A2AB59 (RHG27_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GTPase-activating protein 27

Alternative name(s):
CIN85-associated multi-domain-containing Rho GTPase-activating protein 1
Rho-type GTPase-activating protein 27

Gene names

Name:	Arhgap27
Synonyms:	Camgap1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 By similarity.
Subunit structure	Interacts with SH3KBP1/CIN85 By similarity.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Tissue specificity	Widely expressed. Highly expressed in kidney, lung, small intestine and thymus. Ref.4
Sequence similarities	Contains 1 PH domain. Contains 1 Rho-GAP domain. Contains 1 SH3 domain. Contains 3 WW domains.
Sequence caution	The sequence AAH96671.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of Cdc42 GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB receptor-mediated endocytosis Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Inferred from sequence or structural similarity. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Rac GTPase activator activity Inferred from sequence or structural similarity. Source: UniProtKB SH3 domain binding Inferred from sequence or structural similarity. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: A2AB59-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: A2AB59-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: MAADVEGDVY...RCPPRAESPK → MVDMISKLVRRQSRALRA

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 869	869	Rho GTPase-activating protein 27		PRO_0000317579
Regions
	Domain	8 – 69	62	SH3
	Domain	246 – 280	35	WW 1
	Domain	299 – 333	35	WW 2
	Domain	414 – 447	34	WW 3
	Domain	477 – 593	117	PH
	Domain	677 – 866	190	Rho-GAP
Amino acid modifications
	Modified residue	155	1	Phosphoserine Ref.6
	Modified residue	215	1	Phosphoserine Ref.5
	Modified residue	227	1	Phosphotyrosine Ref.5
	Modified residue	620	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 217	217	MAADV…AESPK → MVDMISKLVRRQSRALRA in isoform 2.		VSP_031057

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: F53EDBAFE1B2A6E7	FASTA	869	97,049
	10 20 30 40 50 60 MAADVEGDVY VLVEHPFEYT GKDGRRIAIQ PNERYRLLRR STEHWWHVRR EPGGRPFYLP 70 80 90 100 110 120 AQYVRELPAL GDPAPAPQPS VPQQRPAVPE PLAYDYRFVS TPVGADGSSA EPRGRASSLC 130 140 150 160 170 180 GPARQRTGGQ RNSLAPGGPA CLYVRPAAPV RPAQSLDDLA RGGTAPPAGL LGSAGHFKAS 190 200 210 220 230 240 SVAGSWVCPR PLAPSDSENV YEAIPDLRCP PRAESPKQVD DPPEPVYANV ERQPRATSPR 250 260 270 280 290 300 SAAAPPRLSP VWETHTDTGT GRPYYYNPDT GVTTWESPFE TPEGTTSPAT SRASVGSGES 310 320 330 340 350 360 LETEWGQYWD EESRRVFFYN PLTGETAWED ETEELEEDHQ EQLEMQPSLS PRSPGQQRPP 370 380 390 400 410 420 TPETDYPELL ASYPEEDYSP VGSFSDPGPA SPLVAPPGWS CQITPDKQML YTNQFTQEQW 430 440 450 460 470 480 VRLEDQHGKP YFYNPEDSSV QWELPQVPIP APRSVRKSSQ DSDTPAQASP PEEKIKTLDK 490 500 510 520 530 540 AGVLHRTKTV DKGKRLRKKH WSTSWTVLEG GVLTFFKDSK TSAAGGLRQP SKLSTPEYTV 550 560 570 580 590 600 ELKGASLSWA PKDKSSKKNV LELRSRDGSE YLIQHDSEAI ISTWHKAIAE GISELSADLL 610 620 630 640 650 660 QGEEGEPSSA DFGSSERLGS WREEDVRQNA ASPSLSPGGL ESDLSRVRHK LRKFLQRRPT 670 680 690 700 710 720 LQSLRDKGYI KDQVFGCALA QLCERERSPV PRFVQQCIRT VEARGLDIDG LYRISGNLAT 730 740 750 760 770 780 IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE PLFPFSHFHQ FIAAIKLQDP 790 800 810 820 830 840 AQRSRCVRDL VRTLPAPNQD TLRLLIQHLC RVIEHGEQNR MTVQNVAIVF GPTLLRPEME 850 860 EASMPMTMVF QNQVVELILH QCADIFPPH
	Isoform 2 [UniParc]. Checksum: EC550B4E2ADCCE9B	FASTA	670	75,802
	10 20 30 40 50 60 MVDMISKLVR RQSRALRAQV DDPPEPVYAN VERQPRATSP RSAAAPPRLS PVWETHTDTG 70 80 90 100 110 120 TGRPYYYNPD TGVTTWESPF ETPEGTTSPA TSRASVGSGE SLETEWGQYW DEESRRVFFY 130 140 150 160 170 180 NPLTGETAWE DETEELEEDH QEQLEMQPSL SPRSPGQQRP PTPETDYPEL LASYPEEDYS 190 200 210 220 230 240 PVGSFSDPGP ASPLVAPPGW SCQITPDKQM LYTNQFTQEQ WVRLEDQHGK PYFYNPEDSS 250 260 270 280 290 300 VQWELPQVPI PAPRSVRKSS QDSDTPAQAS PPEEKIKTLD KAGVLHRTKT VDKGKRLRKK 310 320 330 340 350 360 HWSTSWTVLE GGVLTFFKDS KTSAAGGLRQ PSKLSTPEYT VELKGASLSW APKDKSSKKN 370 380 390 400 410 420 VLELRSRDGS EYLIQHDSEA IISTWHKAIA EGISELSADL LQGEEGEPSS ADFGSSERLG 430 440 450 460 470 480 SWREEDVRQN AASPSLSPGG LESDLSRVRH KLRKFLQRRP TLQSLRDKGY IKDQVFGCAL 490 500 510 520 530 540 AQLCERERSP VPRFVQQCIR TVEARGLDID GLYRISGNLA TIQKLRYKVD HDERLDLDDG 550 560 570 580 590 600 RWEDVHVITG ALKLFFRELP EPLFPFSHFH QFIAAIKLQD PAQRSRCVRD LVRTLPAPNQ 610 620 630 640 650 660 DTLRLLIQHL CRVIEHGEQN RMTVQNVAIV FGPTLLRPEM EEASMPMTMV FQNQVVELIL 670 HQCADIFPPH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 749-869. Strain: Czech II. Tissue: Lung.
[4]	"Identification and characterization of a novel Rho GTPase activating protein implicated in receptor-mediated endocytosis." Sakakibara T., Nemoto Y., Nukiwa T., Takeshima H. FEBS Lett. 566:294-300(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND TYR-227, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK046763 mRNA. Translation: BAE20660.1. AL772325, AL662804 Genomic DNA. Translation: CAM16599.1. AL662804, AL772325 Genomic DNA. Translation: CAM21566.1. BC096671 mRNA. Translation: AAH96671.1. Different initiation.
IPI	IPI00648511. IPI00886308.
RefSeq	NP_001192165.1. NM_001205236.1. NP_598476.2. NM_133715.5.
UniGene	Mm.259113. Mm.397197. Mm.399816.
3D structure databases
ProteinModelPortal	A2AB59.
SMR	A2AB59. Positions 7-67, 479-592, 658-866.
ModBase	Search...
PTM databases
PhosphoSite	A2AB59.
Proteomic databases
PaxDb	A2AB59.
PRIDE	A2AB59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000041385; ENSMUSP00000039427; ENSMUSG00000034255. ENSMUST00000107024; ENSMUSP00000102639; ENSMUSG00000034255.
GeneID	544817.
KEGG	mmu:544817.
UCSC	uc007luc.2. mouse. uc007lud.2. mouse.
Organism-specific databases
CTD	201176.
MGI	MGI:1916903. Arhgap27.
Phylogenomic databases
eggNOG	NOG279563.
GeneTree	ENSGT00700000104029.
HOGENOM	HOG000294167.
HOVERGEN	HBG005328.
InParanoid	A2AB59.
OMA	KGYIRDQ.
OrthoDB	EOG4X3H0P.
Gene expression databases
ArrayExpress	A2AB59.
Bgee	A2AB59.
CleanEx	MM_ARHGAP27.
Genevestigator	A2AB59.
Family and domain databases
Gene3D	1.10.555.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR015767. Rho_GTPase_activating. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. IPR001452. SH3_domain. IPR001202. WW_dom. [Graphical view]
PANTHER	PTHR23181. PTHR23181. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00620. RhoGAP. 1 hit. PF00397. WW. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00324. RhoGAP. 1 hit. SM00326. SH3. 1 hit. SM00456. WW. 3 hits. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit. SSF50044. SH3. 1 hit. SSF51045. WW_Rsp5_WWP. 1 hit.
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50238. RHOGAP. 1 hit. PS50002. SH3. 1 hit. PS01159. WW_DOMAIN_1. False negative. PS50020. WW_DOMAIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ARHGAP27. mouse.
NextBio	412048.
SOURCE	Search...

Entry information

Entry name

RHG27_MOUSE

Accession

Primary (citable) accession number: A2AB59
Secondary accession number(s): Q3V366, Q4V9V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 20, 2007
Last modified:	May 29, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program