DOC2G_MOUSE
ID DOC2G_MOUSE Reviewed; 387 AA.
AC Q9ESN1; Q6P8R8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Double C2-like domain-containing protein gamma;
DE Short=Doc2-gamma;
GN Name=Doc2g;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11027523; DOI=10.1006/bbrc.2000.3520;
RA Fukuda M., Mikoshiba K.;
RT "Doc2g, a third isoform of double C2 protein, lacking calcium-dependent
RT phospholipid binding activity.";
RL Biochem. Biophys. Res. Commun. 276:626-632(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in regulation of vesicular trafficking. In
CC vitro, does not bind calcium and phospholipids.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
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DR EMBL; AB046665; BAB16686.1; -; mRNA.
DR EMBL; BC061104; AAH61104.1; -; mRNA.
DR CCDS; CCDS29409.1; -.
DR PIR; JC7398; JC7398.
DR RefSeq; NP_068563.2; NM_021791.3.
DR AlphaFoldDB; Q9ESN1; -.
DR SMR; Q9ESN1; -.
DR STRING; 10090.ENSMUSP00000025806; -.
DR iPTMnet; Q9ESN1; -.
DR PhosphoSitePlus; Q9ESN1; -.
DR PaxDb; Q9ESN1; -.
DR PRIDE; Q9ESN1; -.
DR ProteomicsDB; 277486; -.
DR DNASU; 60425; -.
DR GeneID; 60425; -.
DR KEGG; mmu:60425; -.
DR UCSC; uc008fyd.1; mouse.
DR CTD; 60425; -.
DR MGI; MGI:1926250; Doc2g.
DR eggNOG; KOG1013; Eukaryota.
DR InParanoid; Q9ESN1; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; Q9ESN1; -.
DR TreeFam; TF351844; -.
DR BioGRID-ORCS; 60425; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Doc2g; mouse.
DR PRO; PR:Q9ESN1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ESN1; protein.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IGI:MGI.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR014638; Doc2.
DR InterPro; IPR030536; Doc2g.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR001565; Synaptotagmin.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF7; PTHR45729:SF7; 1.
DR Pfam; PF00168; C2; 2.
DR PIRSF; PIRSF036931; Doc2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..387
FT /note="Double C2-like domain-containing protein gamma"
FT /id="PRO_0000079971"
FT DOMAIN 83..209
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 243..376
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 11..12
FT /note="HG -> QR (in Ref. 2; AAH61104)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> M (in Ref. 2; AAH61104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43347 MW; F1A6EF317906EBE1 CRC64;
MACAGPASGR HGVSMQEHMA IDVSPGPIRP IRLISNYFPH FYPFLEPVLR APDRQAMLAP
AIPSAPQLQP NPEPEGDSDD STALGTLEFT LLFDEDNSAL HCTAHRAKGL KPPAAGSVDT
YVKANLLPGA SKASQLRTRT VRGTREPVWE ETLTYHGFTC QDAGRKTLRL CVCEDSRLRR
RRRGPPLGEL RVPLRKLVPN RARSFDICLE KRKLTKRPKS LDTARGMSLY EEEEVEAEVF
GEERGRILLS LCYSSERGGL LVGVLRCVHL APMDANGYSD PFVRLFLHPS SGKKSKYKTS
VRRKTLNPEF NEEFFYAGHR EELAQKALLV SVWDYDLGTA DDFIGGVQLS GRASGERLRH
WRECLGHCDH RLELWHLLDS VPPQLGD
