P63041 (CPLX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complexin-1

Alternative name(s):
Complexin I
Short name=CPX I
Synaphin-2

Gene names

Name:

Cplx1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells By similarity.
Subunit structure	Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. Ref.1 Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm › cytosol. Note: Enriched at synaptic-releasing sites in mature neurons. Ref.1 Ref.4 Ref.8
Tissue specificity	Nervous system. Strongly expressed in brain, where it is predominant in neurons from cerebral cortex and thalamus (at protein level). Ref.1 Ref.2 Ref.5 Ref.8
Sequence similarities	Belongs to the complexin/synaphin family.

Ontologies

Keywords
Biological process	Exocytosis Neurotransmitter transport Transport
Cellular component	Cytoplasm
Domain	Coiled coil
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	synaptic vesicle exocytosis Inferred from direct assay Ref.7. Source: RGD
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from direct assay Ref.1. Source: MGI neuronal cell body Inferred from direct assay Ref.1. Source: MGI synapse Inferred from direct assay Ref.1. Source: MGI synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Inferred from direct assay Ref.1. Source: MGI
Molecular function	syntaxin-1 binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 134

134

Complexin-1

PRO_0000144872

Regions

Region

48 – 70

23

Interaction with the SNARE complex

Coiled coil

29 – 64

36

Potential

Secondary structure

1

.

.

.

134

Helix Strand Turn

Details...

Helix

35 – 70

36

Sequences

	Sequence		Length	Mass (Da)
	P63041 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: BA1B6F074923A3A4	FASTA	134	15,122
	10 20 30 40 50 60 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE 70 80 90 100 110 120 VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEPE EEDESILDTV 130 IKYLPGPLQD MFKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complexins: cytosolic proteins that regulate SNAP receptor function." McMahon H.T., Missler M., Li C., Suedhof T.C. Cell 83:111-119(1995) [PubMed: 7553862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-49; 55-69 AND 74-96, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT. Tissue: Brain.
[2]	"Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex." Ishizuka T., Saisu H., Odani S., Kumanishi T., Abe T. Neuroscience 88:295-306(1999) [PubMed: 10051208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Brain.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Regulatory roles of complexins in neurotransmitter release from mature presynaptic nerve terminals." Ono S., Baux G., Sekiguchi M., Fossier P., Morel N.F., Nihonmatsu I., Hirata K., Awaji T., Takahashi S., Takahashi M. Eur. J. Neurosci. 10:2143-2152(1998) [PubMed: 9753100] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Immunohistochemical distribution of the two isoforms of synaphin/complexin involved in neurotransmitter release: localization at the distinct central nervous system regions and synaptic types." Yamada M., Saisu H., Ishizuka T., Takahashi H., Abe T. Neuroscience 93:7-18(1999) [PubMed: 10430466] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions." Pabst S., Hazzard J.W., Antonin W., Suedhof T.C., Jahn R., Rizo J., Fasshauer D. J. Biol. Chem. 275:19808-19818(2000) [PubMed: 10777504] [Abstract] Cited for: SUBUNIT.
[7]	"Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis." Pabst S., Margittai M., Vainius D., Langen R., Jahn R., Fasshauer D. J. Biol. Chem. 277:7838-7848(2002) [PubMed: 11751907] [Abstract] Cited for: SUBUNIT.
[8]	"Structurally and functionally unique complexins at retinal ribbon synapses." Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C., Dresbach T., Hofmann K., Brose N. J. Cell Biol. 169:669-680(2005) [PubMed: 15911881] [Abstract] Cited for: SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[9]	"Three-dimensional structure of the complexin/SNARE complex." Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J. Neuron 33:397-409(2002) [PubMed: 11832227] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-83 IN COMPLEX WITH STX1A; SNAP25 AND VAMP2, STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U35098 mRNA. Translation: AAC52270.1.
D70817 mRNA. Translation: BAA11097.1.
BC093605 mRNA. Translation: AAH93605.1.

IPI

IPI00210978.

PIR

A57233.

RefSeq

NP_074055.1. NM_022864.2.

UniGene

Rn.10133.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KIL	X-ray	2.30	E	26-72	[»]

ProteinModelPortal

P63041.

SMR

P63041. Positions 32-72.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63041. 3 interactions.

STRING

P63041.

PTM databases

PhosphoSite

P63041.

Proteomic databases

PRIDE

P63041.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000061720; ENSRNOP00000058432; ENSRNOG00000000060.

GeneID

64832.

KEGG

rno:64832.

UCSC

NM_022864. rat.

Organism-specific databases

CTD

10815.

RGD

70944. Cplx1.

Phylogenomic databases

eggNOG

maNOG20874.

GeneTree

ENSGT00490000043416.

HOVERGEN

HBG062792.

InParanoid

P63041.

OMA

SIVDTVM.

OrthoDB

EOG44MXTP.

Gene expression databases

ArrayExpress

P63041.

Genevestigator

P63041.

GermOnline

ENSRNOG00000000060. Rattus norvegicus.

Family and domain databases

InterPro

IPR008849. Synaphin.
[Graphical view]

KO

K15294.

PANTHER

PTHR16705. Synaphin. 1 hit.

Pfam

PF05835. Synaphin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

613760.

Entry information

Entry name

CPLX1_RAT

Accession

Primary (citable) accession number: P63041
Secondary accession number(s): O09057 , O09142, Q566D7, Q64276

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program