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Database: UniProt
Entry: G3WAW1_SARHA
LinkDB: G3WAW1_SARHA
Original site: G3WAW1_SARHA 
ID   G3WAW1_SARHA            Unreviewed;      1697 AA.
AC   G3WAW1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Protein unc-13 homolog A {ECO:0008006|Google:ProtNLM};
GN   Name=UNC13A {ECO:0000313|Ensembl:ENSSHAP00000012566.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000012566.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000012566.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000012566.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 9305.ENSSHAP00000012566; -.
DR   Ensembl; ENSSHAT00000012670.2; ENSSHAP00000012566.2; ENSSHAG00000010759.2.
DR   eggNOG; KOG1011; Eukaryota.
DR   GeneTree; ENSGT00940000154929; -.
DR   HOGENOM; CLU_001304_3_0_1; -.
DR   TreeFam; TF312844; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
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:SF1; PROTEIN UNC-13 HOMOLOG A; 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:UP000007648};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..97
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          545..595
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          651..775
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1085..1228
FT                   /note="MHD1"
FT                   /evidence="ECO:0000259|PROSITE:PS51258"
FT   DOMAIN          1337..1479
FT                   /note="MHD2"
FT                   /evidence="ECO:0000259|PROSITE:PS51259"
FT   DOMAIN          1512..1639
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          181..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1672..1697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..360
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1697 AA;  192567 MW;  824B059FF553F15D CRC64;
     MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG NLPCWEQDFM FEINRLDLGL
     TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQVIMTDNEI CGTKDPTFHR
     ILLDTRFELP LDIPEEEARY WAKKLEQLNA MRDQDDYSFQ EEQDKPLPVP SSQCCNWSYF
     GWGEQQNEDP DSAVDDRDSD YRSETSNSIP PPYYTTSQPN ASVHQYSVRP PPLGSRDSRD
     SYSDSMRSYE DYSEAPPVSP TGSSRYASSG ELSQGSSQLS EDFDPDDQSL QGSEIEEERD
     RDSYHSCHSS VSYHKDSPHW DQNEEEEEED LEEEEEEDLE EEDLEDLEDL EDEELRQEGY
     SENEEEYSKE ESYPPTAPTT SEREEKPSPV STEVPEVAKM PPEPAGAEEV PGAERAPEPE
     PPKLEERARE DEEGQDSMSR AKANWLRVFN KVRMQLQEAR GEGDMSNSLW FKGGPGGGLI
     IIDSMPDIRK RKPIPLVSDL SLVQSRKAGI TSALASSTLN NEELKNHVYK KTLQALIYPI
     SCTTPHNFEV WTATTPTYCY ECEGLLWGIA RQGMRCTECG VKCHEKCQDL LNADCLQRAA
     EKSSKHGAED RTQNIIMVLK DRMKIRERNK PEIFELIQEI FAVSKTTHTQ QMKAVKQSVL
     DGTSKWSAKI SITVVCAQGL QAKDKTGSSD PYVTVQVGKT KKRTKTIYGN LNPVWEENFH
     FECHNSSDRI KVRVWDEDDD IKSRVKQRFK RESDDFLGQT IIEVRTLSGE MDVWYNLDKR
     TDKSAVSGAI RLHISVEIKG EEKVAPYHVQ YTCLHENLFH FVTDVQNSGA VRIPDAKGDD
     AWKVYYDETA QEIVDEFAMR YGVESIYQAM THFACLSSKY MCPGVPAVMS TLLANINAYY
     AHTTASTNVS ASDRFAASNF GKERFVKLLD QLHNSLRIDL SMYRNNFPAS SPERLQDLKS
     TVDLLTSITF FRMKVQELQS PPRASQVVKD CVKACLNSTY EYIFNNCHEL YSREYQTDPA
     KKGEVPPEEQ GPSIKNLDFW SKLITLIVSI IEEDKNSYTP CLNQFPQELN VGKISAEVMW
     NLFAQDMKYA MEEHDKHRLC KSADYMNLHF KVKWLYNEYV TELPSFKDRV PEYPAWFEPF
     VIQWLDENEE VSRDFLHGAL ERDKKDGFQQ TSEHALFSCS VVDVFSQLNQ SFEIIKKLEC
     PDPQIVGHYM RRFAKTISNV LLQYAEIISK DFTTYCSKEK EKVPCILMNN TQQLRVQLEK
     MFEAMGGKEL DAEASDILKE LQVKLNNVLD ELSRLFATSF QPHIEECVKQ MGDILSQVKG
     TGNVPASACS SVAQDADNVL QPIMDLLDSN LTLFAKICEK TVLKRVLKEL WKLVMNTMEK
     TIVLPPLTDQ TGTQMIFNAA KELGQLSKLK DHMVREEAKS LTPKQCAVVE LALDTIKQYF
     HAGGVGLKKT FLEKSPDLQS LRYALSLYTQ ATDLLIKTFV QTQSAQVHGG KGIRFTLSEE
     IYPEKGSGVD DPVGEVSVHV ELFTHPGTGE HKVTVKVVAA NDLKWQTSGI FRPFIEVNII
     GPQLSDKKRK FATKSKNNSW APKYNETFQF TLSADAGPEC YELQVCVKDY CFAREDRTVG
     LAVLQLKELL QRGSCACWLP LGRRIHMDDT GLTVLRILSQ RSNDEVAKEF VKLKSDTRSA
     EEGGAGPGPG SGQGPGP
//
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