ID A0A1S3G0F1_DIPOR Unreviewed; 1591 AA.
AC A0A1S3G0F1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protein unc-13 homolog B isoform X2 {ECO:0000313|RefSeq:XP_012882120.1};
GN Name=Unc13b {ECO:0000313|RefSeq:XP_012882120.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012882120.1};
RN [1] {ECO:0000313|RefSeq:XP_012882120.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012882120.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_012882120.1; XM_013026666.1.
DR STRING; 10020.ENSDORP00000015544; -.
DR GeneID; 105993409; -.
DR CTD; 10497; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000081671; 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:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:UniProt.
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:UP000081671};
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..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1591 AA; 180765 MW; 7F2ABEE82B37274F CRC64;
MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AETLMKNDEI CGTKNPTPHK
ILLDTRFELP FDIPEEEARY WTYKLEQINA FGADNEYSIQ EESQRKPLPT AAAQCSFEDP
DSAVDDRDSD YRSETSNSIP PPYHTTSQPN ASVHQFHMPV RLPQQLLLQG SSRDSCSDSM
QSYDLYYPER QALSPTSSSR YGSSCNVSQG SSQLSELDQY PEQDDDRRER DSIHSCHSSG
SLSRDSKPNF GEQEKALEVT CEAEKERICE LKEIKEDATI HPPSDLILHK DHIVGPQESL
PEENASSPFT QARAHWIRAV TKVRLQLQEI PDDGDPSLPQ WLPEGPAGGL YGIDSMPDLR
RKKPLPLVSD LSLVQSRKAG ITSAMATRTS LKDEELKSHV YKKTLQALIY PISCTTPHNF
EVWTATTPTY CYECEGMLWG IARQGMRCSE CGVKCHEKCQ DLLNADCLQR AAEKSSKHGA
EDRTQNIIMA MKDRMKIRER NKPEIFEVIR DVFTVSKVAH VQQMKTVKQS VLDGTSKWSA
KITITVVCAQ GLQAKDKTGS SDPYVTVQVG KTKKRTKTIF GNLNPVWEEK FHFECHNSSD
RIKVRVWDED DDIKSKVKQR LKRESDDFLG QTIIEVRTLS GEMDVWYNLE KRTDKSAVSG
AIRLQISVEI KGEEKVAPYH VQYTCLHENL FHFLTDIQGS GVVRIPEARG DDAWKVYFDE
TAQEIVDEFA MRYGIESIYQ AMTHFACLSS KYMCPGVPAV MSTLLANINA YYAHTTASTN
VSASDRFAAS NFGKERFVKL LDQLHNSLRI DLSTYRNNFP AGSPERLQDL KSTVDLLTSI
TFFRMKVQEL QSPPRASQVV KDCVKACLNS TYEYIFNNCH DLYSHQYQLN QELPPEEQGP
SIQNLDFWPK LITLIVSIIE EDKNSYTPVL NQFPQELNVG KVSAEVMWHL FSQDMKYALE
EHEKGRLCKS ADYMNLHFKV KWLHNEYVRD LPALQGQVPE YPAWFEQFVL QWLDENEDVS
LEFLRGALER DKKDGFQQTS EHALFSCSVV DVFTQLNQSF EIIRKLECPD PSILAHYMRR
FAKTIGKVLM QYADILSKDF PAYCTKEKLP CILMNNMQQL RVQLEKMFEA MGGKELDPEA
ADSLKELQVK LNTVLDELSM VFGNSFQVQI DECVRQMADI LGQVRGTGNA SPNARASVAQ
DADSVLRPLM DFLDGNLTLF ATVCEKTVLK RVLKELWRVV MNTMERMIVL PPLTDQTGTQ
LIFTAAKELS QLSKLKDHMV REETRNLTPK QCAVLDLALD TIKQYFHAGG NGLKKTFLEK
SPDLQSLRYA LSLYTQTTDT LIKTFVRSQT AQGSGVDDPM GEVSIQVDLF THPGTGEHKV
TVKVVAANDL KWQTAGMFRP FVEVTMVGPH QSDKKRKFTT KSKSNNWSPK YNETFHFLLG
NEEGPEAYEL QICVKDYCFA REDRVIGLAV MPLRDVATKG SCACWCPLGR KIHMDETGMT
ILRILSQRSN DEVAREFVKL KSESRSTEEG S
//
