ID A0A2K6KRM0_RHIBE Unreviewed; 1622 AA.
AC A0A2K6KRM0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Unc-13 homolog B {ECO:0000313|Ensembl:ENSRBIP00000013900.1};
GN Name=UNC13B {ECO:0000313|Ensembl:ENSRBIP00000013900.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000013900.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000013900.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000013900.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the unc-13 family.
CC {ECO:0000256|ARBA:ARBA00005823}.
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DR Ensembl; ENSRBIT00000037716.1; ENSRBIP00000013900.1; ENSRBIG00000030923.1.
DR GeneTree; ENSGT00940000154929; -.
DR Proteomes; UP000233180; 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 3: Inferred from homology;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 489..539
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 595..719
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1025..1168
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1275..1417
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1450..1577
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 188..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1622 AA; 184565 MW; 11A467055506A3F2 CRC64;
MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AEALMKDDEI CGTRNPTPHK
ILLDTRFELP FDIPEEEARY WTYKWEQINA LGADNEYSSQ EESQRKPLPT AAAQCCHWTY
LGWGEQQTFE DPDSAVDDRD SDYRSETSNS IPPPYHTTSQ PNTSVHQFPV PVGLPQQLLL
QGSSRDSCND SMQSYDFDYP ERRAISPTSS SRYGSSCNVS QGSSQLSELD QYHEQDDDHR
ERDSIHSCHS SNSLSRDGQA GFREQEKPLE VTVQAEKEAA CEPKKTKEDA TTPPPPDLMQ
HKDHFLGPQE SFPEENVSSP FTHARAHWIR AVTKVRLQLQ EIPDDGDPSL PQWLPEGPAG
GLYGIDSMPD LRRKKPLPLV SDLSLVQSRK AGITSAMATR TSLKDEELKS HVYKKTLQAL
IYPISCTTPH NFEVWTATTP TYCYECEGLL WGIARQGMRC SECGVKCHEK CQDLLNADCL
QRAAEKSCKH GAEDRTQNII MAMKDRMKIR ERNKPEIFEV IRDVFTVSKA AHVQQMKTVK
QSVLDGTSKW SAKITITVVC AQGLQAKDKT GSSDPYVTVQ VGKTKKRTKT IFGNLNPVWE
EKFHFECHNS SDRIKVRVWD EDDDIKSRVK QRLKRESDDF LGQTIIEVRT LSGEMDVWYN
LEKRTDKSAV SGAIRLQISV EIKGEEKVAP YHVQYTCLHE NLFHYLTDIQ GSGGVRIPEA
RGDDAWKVYF DETAQEIVDE FAMRYGIESI YQAMTHFACL SSKYMCPGVP AVMSTLLANI
NAYYAHTTAS TNVSASDRFA ASNFGKERFV KLLDQLHNSL RIDLSTYRNN FPAGSPERLQ
DLKSTVDLLT SITFFRMKVQ ELQSPPRASQ VVKDCVKACL NSTYEYIFNN CHDLYSHQYQ
LKQELPPEEQ GPSIRNLDFW PKLITLIVSI IEEDKNSYTP VLNQFPQELN VGKVSAEVMW
HLFAQDMKYA LEEHEKDRLC KSADYMNLHF KVKWLHNEYV RDLPVLQGQV PEYPAWFEQF
VLQWLDENED VSLEFLHGAL ERDKKDGFQQ TSEHALFSCS VVDVFTQLNQ SFEIIRKLEC
PDPSILAHYM RRFAKTIGKV LMQYADILSK DFPTYCTKEK LPCILMNNMQ QLRVQLEKMF
EAMGGKELDL EAADSLKELQ VKLNTVLDEL SMVFGNSFQV RIDECVRQMA DILGQVRGTG
NASPDARASA TQDADSVLRP LMDFLDGNLT LFATVCEKTV LKRVLKELWR VVMNTMERMI
VLPPLTDQTG TQMIFTAAKE LSHLSKLKDH MVREETRNLT PKQCAVLDLA LDTIKQYFHA
GGNGLKKTFL EKSPDLQSLR YALSLYTQTT DTLIKTFVRS QTTQVHDGKG IRFTANEDIR
PEKGSGVDDP VGEVSIQVDL FTHPGTGEHK VTVKVVAAND LKWQTAGMFR PFVEVTMVGP
HQSDKKRKFT TKSKSNNWAP KYNETFHFLL GNEEGPESYE LQICVKDYCF AREDRMLGLA
VMPLRDVTAK GSCACWCPLG RKIHMDETGL TILRILSQRS NDEVAREFVK LKSESRSTEE
GS
//
