[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF ARG-938; TYR-1399 AND TYR-1404, PHOSPHORYLATION AT TYR-1399 AND TYR-1404, AND SUBCELLULAR LOCATION. STRAIN=NIH Swiss; TISSUE=Embryo; DOI=10.1242/jcs.01526; PubMed=15546919 [NCBI, ExPASy, EBI, Israel, Japan] Stacey T.T.I., Nie Z., Stewart A., Najdovska M., Hall N.E., He H., Randazzo P.A., Lock P.; "ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner."; J. Cell Sci. 117:6071-6084(2004).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). STRAIN=C57BL/6; TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-1538 (ISOFORM 3). TISSUE=Brain; Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.; "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."; Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1404, AND MASS SPECTROMETRY. TISSUE=Mast cell; PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan] Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.; "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."; J. Immunol. 179:5864-5876(2007).

Comments

FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts preferentially on ARF5 and on RHOA.
SUBUNIT: Interacts with INPPL1/SHIP2 (By similarity).
INTERACTION:
P07948:LYN (xeno); NbExp=2; IntAct=EBI-621463, EBI-79452;
P12931:SRC (xeno); NbExp=3; IntAct=EBI-621463, EBI-621482;
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Note=Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q8R5G7-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	ARAP3 delta-SAM
Isoform ID	Q8R5G7-2
Features which should be applied to build the isoform sequence: VSP_015003.

Name	3
Isoform ID	Q8R5G7-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_015002, VSP_015004.

PTM: Tyrosine phosphorylated at a low basal level. PDGF treatment stimulates phosphorylation. Tyrosine phosphorylation is increased in cells that are in the process of becoming attached to a substrate and that start spreading and flattening.
SIMILARITY: Contains 1 Arf-GAP domain.
SIMILARITY: Contains 5 PH domains.
SIMILARITY: Contains 1 Ras-associating domain.
SIMILARITY: Contains 1 Rho-GAP domain.
SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF469621; AAL78677.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF469622; AAL78678.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068145; AAH68145.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK220486; BAD90507.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_631945.2; -.

UniGene

Mm.247642

3D structure databases

ModBase

Q8R5G7.

Protein-protein interaction databases

IntAct

Q8R5G7; -.

PTM databases

PhosphoSite

Q8R5G7; -.

Organism-specific databases

MGI

MGI:2147274; Centd3.

Gene expression databases

ArrayExpress

Q8R5G7; -.

CleanEx

MM_CENTD3; -.

GermOnline

ENSMUSG00000024451; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005856;	Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-KW).
GO:0030027;	Cellular component: lamellipodium (inferred from direct assay from MGI).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0001726;	Cellular component: ruffle (inferred from direct assay from MGI).
GO:0008060;	Molecular function: ARF GTPase activator activity (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005100;	Molecular function: Rho GTPase activator activity (inferred from direct assay from MGI).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0030336;	Biological process: negative regulation of cell migration (inferred from direct assay from MGI).
GO:0035021;	Biological process: negative regulation of Rac protein signal transduction (inferred from direct assay from MGI).
GO:0035024;	Biological process: negative regulation of Rho protein signal transduction (inferred from direct assay from MGI).
GO:0032312;	Biological process: regulation of ARF GTPase activity (inferred from electronic annotation from InterPro).
GO:0008360;	Biological process: regulation of cell shape (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001164; ArfGAP.
IPR001849; PH.
IPR011993; PH_type.
IPR000159; Ras-assoc.
IPR000198; RhoGAP.
IPR001660; SAM.
IPR011510; SAM_2.
IPR013761; SAM_type.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 3.
G3DSA:1.10.555.10; RhoGAP; 1.
G3DSA:1.10.150.50; SAM_type; 1.

Pfam

PF01412; ArfGap; 1.
PF00169; PH; 3.
PF00788; RA; 1.
PF00620; RhoGAP; 1.
PF07647; SAM_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00405; REVINTRACTNG.

SMART

SM00105; ArfGap; 1.
SM00233; PH; 5.
SM00324; RhoGAP; 1.
SM00454; SAM; 1.
SMART graphical view of domain structure.

PROSITE

PS50115; ARFGAP; 1.
PS50003; PH_DOMAIN; 3.
PS50200; RA; 1.
PS50238; RHOGAP; 1.
PS50105; SAM_DOMAIN; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8R5G7.

Genome annotation databases

Ensembl

ENSMUSG00000024451; Mus musculus. [Contig view]

GeneID

106952; -.

KEGG

mmu:106952; -.

Phylogenomic databases

HOGENOM

Q8R5G7; -.

HOVERGEN

Q8R5G7; -.

Other

NextBio

358482; -.

SOURCE

Centd3; Mus musculus.

ROUGE

KIAA4097.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Phosphoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1538`	`1538`	`Centaurin-delta-3.`	`PRO_0000074216`
`DOMAIN`	`4 68`	`65`	`SAM.`
`DOMAIN`	`282 374`	`93`	`PH 1.`
`DOMAIN`	`389 478`	`90`	`PH 2.`
`DOMAIN`	`479 606`	`128`	`Arf-GAP.`
`DOMAIN`	`671 785`	`115`	`PH 3.`
`DOMAIN`	`795 901`	`107`	`PH 4.`
`DOMAIN`	`903 1084`	`182`	`Rho-GAP.`
`DOMAIN`	`1113 1206`	`94`	`Ras-associating.`
`DOMAIN`	`1219 1321`	`103`	`PH 5.`
`COMPBIAS`	`1493 1536`	`44`	`Pro-rich.`
`MOD_RES`	`1399 1399`		`Phosphotyrosine.`
`MOD_RES`	`1404 1404`		`Phosphotyrosine.`
`MOD_RES`	`1438 1438`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`1 618`		`Missing (in isoform 3).`	`VSP_015002`
`VAR_SEQ`	`1 78`		`Missing (in isoform 2).`	`VSP_015003`
`VAR_SEQ`	`1446 1538`		`KASMLGHEERIPDPPPGPPSKSSSQARGSLEEQLLQELNN` `LILRKGEPASCPESSSQPTSPQAPSPTSLPTPTPSLPTQP` `PCTSNPPSSQPLT -> GPSPFVCTMKSLKEGEG (in isoform 3).`	`VSP_015004`
`MUTAGEN`	`938 938`		`R->L: Loss of Rho GAP activity. Enhances cell spreading.`
`MUTAGEN`	`1399 1399`		`Y->F: Strongly reduces phosphorylation by CSK; when associated with F-1404.`
`MUTAGEN`	`1404 1404`		`Y->F: Strongly reduces phosphorylation by CSK; when associated with F-1399.`
`CONFLICT`	`144 144`		`H -> Q (in Ref. 1; AAL78677/AAL78678).`
`CONFLICT`	`167 167`		`R -> Q (in Ref. 1; AAL78677/AAL78678).`
`CONFLICT`	`1304 1304`		`M -> T (in Ref. 1; AAL78677/AAL78678).`
`CONFLICT`	`1500 1500`		`S -> P (in Ref. 1; AAL78677/AAL78678).`

Sequence information

Length: 1538 AA [This is the length of the unprocessed precursor]

Molecular weight: 169750 Da [This is the MW of the unprocessed precursor]

CRC64: C18DBC9305FADE6B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAPQDLDIA VWLALVHLEQ YADTFRRHGL ATAGAAQHLG HEELRHLGIS ATGHRKRILR 

        70         80         90        100        110        120 
LLRAGSAEGF LDSHLDNTME PTPSPAPDAQ PPKPVPKPRT VFGLSNPATA QRPGLSPIFW 

       130        140        150        160        170        180 
DPEVSRNSEC TQRSSPLLPS SSEHPSVPNT MEMMPNAIYF GLDLRGRAQA AQDVTPDSSQ 

       190        200        210        220        230        240 
ATVPTPAFRP TTGTVHIMDP GCLYYGVQPV GIPGASDRRD GRGVCQERAE HRQDLETRED 

       250        260        270        280        290        300 
AGYASLELPG DSILSLPTQD AETSDDLISP YASFSSTADR PVPLLSGWLD KLSPQGNYVF 

       310        320        330        340        350        360 
QRRFVQFNGR SLMYFGSDKD PFPKGVIPLT AIEMTRSSKD NKFQVITGQR VFVFRTESEA 

       370        380        390        400        410        420 
QRDLWCSTLQ SCLKEQRLLG HPRPPHPPRP LRTGTLELRG HKAKVFAALI PGELALYKSE 

       430        440        450        460        470        480 
QAFSLGIGIC FIELQGCSVR ETKSRSFDLL TPHRCFSFTA ESGGARQSWA AALQEAVTET 

       490        500        510        520        530        540 
LSDYEVAEKV WSNPANRHCA DCRASRPDWA AVNLGVVICK QCAGQHRALG SGISKVQSLK 

       550        560        570        580        590        600 
LDTSVWSNEI VQLFIVLGND RANCFWAGAL PPGEGLHPDS APGPRGEFIS RKYKLGLFRK 

       610        620        630        640        650        660 
PHPRHPDHSQ LLQALCAAMA GPNLLKNMAQ LLCVETSEGE EPLSPSALNG SLLSLLPSDS 

       670        680        690        700        710        720 
PGVYNEVVVP ATYRGFLYCG SISNKAGAPP LRRGRDAPPR LWCVLGAALE MFASESSPEP 

       730        740        750        760        770        780 
LSLLQPQDIV CLGVSPPPAD PGDLDRFPFS FELILTGGRI QHFATDGADS LEAWISAVGK 

       790        800        810        820        830        840 
WFSPLSCHQL LGPGLLRMGR LWLRSPSHAG LAPGLWLSGF GLLRGDHLFL CPAPGPGPPA 

       850        860        870        880        890        900 
PEDMVHLRRL QEISVVSAAD TPDKKEHLVL VETGRTLYLQ GEGRLDFAAW NTAIGGAAGG 

       910        920        930        940        950        960 
GGTGLQEQQM SRGDIPIIVD ACISFVTQHG LRLEGVYRKG GARARSLRLL AEFRRDARSV 

       970        980        990       1000       1010       1020 
KLRPREHFVE DVTDTLKRFF RELDDPVTSA RLLPRWREAA ELSQKNQRLE KYKEVISCLP 

      1030       1040       1050       1060       1070       1080 
RVNRRTLATL IGHLYRVQKC ASLNQMCTRN LALLFAPSVF QTDGRGEHEV RVLQELIDGY 

      1090       1100       1110       1120       1130       1140 
ISVFDIDSDQ AAQIDLEVSL ITTWKDVQLS QAGDLIMEVY IEQQLPDNCV TLKVSPTLTA 

      1150       1160       1170       1180       1190       1200 
EELTNQVLEM RGAASGTDLW VTFEILEHGE LERPLHPKEK VLEQALQWCQ LPEPCSASLL 

      1210       1220       1230       1240       1250       1260 
LRKVSMAHAG CLFTGVRRES PRVGLLRCRE EPPRLLGNRF QERFFLVRGR CLLLLKEKKS 

      1270       1280       1290       1300       1310       1320 
SKPEREWSLE GAKVYLGIRK KLKPPTLWGF TLILEKMHLC LSCMDEEEMW DWTTSILKAQ 

      1330       1340       1350       1360       1370       1380 
HDDQQSVVLR RRSSSDLARQ KFGTMPLLPI RGDDSGATLL SANQTLRRLH NRRTLSMFFP 

      1390       1400       1410       1420       1430       1440 
MKSPQGSVEE QDELEEPVYE EPVYEEVGAF PELTKDTTFS STWEWSAKSD PSLTSQRSFD 

      1450       1460       1470       1480       1490       1500 
QPPLSKASML GHEERIPDPP PGPPSKSSSQ ARGSLEEQLL QELNNLILRK GEPASCPESS 

      1510       1520       1530 
SQPTSPQAPS PTSLPTPTPS LPTQPPCTSN PPSSQPLT

Q8R5G7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools