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O35412 (SI1L1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal-induced proliferation-associated 1-like protein 1

Short name=SIPA1-like protein 1
Alternative name(s):
SPA-1-like protein p1294
Spine-associated Rap GTPase-activating protein
Short name=SPAR
Gene names
Name:Sipa1l1
Synonyms:Spa1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1822 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis. Ref.2

Subunit structure

Interacts (via PDZ domain) with EPHA4 (via PDZ motif); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases By similarity. Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin cytoskeleton. Ref.2 Ref.3 Ref.7

Subcellular location

Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapsesynaptosome. Note: Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons. Ref.2 Ref.3

Tissue specificity

Detected in brain (at protein level). Ref.2 Ref.3

Post-translational modification

Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2. Ref.5 Ref.6 Ref.8

Phosphorylated at Ser-1367 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome. Ref.4 Ref.5 Ref.6 Ref.8

Sequence similarities

Contains 1 PDZ (DHR) domain.

Contains 1 Rap-GAP domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
Synaptosome
   DomainCoiled coil
   Molecular functionGTPase activation
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay Ref.2. Source: UniProtKB

activation of Rap GTPase activity

Inferred from direct assay Ref.2. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rap GTPase activity

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dendrite morphogenesis

Inferred from mutant phenotype PubMed 15703396. Source: RGD

regulation of dendritic spine morphogenesis

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of synaptic plasticity

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

dendritic spine

Inferred from direct assay Ref.2. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 12059963. Source: RGD

postsynaptic density

Inferred from direct assay Ref.2Ref.3. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex

Inferred from direct assay PubMed 15823548. Source: RGD

   Molecular_functionGTPase activator activity

Traceable author statement PubMed 12059963. Source: RGD

actin filament binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.3Ref.7. Source: UniProtKB

protein complex binding

Inferred from physical interaction Ref.5. Source: RGD

protein kinase binding

Inferred from physical interaction Ref.6Ref.8. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from direct assay Ref.5. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18221822Signal-induced proliferation-associated 1-like protein 1
PRO_0000056748

Regions

Domain638 – 855218Rap-GAP
Domain992 – 106877PDZ
Coiled coil1753 – 181361 Potential
Compositional bias93 – 12937Ser-rich
Compositional bias1153 – 1486334Ser-rich

Amino acid modifications

Modified residue1621Phosphoserine By similarity
Modified residue2881Phosphoserine By similarity
Modified residue12201Phosphoserine By similarity
Modified residue12731Phosphoserine By similarity
Modified residue12881Phosphoserine By similarity
Modified residue13441Phosphoserine; by PLK2 Ref.5
Modified residue13481Phosphothreonine; by PLK2 Ref.5
Modified residue13671Phosphoserine; by CDK5 Ref.6
Modified residue14491Phosphoserine By similarity
Modified residue14511Phosphoserine By similarity
Modified residue15671Phosphoserine By similarity
Modified residue15691Phosphothreonine By similarity
Modified residue15721Phosphoserine By similarity
Modified residue15831Phosphoserine By similarity
Modified residue15861Phosphoserine By similarity
Modified residue16031Phosphoserine By similarity
Modified residue17521Phosphoserine By similarity

Experimental info

Mutagenesis7431R → A: Decreases stimulation of the GTPase activity of RAP2A. Ref.2
Mutagenesis846 – 8472RT → AS: Abolishes stimulation of the GTPase activity of RAP2A.
Mutagenesis13441S → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1348. Ref.5
Mutagenesis13481T → A: Abolishes ubiquitination and degradation by the proteasome; when associated with A-1344. Ref.5
Mutagenesis13671S → A: Abolishes phosphorylation by CDK5 and subsequent phosphorylation by PLK2, leading to prevent ubiquitination and degradation by the proteasome. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O35412 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 479821CE8820B4FD

FASTA1,822201,925
        10         20         30         40         50         60 
MTSLKRSQTE RPVTADRASV VSTDGTPKVH TDDFYMRRFR SQNGSLGSSV MAAVGPPRSE 

        70         80         90        100        110        120 
GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI ETSSCLESLS SKGSPVSQGS 

       130        140        150        160        170        180 
SVSLNSNDSA MLKSIQNTLK NKTGPAESMD SRFLMPEAYP SSPRKALRRI RQRSNSDITI 

       190        200        210        220        230        240 
SELDVDSFDE CISPTYKSGP SLHREYGSTS SIDKQGTSGE SFFGLLKGYK DDRADRGPTP 

       250        260        270        280        290        300 
TKLSDFLITG GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR 

       310        320        330        340        350        360 
NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR HNVIKRRNTT 

       370        380        390        400        410        420 
TGASAAAVAS LVSGPLSHST SFSSPMGSTE DFNSKGSLGM DQGDDKSNEL VMSCPYFRNE 

       430        440        450        460        470        480 
IGGEGERKIS LSKSNSGSFS GCESTSFESA LSSHCTNAGV AVLEVPKESL MLHLDRVRRY 

       490        500        510        520        530        540 
TVEHVDLGAY YYRKCFYQKE HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR 

       550        560        570        580        590        600 
TSELMTLRGS VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM 

       610        620        630        640        650        660 
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN TPKVTEQFMK LDEQGLNYQQ KVGIMYCKAG 

       670        680        690        700        710        720 
QSTEEEMYNN ESAGPAFEEF LQLLGERVRL KGFEKYRAQL DTKTDSTGTH SLYTTYKDYE 

       730        740        750        760        770        780 
IMFHVSTMLP YTPNNKQQLL RKRHIGNDIV TIVFQEPGAQ PFSPKNIRSH FQHVFVIVRA 

       790        800        810        820        830        840 
HNPCTESVCY SVAVTRSRDV PSFGPPIPKG VTFPKSNVFR DFLLAKVINA ENAAHKSEKF 

       850        860        870        880        890        900 
RAMATRTRQE YLKDLAEKNV TNTPIDPSGK FPFISLASKK KEKSKPYPGA ELSSMGAIVW 

       910        920        930        940        950        960 
AVRAKDYNKA MEFDCLLGIS NEFIVLIEQE TKSVVFNCSC RDVIGWTSSD SSLKIFYERG 

       970        980        990       1000       1010       1020 
ECISVESFMS SEDIKEIVKR LQFVSKGCES VEMTLRRNGL GQLGFHVNYE GIVADVEPYG 

      1030       1040       1050       1060       1070       1080 
YAWQAGLKQG SRLVEICKVA VATLSHEQMI DLLRTSVTVK VVIIPPHDDC TPRRSCSETY 

      1090       1100       1110       1120       1130       1140 
RMPVMEYKMN EGVSYEYKFP FRSNNKWQRN AGKGAHSPQV PLQLQSPMIS RVNAGKGDGK 

      1150       1160       1170       1180       1190       1200 
MPLPERAANI PRSISSDGRP LERRLSPGSD IYVTVSSMAL ARSQCRNSPS NLSSSSETGS 

      1210       1220       1230       1240       1250       1260 
GGGTYRQKSM PEGFGVSRRS PASIDRQNTQ SDIGGSGKST PSWQRSEDSL ADQMEPTCHL 

      1270       1280       1290       1300       1310       1320 
PAVSKVLPAF RESPSGRLMR QDPVVHLSPN KQGHSDSHYS SHSSSNTLSS NASSAHSDEK 

      1330       1340       1350       1360       1370       1380 
WYDGDRTESD LNSYNYLQGT SADSGIDTAS YGLSHGSTAS LGASTSSPRS GPGKEKVAPL 

      1390       1400       1410       1420       1430       1440 
WHSSSEVLSL ADRTLETEGH GMDRKTESSL SLDIHSKSQG GSSPLTRENS TFSINDATSH 

      1450       1460       1470       1480       1490       1500 
TSTMSSRHSA SPVVFSSARS SPKEELHPTT SSQLAPSFSS SSSSSSGPRT FYPRQGATSK 

      1510       1520       1530       1540       1550       1560 
YLIGWKKPEG TINSVGFMDT RKRHQSDGNE IAHTRLRAST RDLRASPKPT SKSTIEEDLK 

      1570       1580       1590       1600       1610       1620 
KLIDLESPTP ESQKNFKFHG LSSPQSPFPS TPTSRRALHR TLSDESIYSS QREHFFTSRA 

      1630       1640       1650       1660       1670       1680 
SLLDQALPND VFFSSTYPSL PKSLPLRRPS YTLGMKSLHG EFFASDSSLT DIQETRRQPI 

      1690       1700       1710       1720       1730       1740 
PDPGLMPLPD TASDLDWSNL VDAAKAYEVQ RASFFAASDE NHRPLSAASN SDQLEEQALV 

      1750       1760       1770       1780       1790       1800 
QMKSYSSSKD SSPTLASKVD QLEGMLKMLR EDLKKEKEDK AHLQAEVEHL REDNLRLQEE 

      1810       1820 
SQNASDKLKK FTEWVFNTID MS 

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References

[1]Takeuchi M., Ide N., Hata Y., Takai Y.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP."
Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M.
Neuron 31:289-303(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DLG4, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-743 AND 846-ARG-THR-847, TISSUE SPECIFICITY.
[3]"ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the scaffolding protein ProSAP2/Shank3."
Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H., Proepper C., Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.
J. Biol. Chem. 281:13805-13816(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LZTS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"The EphA4 receptor regulates neuronal morphology through SPAR-mediated inactivation of Rap GTPases."
Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.
J. Neurosci. 27:14205-14215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the SCFbeta-TRCP ubiquitin ligase in hippocampal neurons."
Ang X.L., Seeburg D.P., Sheng M., Harper J.W.
J. Biol. Chem. 283:29424-29432(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1344 AND THR-1348, UBIQUITINATION, MUTAGENESIS OF SER-1344 AND THR-1348.
[6]"Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity."
Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M.
Neuron 58:571-583(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1367, UBIQUITINATION, MUTAGENESIS OF SER-1367.
[7]"Postsynaptic PDLIM5/Enigma homolog binds SPAR and causes dendritic spine shrinkage."
Herrick S., Evers D.M., Lee J.Y., Udagawa N., Pak D.T.
Mol. Cell. Neurosci. 43:188-200(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDLIM5 AND PDLIM7.
[8]"Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory."
Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.
Neuron 69:957-973(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, UBIQUITINATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026504 mRNA. Translation: AAB81526.1.
PIRT14106.
RefSeqNP_647546.1. NM_139330.1.
UniGeneRn.10835.

3D structure databases

ProteinModelPortalO35412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid251530. 6 interactions.
STRING10116.ENSRNOP00000010626.

PTM databases

PhosphoSiteO35412.

Proteomic databases

PaxDbO35412.
PRIDEO35412.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID246212.
KEGGrno:246212.
UCSCRGD:708497. rat.

Organism-specific databases

CTD26037.
RGD708497. Sipa1l1.

Phylogenomic databases

eggNOGNOG279955.
HOGENOMHOG000154319.
HOVERGENHBG056135.
InParanoidO35412.
KOK17701.
PhylomeDBO35412.

Gene expression databases

GenevestigatorO35412.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR021818. DUF3401.
IPR001478. PDZ.
IPR000331. Rap_GAP_dom.
[Graphical view]
PfamPF11881. DUF3401. 1 hit.
PF00595. PDZ. 1 hit.
PF02145. Rap_GAP. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio623491.

Entry information

Entry nameSI1L1_RAT
AccessionPrimary (citable) accession number: O35412
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families