ID A0A3Q1EPP5_9TELE Unreviewed; 1577 AA.
AC A0A3Q1EPP5;
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:ENSAPOP00000005442.1};
GN Name=UNC13B {ECO:0000313|Ensembl:ENSAPOP00000005442.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000005442.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000005442.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSAPOT00000008336.1; ENSAPOP00000005442.1; ENSAPOG00000007328.1.
DR GeneTree; ENSGT00940000154929; -.
DR Proteomes; UP000257200; 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:UP000257200};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 463..513
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 569..693
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1003..1146
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1251..1391
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1405..1532
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 172..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1577 AA; 178894 MW; 55AE66AECB7B6A64 CRC64;
MSLLCVRVKK AKLHGSPDKF NTYVTLKVQN VKSTTITVRG DQPCWEQDFM FEINRLDLGL
IVEVWNKGLI WDTMLGTAWI PLKSIPQSSE EGSGEWIFLD AEVLMKEDEI CGTKNPTPHR
VLLDTRFELP FDIPDDEAQY WTGKLERINT MGMHDEDDAQ SRPLPFVASQ CSLDDQDSAV
EDRDSDYRSE TSNSLPPRYH TTAQPNSSLH QYPMGPRCQQ HQDGFRDSDH SFELDCRDQR
GTSPADSSHF GSSGNLSQTS SQVSEIGHES TGGSELEESF HSYHSTGCHP STTGQPRSSR
HLPTNGYSTV TEQERNRPPS EAGKGLKNDV PAVRGSSKPP RFHYDGPPLP FNPARVRWLK
AINKVRVQLR EVQGEEPGAR QAWAEPGGTS ASGLYGIDSM PDLRKKKPIP LVSDVVQSLV
QARKAGIASA MAARSSIKDE ELKNHVYKKT LQALIYPISC TTPHNFEVWT ATTPTYCYEC
EGLLWGIARQ GMRCSECGVK CHEKCQELLN ADCLQRAAEK SSKHGAEDRT QNIIMAMKDR
MKIRERNKPE IFELIREVFV ISKTVHAQQM KITKQSVLDG TSGWSAKITI TVVCAQGLQA
KDKTGSSDPY VTVQVGRTKK RTKTIYGNLN PVWEEKFHFE CHNTSDRIKV RVWDEDDDIK
SRVKQRLKRE SDDFLGQSII EVRTLSGEMD VWYNLEKRTD KSAVSGAIRL HINVEIKGEE
KVAPYHIQYT CLHENLFHHT TDVLGQGVVK IPEARGDDSW KVYFDDVPQE IVDEFAMRYG
IESIYQAMTH FACLSSKYMC PGVPAVMSSL LANINAFYAR TTASNNVSAS DRFAASNFGK
ERFVKLLDQL HNSLRIDLST YRNHFPASNK DRLQDLKSTV DLLTSITFFR MKVQEIPSPP
RASQVVKDCV KACLNSTYDY IFNNCYELYS RQYHPLETIK DELPLEEQGP SIKNLDFWPK
LIMLIVSIIE EDGNSYGPVL NQFPQELNVG KVSAEVMWTL FAQDMKYAMD EHEKHRLCKS
TDYMNLHFKV KWLYNEYVKD LPAFDSAVPD YPAWFVQFVL QWLDENEDVS MEFMHGALER
DKKDGFQQTS EHALFSCSVV DIFTQLNQSF EIIKKLECPD PDVTAQYTRR FSKTITKVLL
QYSAILTKSF PSYIDKENIP CVLMNNVQQL RIQLEKMFEW MGAKQMDSEA SDLLNELQVK
LNNALDELTG TFGNSFQSRI HDCMRQMASL LYQVKGPLNA NTKAQVDGDS DNVLRPLMDF
LDGKLTLFAT VCEKTVLKRV LKELWRIVMT NLEKTIVLPQ SNDTFGAQLF SAAKELGQLS
KLKDHMAGEA RSLSPRQCAV MDVALDTIKQ YFHAGGNGLK KTFLDKSPEL SSLRHALSLY
TQTTDTLIKT FVTSQQAQGP GVENPIGEVS VHIELHTHPS SGERRATVRV VLARDLKWQT
SGMFRPFVEI TMIGPHLADR KRKFQTKSKN NSWSPKFNES FQFVLGSVNG FECYELQVCV
KDYCFGRADR VVGLAVIQLK DIMWTGNCAC WCPLGERVHM DDKGLTVMRI LSQRSNDDVA
KEFVKLKSES RSAEEGR
//
