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Database: UniProt
Entry: A0A091PAJ3_APAVI
LinkDB: A0A091PAJ3_APAVI
Original site: A0A091PAJ3_APAVI 
ID   A0A091PAJ3_APAVI        Unreviewed;      2168 AA.
AC   A0A091PAJ3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Protein unc-13 C {ECO:0000313|EMBL:KFP88555.1};
GN   ORFNames=N311_12809 {ECO:0000313|EMBL:KFP88555.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP88555.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP88555.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP88555.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL382866; KFP88555.1; -; Genomic_DNA.
DR   Proteomes; UP000054244; 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:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
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; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1053..1103
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1159..1283
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1591..1734
FT                   /note="MHD1"
FT                   /evidence="ECO:0000259|PROSITE:PS51258"
FT   DOMAIN          1840..1982
FT                   /note="MHD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51259"
FT   DOMAIN          1996..2123
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          26..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          253..287
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        41..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2168 AA;  246991 MW;  11E62113176D6697 CRC64;
     MVSALLKSLI SPYIYKICKG MFTKKSGNST KRKESCQSKK EQDLTQIGQT KNPKFSNTLK
     STVKKIAKCP SARNLSTEEE ESNREFSLSP TFSYRVAIAN GLQKHIFVTN NNNEDIVHDL
     SSNDSSCSES LSEVKNSSKK NEYLSHTMPV RRNRKSLSSL APSDGSSDGE RTLHTLKLGA
     LRKLRKWKKS QECVSSDSEL STWKKTWGLR SKSLDRAGRH QKSNTLEPGF SSTGCISQTH
     DVMEMIFKEL QGISQIETEL SELRGHVNAL KQSIDEISSS VEVVQNEIEQ LRTGFVQSRR
     ETRDIHDYIK QIGHPGNKAS LRFLNVPEER LEKTESMVYK ILIDKMGFSE AQSTIKIEFA
     QRLGQQRDCP NAKPRPILVY FESSQQRDLV LKKSYKLKGT GIGISTDLFS HDVRDKKERG
     LPSSQTYESM DMKLLTVETK TKIHDWESPD SDKDLESDIN KNSYAKISKS ALQVKTNTTK
     ASIESPNTED LNRTADDNTF SNRRNYGNQS PEFDNMEKQS QTYYSDVTPL WHLQNDFATP
     KLSRSESDFS KLCQSYSEDF SENQYFSRTN GGSLLSSSDR ELWQRRQDDS TVWYSSSQEQ
     TFVQDVQQYP EQNEVENTAA VDSGVSNGII CASGDRSHFS DSQLSLHDDL SPWKDWNHLK
     QGADMGLDSS TQDVFVYDMS SLDSESQSQW TGQYDDYQET NSISSYQNQN RLPMMYRSQS
     ELPSDDSEET APKSWHSRLS IDLSDKSFSF PKFGSTLQRA KSALEVVWNK STQSLSGYED
     SGSSFMGRFR TLSQSTANES STTLDSDVYA EPYCYKAEYE EDLIEPPGEN ETDYVEVMEQ
     VLAKLENRTN SSETSEQVQE YELGQPLYEA PYAVLPEEQY DTQFNGVVIE QILEVESDMA
     ADTEVREDEN QNIPEMLTET PKKKRIRPSF KEAALKAYKK QMNELEEKIL AGDSGSVDEK
     ARIVSGSSLD TSKLYAVQAF SAAGRGLYGI DSMPDLRRKK SFPIVRDVTL AARKSGISMA
     MLIRTSINND DMKIHVFKKT LQALIYPISS TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ
     GMRCTECGVK CHEKCQDLLN ADCLQRAAEK SSKHGAEDKT QNIISAMKER MKIREKNRPE
     VFEVIQEMFN ISKEDFVQYT KAAKQSVLDG TSKWSAKITI TVLCAQGLQA KDKTGSSDPY
     VTVQVGKTKR RTKTIFGNLN PVWDEKFYFE CHNSTDRIKV RVWDEDDDIK SRVKQHFKKE
     SDDFLGQTII EVRTLSGEMD VWYNLEKRTD KSAVSGAIRL KINVEIEGEE KVAPYHVQYT
     CLHENLFHYL TEVKSNGVVK IPEVRGDEAW KVYFDDAAQE IVDEFAMRYG IEYIYQAMTH
     FSCLSSKYMC PGVPAVMSTL LANINAFYAH TTAATNVSAS DRFAATNFGR EKFIKLLDQL
     HNSLRIDLSK YRDNFPASNS ERLQDLKSTV DLLTSITFFR MKVLELQSPP RASTVVKDCV
     RACLDSTYKY IFDNCYDLYS QLVDQSKKQE VPKEEQGPTT KNLDFWAQLI TLMVTIIDED
     KTAYTPILNQ FPQELNMGKI SAEIMWTLFA QDMKYALEEH EKQRLCKSTD YMNLHFKVKW
     FYNEYVRELS AFKDAVPEYS LWFEPFVIQW LDENEDVSME FLHGALERDK KDGFQQTSDH
     ALFSCSVVDV FTQLNQSFEI IRKLECPNPE ALSHLMRRFA KTINKVLLQY AVIISNYFSS
     YCDKDNVPCI LMNNIQQLRV QLEKMFESMG GKELDPEASA VLKELQMKLS NVLDELSVTY
     GTSFQFIIED CVRQMSNELN QMRGNGNAAA NKNSAAIDAE IVLRPLMDFL DKTLSVSAKI
     CEKTVLKRVL KELWKLVLNK IEKQIVLPPL TDQTGPQMIF SAAKDLGQLS KLKDHMIREE
     ARSLTLRQCA IMEVALVTIK QYFHAGGSGL KKNFLEKSPD LQSLKYALSL YTQTTDALIK
     KFIDTQKSQS QTTNNSVGEI SIQVDVSTHP GTGEHKVTVK VVALNNLNWQ TTAMFRPFVE
     VFLLGPNLSD KKRKHGTKTK SNTWSPKYNE TFQFILSNED KPGAYELHLS VKDYCFARED
     RIIGMAVLQL QNIAEKGSCA SWYPLLRNIS VDETGLTILR ILSQRTNDEV AKEFVRLKTE
     TRSAEEMA
//
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