predicted;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1099..1149
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1205..1329
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1639..1782
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1857..1988
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 2002..2129
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2174 AA; 246338 MW; E1A63A90632404C2 CRC64;
MVANLFKSLI LPYIHKLCKG MFTKKLGNTT KKKENHQQKK DQDFPTAGQT KTPKFSNTLK
STVKKIAKCS TTRNLSTEEE EANKEFSLSP TFSYRVAIAN GLQKNINVTS SDNEDRLQEL
SSIESSYSES LNELRSSTEN QAQSTHTMPV RRNRKSSSSL APSEGSSDGE RTLHSLKLGA
LRKLRKWKKS QECVSSDSEL STMKKTWGIR SKSLDRTARN PKTNALEPGF SSSGCISQTH
DVMEMIFKEL QGISQIETEL SELRGHVNAL KHSIDEISSS VEVVQSEIEQ LRTGFVQSRR
ETRDIHDYIK HLGHVGSKAS LRFLNVPEER FEYVESVVYQ ILIDKMGFSD APNAIKIEFA
QRIGHQRDCP NAKPRPILVY FETPQQRDSV LKKSYKLKGT GIGISTDILT HDIRERKERG
IPSSQTYESM DIKLSTPEPK TKNNWQSPDD SDGELKSDLN RNSYAVFSKS EFPTKGSTSK
SSSKSHNARA KNKTASSSRI SNKSDYDKIS SQLPESDNLE KQTTTHYADA TPLWHSQNDF
FTGKLSRSES DFSKLCQSYS EDFSENQFFT RTNGSSLLSS SDRELWQRKQ EGTPTLYDSL
QDQHSNGAVQ GVQGQSEIEN TETVDSGMSN GMACASGDQS HYSESQLSLH EDLSPWKEWS
QVEQGADLGL DSSTQEAFDY DTNSLPDQQL DIYNKDLEDL GKCPSDLQDD SESYDFTQDD
NSSPCPGLDN EPQGQWVGQY DSYQEANSNE LYQNQNQLPR MYRSQSELQS DDSEDAPPKS
WHSRLSIDLS DKAFSFPKFG STLQRAKSAL EVVWNKSTQS LSGYEDSGSS LMGRFRTLSQ
STANESSTTL DSDVYTEPFY YKAEDEEDYS EPVADNETDY VEVMEQVLAK LENRTSMTET
DEQMQVYDHP SYETPYETPQ DEGYDGQADD VVREGGLEPL NEIPAEMEIR EDENQNIPEQ
PVEITKPKRI RPSFKEAALK AYKKQMAELE EKILAGDSSS MDEKARIVSG SDLDASKFSG
LQAIGGAGRG LYGIDSMPDL RRKKTLPIVR DVAMTLAARK SGLSLAMVIR TSLNNEELKI
HVFKKTLQAL IYPMSSTTPH NFEVWTATTP TYCYECEGLL WGIARQGMKC LECGVKCHEK
CQDLLNADCL QRAAEKSSKH GAEDKTQTII TAMKERMKIR EKNRPEVFEV IQEMFQISKE
DFVRYTKAAK QSVLDGTSKW SAKITITVVS AQGLQAKDKT GSSDPYVTVQ VGKNKRRTKT
IFGNLNPVWD EKFYFECHNS TDRIKVRVWD EDDDIKSRVK QHFKKESDDF LGQTIVEVRT
LSGEMDVWYN LEKRTDKSAV SGAIRLKINV EIKGEEKVAP YHIQYTCLHE NLFHYLTEVK
SNGGVKIPEV KGEEAWKVFF DDASQEIVDE FAMRYGIESI YQAMTHFSCL SSKYMCPGVP
AVMSTLLANI NAFYAHTTVS TNVQVSASDR FAATNFGREK FIKLLDQLHN SLRIDLSKYR
ENFPASNAER LQDLKSTVDL LTSITFFRMK VLELQSPPKA SMVVKDCVRA CLDSTYKYIF
DNCHELYSQL IDPSKKQDIP REDQGPTTKN LDFWPQIITL MVTIIDEDKT AYTPVLNQFP
QELNMGKISA EIMWTLFAQD MKYALEEHEK QRLCKSTDYM NLHFKVKWFY NEYVRELPAF
KDAVPEYSLW FEPFVMQWLD ENEDVSMEFL HGALGRDKKD GFPQTSDHAL FSCSVVDVFA
QLNQSFEIIK KLECPNPEAL SHLMRRFAKT INKVLLQYAA IVSSDFSSYC DKENVPCILM
NNIQQLRVQL EKMFESMGGK ELDPEASTIL KELQVKLNGA LDELSITYGE SFQHIIEECI
KQMSFELNQM RTNGNTASNK NSSAMDAEIV LRPLMDFLDK GPQMIFIAAK DLGQLSKLKE
HMIREDAKGL TPRQCAVMEV VLATIKQYFH AGGNGLKKNF LEKSPDLQSL RYALSLYTQT
TDALIKKFID TQTSQSRPSK DSVGQISVHV DITATPGTGE HKVTVKVIAI NDLNWQTTAM
FRPFVEVCIL GPNLGDKKRK QGTKTKSNTW SPKYNETFQF ILGNENRPGA YELHLSVKDY
CFAREDRIIG MTVIQLQNIA EKGSYGSWYP LLKNVSMDET GLTILRILSQ RTSDDVAKEF
VRLKSETRSA EESA
//
