Rabphilin-3A - Rattus norvegicus (Rat)

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P47709 (RP3A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Rabphilin-3A

Alternative name(s):
Exophilin-1

Gene names

Name:

Rph3a

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	684 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.
Subunit structure	Monomer.
Subcellular location	Cell junction › synapse By similarity.
Tissue specificity	Specifically expressed in brain.
Sequence similarities	Contains 2 C2 domains. Contains 1 FYVE-type zinc finger. Contains 1 RabBD (Rab-binding) domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell junction Synapse
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	brain development Inferred from expression pattern. Source: RGD intracellular protein transport Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from direct assay. Source: RGD extrinsic to membrane Inferred from direct assay Ref.1. Source: RGD protein complex Inferred from direct assay. Source: RGD secretory granule Inferred from direct assay. Source: RGD synaptic vesicle membrane Inferred from direct assay Ref.1. Source: RGD synaptosome Inferred from direct assay. Source: RGD
Molecular function	Rab GTPase binding Inferred from electronic annotation. Source: InterPro calcium ion binding Inferred from direct assay. Source: RGD inositol 1,4,5 trisphosphate binding Inferred from direct assay. Source: RGD phosphate ion binding Inferred from direct assay. Source: RGD phosphatidylinositol-4,5-bisphosphate binding Inferred from direct assay. Source: RGD protein complex binding Inferred from direct assay. Source: RGD selenium binding Inferred from direct assay Ref.2. Source: RGD transporter activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 684

684

Rabphilin-3A

PRO_0000190229

Regions

Domain

40 – 157

118

RabBD

Domain

384 – 488

105

C2 1

Domain

542 – 645

104

C2 2

Zinc finger

88 – 145

FYVE-type

Compositional bias

280 – 364

Pro-rich

Amino acid modifications

Modified residue

274

Phosphoserine By similarity

Secondary structure

684

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P47709 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 05838BC3C7A86444
Show »

FASTA

684

75,832

        10         20         30         40         50         60 
MTDTVVNRWM YPGDGPLQSN DKEQLQAGWS VHPGAQTDRQ RKQEELTDEE KEIINRVIAR 

        70         80         90        100        110        120 
AEKMETMEQE RIGRLVDRLE TMRKNVAGDG VNRCILCGEQ LGMLGSACVV CEDCKKNVCT 

       130        140        150        160        170        180 
KCGVETSNNR PHPVWLCKIC LEQREVWKRS GAWFFKGFPK QVLPQPMPIK KTKPQQPAGE 

       190        200        210        220        230        240 
PATQEQPTPE SRHPARAPAR GDMEDRRAPG QKPGPDLTSA PGRGSHGPPT RRASEARMST 

       250        260        270        280        290        300 
TTRDSEGWDH GHGGGAGDTS RSPGGEQGLR RANSVQASRP APASMPSPAP PQPVQPGPPG 

       310        320        330        340        350        360 
GSRAAPGPGR FPEQSTEAPP SDPGYPGAVA PAREERTGPT GGFQAAPHTA GPYSQAAPAR 

       370        380        390        400        410        420 
QPPPAEEEEE EANSYDSDQA TTLGALEFSL LYDQDNSNLQ CTIIRAKGLK PMDSNGLADP 

       430        440        450        460        470        480 
YVKLHLLPGA SKSNKLRTKT LRNTRNPVWN ETLQYHGITE EDMQRKTLRI SVCDEDKFGH 

       490        500        510        520        530        540 
NEFIGETRFS LKKLKANQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE QVERIGDIEE 

       550        560        570        580        590        600 
RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK KAKHKTQIKK 

       610        620        630        640        650        660 
KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA KGERLKHWYE 

       670        680 
CLKNKDKKIE RWHQLQNENH VSSD

« Hide

References

[1]	"Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C." Li C., Takei K., Geppert M., Daniell L., Stenius K., Chapman E.R., Jahn R., de Camilli P., Suedhof T.C. Neuron 13:885-898(1994) [PubMed: 7946335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A." Ostermeier C., Brunger A.T. Cell 96:363-374(1999) [PubMed: 10025402] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 44-167 IN COMPLEX WITH RAB3A. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U12571 mRNA. Translation: AAA62662.1.

IPI

IPI00189927.

PIR

I58166.

RefSeq

NP_598202.1. NM_133518.1.

UniGene

Rn.10976.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZBD	X-ray	2.60	B	41-170	[»]
2CHD	X-ray	1.92	A	371-510	[»]
2CM5	X-ray	1.28	A	519-684	[»]
2CM6	X-ray	1.85	A/B	519-684	[»]
3RPB	NMR	-	A	541-680	[»]

ProteinModelPortal

P47709.

SMR

P47709. Positions 44-167, 382-509, 541-680.

ModBase

Search...

Protein-protein interaction databases

IntAct

P47709. 1 interaction.

MINT

MINT-85841.

STRING

P47709.

PTM databases

PhosphoSite

P47709.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

171039.

KEGG

rno:171039.

UCSC

NM_133518. rat.

Organism-specific databases

CTD

22895.

RGD

620073. Rph3a.

Phylogenomic databases

eggNOG

maNOG04022.

GeneTree

ENSGT00600000084227.

HOVERGEN

HBG017739.

InParanoid

P47709.

OrthoDB

EOG4Z0B5S.

Gene expression databases

ArrayExpress

P47709.

Genevestigator

P47709.

GermOnline

ENSRNOG00000001368. Rattus norvegicus.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020477. C2_dom.
IPR018029. C2_membr_targeting.
IPR010911. Rab-bd_domain.
IPR003315. Rabphilin3A_effector_Zn-bd.
IPR001565. Synaptotagmin.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

Pfam

PF00168. C2. 2 hits.
PF02318. RPH3A_effect_N. 1 hit.
[Graphical view]

PRINTS

PR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.

SMART

SM00239. C2. 2 hits.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 2 hits.
SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

621529.

PMAP-CutDB

P47709.

Entry information

Entry name

RP3A_RAT

Accession

Primary (citable) accession number: P47709

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents