ID F6SSI2_CIOIN Unreviewed; 1518 AA.
AC F6SSI2; A0A1W2W570;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Protein unc-13 homolog B-like {ECO:0000313|Ensembl:ENSCINP00000004445.2};
GN Name=LOC100176945 {ECO:0000313|Ensembl:ENSCINP00000004445.2};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000004445.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000004445.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; EAAA01001620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002124363.1; XM_002124327.4.
DR STRING; 7719.ENSCINP00000004445; -.
DR Ensembl; ENSCINT00000004445.2; ENSCINP00000004445.2; ENSCING00000002173.2.
DR GeneID; 100176945; -.
DR KEGG; cin:100176945; -.
DR GeneTree; ENSGT00940000168389; -.
DR HOGENOM; CLU_001304_3_0_1; -.
DR InParanoid; F6SSI2; -.
DR OMA; IVMHTME; -.
DR OrthoDB; 5395569at2759; -.
DR TreeFam; TF312844; -.
DR Proteomes; UP000008144; Unassembled WGS sequence.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
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:SF12; UNC-13, ISOFORM E; 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:UP000008144};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 406..456
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 512..636
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 938..1081
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1190..1332
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1347..1474
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 195..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1518 AA; 172422 MW; E895F40A02704BC8 CRC64;
MSLLCVKVKQ GKLDGAPDKF NTYVSLKVQN VKSTTICVKG CDPLWEQDYM FEISRVDLGL
SIEIWNKGVL WDTLLGTAWL PLSHVPHCNE EGDGAWYQLY TNVNSDKGVV PDVKNATNHK
VLCDVRFELP CELSENEVVM LQQKLDEFNE YQDDTWMVDP FSSTLNKSNA TSSISIDSDY
RSDVSVVGSY QTVQHANASS SQHREARALK KPKAGSLTTD EADSYSREYG SDTESFDSRC
QRYGSEEDAE ADRQVGQEDV GLVLKHESYE DSPPKIPDDL ANSAGDMSFS SAKFKWIHAF
NRVRIGLNGE REDQLGELHC SRKASLWNIG ANSSFYTSID SMPDIRPRKK SIPLVSDLSI
AMIKRQTGIT SALVTSRASL NDEDLKLHVY KKTLQALIYP ISCTTPHKFA IWSASTPTYC
YECEGLLWGI ARQGLRCSEC GVKCHEKCRD LLNADCLHRA AEKSSKHGAE DKTQHIITSM
KDRMKVRENS CPQLFQLMKS VFDVNYDSHH ILMESAKQCV LDGTSKWSAK LSITVISAQG
LQAKDKTGSS DPYVTVQVGK TRKRTKTIYG DLNPLWNENF HFECHNSTDR IKVRVWDEDD
DIKSVLKQQF KRESDDFLGQ TIIEVRTLSG EMDVWYNLEK RTDKSAVSGA IRLHINMEIK
GEEKVAPYHL QYTCLHENLF HYTCKQNNDM VKIPKMDGEE SWKVYFDGQQ QEIVDEFAMR
YGVESIYQAM THFSCLSSKY KSSGAPAVMS ALLANINAYY AHTSPTTHIS ASNRFAASNF
GTERFVKLLD QLHNSLRIDL SMYRKHFPAS KPEKLIDLKS TVDLLTSITF FRMKVQELQS
PPRAGQVVKD CCKACIRSTY GYVFSNCSEI SQTDKTEEGP EEGGPRIDDL DFWTQLITLM
VSVIEEDKNI YTNYLNQFPS EFNVGQVCAG EMWKMFSEDL EKGLLEHAQH RLCKTTDYMN
LQFKVKWLYK EYVAPLDMFQ DAVPEYSQWF EPFTMDWLDV NEKLSMDFLS GAYERDRRDS
FQQSSEHALF SCSVVDIFTQ LNQSYDIIKK LECPDPQVVN QFMTKFAKTI EKVLDTYAEM
VSKDFPKLCA KEDTACVLMN NIQQLRVLLE NLFRNMGGEQ LDSVTSDILK SLQVKLNVRL
GELSEIFGQS FTQRIDNSIK AMGNLLCKIK GNANISIQQR SSDNIAHEAD NVLRPLMDLL
NGSLEMFAKT CEKTVLKHVL KELWKLVVKS LETSIVLPPL NDITGSQLLR NAAKEISQFS
KFRDLAREDV SRNLSPRQCY ILDASLDSIK QYFHAGGKGL RKNYLEKSEE LQSLKYALSL
YTQTTDSLIK TFIETQTTQD EPSVESPQGE VSIQVDIYTH PGTGENKLTI KVVAASNLKW
NTTGMFRPFV DVNLVGPHLS NVRRRYSTKS RSNAWSPKYN ESFSYSIGNV EKISAYELHL
CVKDYCFARD DRVIGVAVMQ LRNISQQGSC ACWCSLGKNI HLNQTGWTVL RILSQRAGDE
IAKEFVQLKS STRSLEEA
//