ID   CPLX3_BOVIN             Reviewed;         158 AA.
AC   Q0IIE0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Complexin-3;
DE   Flags: Precursor;
GN   Name=CPLX3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Complexin that regulates SNARE protein complex-mediated
CC       synaptic vesicle fusion (By similarity). Required for the maintenance
CC       of synaptic ultrastructure in the adult retina (By similarity).
CC       Positively regulates synaptic transmission through synaptic vesicle
CC       availability and exocytosis of neurotransmitters at photoreceptor
CC       ribbon synapses in the retina (By similarity). Suppresses tonic
CC       photoreceptor activity and baseline 'noise' by suppression of Ca(2+)
CC       vesicle tonic release and the facilitation of evoked synchronous and
CC       asynchronous Ca(2+) vesicle release (By similarity).
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q8R1B5}. Cell
CC       membrane; Lipid-anchor {ECO:0000250|UniProtKB:Q8R1B5}. Note=Enriched at
CC       the synaptic terminal (By similarity). Localized at glycinergic
CC       synaptic contacts of AII amacrine cells with OFF cone bipolar cells in
CC       the OFF sublamina of the retina inner nuclear layer (By similarity).
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- PTM: Farnesylation mediates presynaptic targeting.
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; BC122691; AAI22692.1; -; mRNA.
DR   RefSeq; NP_001071357.1; NM_001077889.1.
DR   AlphaFoldDB; Q0IIE0; -.
DR   SMR; Q0IIE0; -.
DR   STRING; 9913.ENSBTAP00000028562; -.
DR   PaxDb; Q0IIE0; -.
DR   PRIDE; Q0IIE0; -.
DR   Ensembl; ENSBTAT00000028562; ENSBTAP00000028562; ENSBTAG00000021426.
DR   GeneID; 509248; -.
DR   KEGG; bta:509248; -.
DR   CTD; 594855; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021426; -.
DR   VGNC; VGNC:27653; CPLX3.
DR   eggNOG; ENOG502QZ0D; Eukaryota.
DR   GeneTree; ENSGT00950000182938; -.
DR   InParanoid; Q0IIE0; -.
DR   OMA; QSAEKCY; -.
DR   OrthoDB; 1441014at2759; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000021426; Expressed in retina and 28 other tissues.
DR   GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; PTHR16705; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Exocytosis; Lipoprotein; Membrane; Methylation;
KW   Neurotransmitter transport; Prenylation; Reference proteome;
KW   Sensory transduction; Synapse; Transport; Vision.
FT   CHAIN           1..155
FT                   /note="Complexin-3"
FT                   /id="PRO_0000290029"
FT   PROPEP          156..158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000290030"
FT   REGION          13..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..74
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         155
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B5"
FT   LIPID           155
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B5"
SQ   SEQUENCE   158 AA;  17625 MW;  D908604A6DB6EA0F CRC64;
     MAFMVKTMVG GQLKNLTGSL GGGEDKGDGD KSAAEAQGMS REEYEEYQKQ LVEEKMERDA
     QFTQRKAERA TLRSHFRDKY RLPKNETDES QIQMAGGDVE LPRELAKMIE EDTEEEEERA
     SVLGQLASLP GLDLGSLKDK AHSTLGDLKQ SAEKCHIM