ID A0A2Y9QKR6_DELLE Unreviewed; 2006 AA.
AC A0A2Y9QKR6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protein unc-13 homolog B isoform X2 {ECO:0000313|RefSeq:XP_022455787.1};
GN Name=UNC13B {ECO:0000313|RefSeq:XP_022455787.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455787.1};
RN [1] {ECO:0000313|RefSeq:XP_022455787.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455787.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022455787.1; XM_022600079.2.
DR Proteomes; UP000248483; 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; 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 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; 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 Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 873..923
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 979..1103
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1409..1552
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1659..1801
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1834..1961
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 96..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2006 AA; 223797 MW; 58A75346FE2F0D10 CRC64;
MKRLLQESEE EIMVTLGSSS RLSPDKAKVE TLCGFKSKSS GPAGSLPEDS FMSPHCGSVA
SAIGGDRDGC LAQHCSFGQQ ASSQLPLGST ACVSGSGSRD LSSASMTTSC QEPSERDQAK
PLLSRGPGQG CSREQQEPLG DVVDYIIREL QGISHLQTEI AELRQHLSQV RGSVEEVSSC
VDSVLSEIEG LQVGSSPLAK VSVGGKAQEP HVDRPSEEAI LYLYGLPEQD GENTMELVHS
FLAKHLCVNG MQCNRYIKEA YRAGRAPAPR PTVVKLAHLE HRDLILQKSI LLQSLGIRIA
TREEPSRPQC CCKNPPKESL SFLEQQPQDC NLNPLNLDEP VFQVETGDRG PITGVYQMRA
QNQHRELQTP EQQGLCFPPK NDLAKPSDES KPRDEVKGTS GTPQIISGTC GELTGREASL
SNLHQFEEPS LELTSKEEDS GKPQVFKQCN QGLEAYKAAK IENNCSNKSE ASSSLSLSGL
LKTEDKLLAC EAGLDILSSK QLEDLLTDKS RRFATLSCDN VIEEIIMGPE TFNDMVHIDL
NKEEERAAQV LKDVFEKSSC LGGSQEDEDV EIKFYTSKLG RAIYHFRSAL QGVFQKLENS
GSMTPEDLES IESGSQSENS DRLLGTVSSG GAQDFSVESP GSQGSESLLN VVSGGVGIST
QGDQTSQDPS NFSLASNNLP LAYSSPGFAL APCLGSETCS RPESPKQGRL SLEQMCAETI
YLNKCINNLK DVLREKRLRQ KKLLHELVQK TDHLSVEDMH PAKSGFSTEK QGPANTGEGK
RGALQIADDG DTSLPQWLPE GPAGGLYGID SMPDLRRKKP LPLVSDLSLV QSRKAGITSA
MATRTSLKDE ELKSHVYKKT LQALIYPISC TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ
GMRCSECGVK CHEKCQDLLN ADCLQRAAEK SSKHGAEDRT QNIIMAMKDR MKIRERNKPE
IFEVIRDVFN VSKVAHVQQM KTVKQSVLDG TSKWSAKITI TVVCAQGLQA KDKTGSSDPY
VTVQVGKTKK RTKTIFGNLN PVWEEKFHFE CHNSSDRIKV RVWDEDDDIK SRVKQRLKRE
SDDFLGQTII EVRTLSGEMD VWYNLEKRTD KSAVSGAIRL QINVEIKGEE KVAPYHVQYT
CLHENLFHYL TDIQGSGGVH IPEARGDDAW KVYFDETAQE IVDEFAMRYG IESIYQAMTH
FACLSSKYMC PGVPAVMSTL LANINAYYAH TTASANVSAS DRFAASNFGK ERFVKLLDQL
HNSLRIDLST YRNNFPAGSP ERLQDLKSTV DLLTSITFFR MKVQELQSPP RASQVVKDCV
KACLNSTYEY IFNNCHDLYS RQYQLNQELP PEEQGPSIRN LDFWPKLITL VVSIIEEDKN
SYTLILNQFP QELNVGKVSA EVMWQLFAQD MKYALEEHEK DRLCKSADYM NLHFKVKWLH
NEYMRDLPAL QGQVPEYPAW FEQFVLQWLD ENEDVSLEFL RGALERDKKD GFQQTSEHAL
FSCSVVDVFT QLNQSFEIIR KLECPDPNIL AHYMRRFAKT IGKVLMEYAD ILSKDFPAYC
TKEKMPCILM NNMQQLRVQL EKMFEAMGGK ELDPEAADSL KELQVKLNTV LDELSMVFGN
SFQVRIDECV QQMADILGQV RGPGNASPSS RASVTQDADG ALRPLMDFLD GNLTLFATVC
EKTVLKRVLK ELWRVVMNTM ERMIVLPPLT DQTGTQLIFT AAKELSHLSK LKDHMAREET
RSLTPKQCAV LDLALDTIKQ YFHAGGNGLK KTFLEKSPDL QSLRYALSLY TQTTDTLIKT
FVRSQIAQVH DGKGIRFTAN EDIQPEKGSG VDDPVGEVSI QVDLFTHPGT GEHKVTVKVV
AANDLKWQTA GMFRPFVEVT MVGPHQSDKK RKFTTKSKSN NWAPKYNETF HFLLGNEEGP
EAYELQICVK DYCFAREDRV LGLAVMPLRD VAAKGSCACW CPLGRKIHMD ETGMTILRIL
SQRSNDEVAR EFVKLKSESR SVEEGS
//
