ID A0A2Y9DDG4_TRIMA Unreviewed; 1591 AA.
AC A0A2Y9DDG4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protein unc-13 homolog B {ECO:0000313|RefSeq:XP_004372354.1};
GN Name=LOC101354912 {ECO:0000313|RefSeq:XP_004372354.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004372354.1};
RN [1] {ECO:0000313|RefSeq:XP_004372354.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_004372354.1; XM_004372297.2.
DR STRING; 127582.A0A2Y9DDG4; -.
DR GeneID; 101354912; -.
DR KEGG; tmu:101354912; -.
DR InParanoid; A0A2Y9DDG4; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000248480; 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: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:UP000248480};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 477..527
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 583..707
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1013..1156
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1263..1405
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1419..1546
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 176..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1591 AA; 180644 MW; 93ACEBC3BD173897 CRC64;
MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AETLMKDDEI CGTKNPTPHK
ILLDTRFELP FDIPEEEARY WTYKLEQINA LGTDNEYSIQ EESQRKLLPT AAAQCSCEDP
DSAVDDRDSD YRSETSNSIP PPYHTTSQPN ASVHQFPVPV QLPQQLLLQG SSRDSCNDSM
QSYDLDYPER RALSPTSSSR YGSSCNVSQG SSQLSELDQY HEQDDDHRER DSIHSCHSSG
SFSRDGQAGV REQEKVLEVT DETEKEKICE PKEIKQDATA HPLPHLVLHK EDILGPQESF
PEDNASSPFT QARAHWIRAV TKVRLQLQEI PDDGDSSLPQ WIPEGPAGGL YGIDSMPDLR
RKKLLPLVSD LSLVQSRKAG ITSAMATHTS LKDEELKSHV YKKTLQALIY PISCTTPHNF
EVWTATTPTY CYECEGLLWG IARQGMRCSE CGVKCHEKCQ DLLNADCLQR AAEKSSKHGA
EDRTQNIIMA MKDRMKIRER NKPEIFEVIR DVFTVSKVAH VQQMKTVKQS VLDGTSKWSA
KITITVVCAQ GLQAKDKTGS SDPYVTVQVG KTKKRTKTIF GNLNPVWEEK FHFECPNSSD
RIKVRVWDED DDIKSRVKQR LKRESDDFLG QTIIEVRTLS GEMDVWYNLE KRTDKSAVSG
AIRLQINVEI KGEEKVAPYH VQYMCLHENL FHYLTDIQGS GGVQIPEARG DDAWKVYFDE
TAQEIVDEFA MRYGIESIYQ AMTHFACLSS KYMCPGVPAV MSTLLANINA YYAHTTASTN
VSASDRFAAS NFGKERFVKL LDQLHNSLRI DLSTYRNNFP AGSPDRLQDL KSTVDLLTSI
TFFRMKVQEL QSPPRASQVV KDCVKACLNS TYEYIFNNCH DLYSRQYQLK HELPPEEQGP
SIRNLDFWPK LITLIVSIIE EDKNSYTPVL NQFPQELNVG KVSAEVMWHL FAQDMKYALE
EHEKDRLCKS ADYMNLHFKV KWLHNEYVQD LPALQGQVPE YPAWFEQFVL QWLDENEDVS
VEFLRGALER DKKDGFQQTS EHALFSCSVV DVFTQLNQSF EIIRKLECPD PNILAHYMRR
FAKTIGKVLM QYADILSKNF PAYCTKEKLP CILMNNMQQL RVQLEKMFEA MGGKELDPEA
ADSLKELQVK LNTVLDELSM VFGNSFQVQI DECVRQMADI LGQVRGPGNA SPNARASVAQ
DADSVLRPLM DFLDGNLTLF ATVCEKTVLK RVLKELWRVV MNTIERMIVV PPLTDQTGTQ
LIFTAAKELS QLSKLKDHMV REETRSLTPK QCAVLDLALD TIKQYFHAGG NGLKKTFLEK
SPDLQSLRYA LSLYTQTTDT LIKTFVRSQT AQGSGMDDSV GEISIQVDLF THPGTGEHKV
TVKVVAANDL KWQTAGMFRP FVEVTMVGPH QSDKKRKFTT KSKSNNWTPK YNETFHFLLG
NEEGPEAYEL QICVKDYCFA REDRVLGLAV MPLRDVAAKG SCACWCPLGR KIHMDETGMT
ILRILSQRSN DEVAREFVKL KSESRSTEEG S
//
