ID A0A3Q2VD78_HAPBU Unreviewed; 1500 AA.
AC A0A3Q2VD78;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Unc-13 homolog B {ECO:0000313|Ensembl:ENSHBUP00000008930.1};
GN Name=UNC13B {ECO:0000313|Ensembl:ENSHBUP00000008930.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000008930.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000008930.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSHBUT00000001109.1; ENSHBUP00000008930.1; ENSHBUG00000010528.1.
DR GeneTree; ENSGT00940000154929; -.
DR OMA; WRIVMTN; -.
DR Proteomes; UP000264840; Unplaced.
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: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; 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:SF8; PROTEIN UNC-13 HOMOLOG B; 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:UP000264840};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..87
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 408..458
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 514..638
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 944..1087
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1192..1314
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1328..1455
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 166..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1500 AA; 171275 MW; A2AC1AB5BCA4E332 CRC64;
LTMLCVFITF NTYVTLKVQN VKSTTITVRG DQPCWEQDFM FEINQLDLGL IVEVWNKGLI
WDTMVGTAWI PLKSIRQSEE EGSGEWLFLD AEVLMKADEI YGTKNPTPHR VLLDTRFELP
FDIPDDEAQY WTGKLERINR MGIHDEYSLQ EDVQSHPLPF AASQCSLDDQ DSAVDDRDSD
YRSETSNSLP PRYHTTAQPN SSMHQYPMGP RPQHRPDGCT DSVHSFDLDY RDPRGSSPVE
SSRFGSSGNL SQTSSQLSET GHESTGGSEL EESFHSYHST GFHPSTNGQY IFISSFSSFH
LMLQSILHWM KAITKVRVQL REEDSDPSVY MDCLEIGGSG LYGIDSMPDL RKKKPIPLVS
DVSLVQARKA GIASAMAARS SIKDEELKNH VYKKTLQALI YPISCTTPHN FEVWTATTPT
YCYECEGLLW GIARQGMRCS ECGVKCHEKC QELLNADCLQ RAAEKSSKHG AEDRTQNIIM
AMKDRMKIRE RNKPEIFELI REVFVISKAI HAQQMKTIKQ SVLDGTSKWS AKITITVVCA
QGLQAKDKTG SSDPYVTVQV GKTKKRTKTI YGNLNPVWEE KFHFECHNSS DRIKVRVWDE
DDDIKSRVKQ RLKRESDDFL GQSIIEVRTL SGEMDVWYNL EKRTDKSAVS GAIRLQINVE
IKGEEKVAPY HVQYTCLHEN LFHHSTDVLG QGVVKIPEAR GDDSWKVYFD DVGQEVVDEF
AMRYGIESIY QAMTHFACLS SKYMCPGVPA VMSTLLANIN AFYAHTTAST NVSASDRFAA
SNFGKERFVK LLDQLHNSLR IDLSSYRNHF PASSKDRLQD LKSTVDLLTS ITFFRMKVQE
LQSPPRASQV VRDCVKACLN STYDYIFNNC HELYSRQYQP KEELPLEEQG PSIKNLDFWP
KLIMLIVSII EEDRNSYTPV LNQFPQELNV GKVSAEVMWT LFAQDMKYAM EEHEKHRLCK
STDYMNLHFK VKWLYNEYVK ELPVFKGVVP DYPSWFVQFV LQWLDENEEV SMEFMNGALE
RDKKDGFQQT SEHALFSCSV VDIFTQLNQS FEIIKKLECP DPRVMAQYSR RFSKTIAKVL
LQYSAMLTKN FPSYIDKEKI PCVLMNNVQQ LRIQLEKMFE SMGAKQMDTE ACDLLNDLQV
RLNNVLDDLS RTFGNSFQTR INECMRQMAS LLYQIKGPVN ANNKNQVEAD SDNMLRPLMD
FLDGKLTLFA TVCEKTVLKR VLKELWRIVM TSLEKTIVLP QGNDTFDHMA GEAKSLSPRQ
CAVMDVALDT IKQYFHAGGN GLKKAFLEKS PELSSLRHAL SLYTQTTDTL IKTFVTTQQA
QGSGVDKPIG EVCIHIELYT HPKSGERKVT VKVVGASDLK WQTSGMFRPF VEITMIGPHL
SDKKRKFQTK SKNNSWSPKF NETFHFVLGN QDGFECYELQ ACVKDYCFGR ADRVVGLVVL
QLRDIMEKGN CACWCPLGQR IYMDDTGLTA LRILSQRSND DVAKEFVRLK SETRSAEEGR
//
