ARHGAP31

Rho GTPaza aktivirajući protein 31 jest protein koji je kod ljudi kodiran genom ARHGAP31 sa hromosoma 3. To je regulator Cdc42/Rac1 GTPaze .^[5]

ARHGAP31
Identifikatori
Aliasi	ARHGAP31
Vanjski ID-jevi	OMIM: 610911 MGI: 1333857 HomoloGene: 10644 GeneCards: ARHGAP31
Lokacija gena (čovjek) Hrom. Hromosom 3 (čovjek)[1] Bend 3q13.32-q13.33 Početak 119,294,383 bp[1] Kraj 119,420,714 bp[1]
Lokacija gena (miš) Hrom. Hromosom 16 (miš)[2] Bend 16|16 B4 Početak 38,418,702 bp[2] Kraj 38,533,636 bp[2]
Ontologija gena Molekularna funkcija • SH3 domain binding • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity Ćelijska komponenta • citosol • međućelijske veze • projekcija ćelije • focal adhesion • lamellipodium Biološki proces • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • regulation of small GTPase mediated signal transduction • GO:0072468 Transdukcija signala • small GTPase mediated signal transduction Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	57514	12549
Ensembl	ENSG00000031081	ENSMUSG00000022799
UniProt	Q2M1Z3	A6X8Z5
RefSeq (mRNK)	NM_020754	NM_020260
RefSeq (bjelančevina)	NP_065805	NP_064656
Lokacija (UCSC)	Chr 3: 119.29 – 119.42 Mb	Chr 16: 38.42 – 38.53 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.444 aminokiselina, а molekulska težina 156.985 Da.^[6]

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MKNKGAKQKL		KRKGAASAFG		CDLTEYLESS		GQDVPYVLKS		CAEFIETHGI
VDGIYRLSGV		TSNIQRLRQE		FGSDQCPDLT		REVYLQDIHC		VGSLCKLYFR
ELPNPLLTYE		LYEKFTEAVS		HCPEEGQLAR		IQNVIQELPP		SHYRTLEYLI
RHLAHIASFS		SKTNMHARNL		ALVWAPNLLR		SKEIEATGCN		GDAAFLAVRV
QQVVIEFILN		HVDQIFNNGA		PGSLENDENR		PIMKSLTLPA		LSLPMKLVSL
EEAQARSLAT		NHPARKERRE		NSLPEIVPPM		GTLFHTVLEL		PDNKRKLSSK
SKKWKSIFNL		GRSGSDSKSK		LSRNGSVFVR		GQRLSVEKAT		IRPAKSMDSL
CSVPVEGKET		KGNFNRTVTT		GGFFIPATKM		HSTGTGSSCD		LTKQEGEWGQ
EGMPPGAEGG		FDVSSDRSHL		QGAQARPPPE		QLKVFRPVED		PESEQTAPKM
LGMFYTSNDS		PSKSVFTSSL		FQMEPSPRNQ		RKALNISEPF		AVSVPLRVSA
VISTNSTPCR		TPPKELQSLS		SLEEFSFHGS		ESGGWPEEEK		PLGAETSAAS
VPKKAGLEDA		KAVPEAPGTV		ECSKGLSQEP		GAHLEEKKTP		ESSLSSQHLN
ELEKRPNPEK		VVEEGREAGE		MESSTLQESP		RARAEAVLLH		EMDEDDLANA
LIWPEIQQEL		KIIESEEELS		SLPPPALKTS		PIQPILESSL		GPFIPSEPPG
SLPCGSFPAP		VSTPLEVWTR		DPANQSTQGA		STAASREKPE		PEQGLHPDLA
SLAPLEIVPF		EKASPQATVE		VGGPGNLSPP		LPPAPPPPTP		LEESTPVLLS
KGGPEREDSS		RKLRTDLYID		QLKSQDSPEI		SSLCQGEEAT		PRHSDKQNSK
NAASEGKGCG		FPSPTREVEI		VSQEEEDVTH		SVQEPSDCDE		DDTVTDIAQH
GLEMVEPWEE		PQWVTSPLHS		PTLKDAHKAQ		VQGLQGHQLE		KRLSHRPSLR
QSHSLDSKPT		VKSQWTLEVP		SSSSCANLET		ERNSDPLQPQ		APRREITGWD
EKALRSFREF		SGLKGAEAPP		NQKGPSGVQP		NPAETSPISL		AEGKELGTHL
GHSSPQIRQG		GVPGPESSKE		SSPSVQDSTS		PGEHPAKLQL		KSTECGPPKG
KNRPSSLNLD		PAIPIADLFW		FENVASFSSP		GMQVSEPGDP		KVTWMTSSYC
KADPWRVYSQ		DPQDLDIVAH		ALTGRRNSAP		VSVSAVRTSF		MVKMCQARAV
PVIPPKIQYT		QIPQPLPSQS		SGENGVQPLE		RSQEGPSSTS		GTTQKPAKDD
SPSSLESSKE		EKPKQDPGAI		KSSPVDATAP		CMCEGPTLSP		EPGSSNLLST
QDAVVQCRKR		MSETEPSGDN		LLSSKLERPS		GGSKPFHRSR		PGRPQSLILF
SPPFPIMDHL		PPSSTVTDSK		VLLSPIRSPT		QTVSPGLLCG		ELAENTWVTP
EGVTLRNKMT		IPKNGQRLET		STSCFYQPQR		RSVILDGRSG		RQIE

Funkcija

ARHGAP31 kodira protein koji aktivira GTPazu (GAP). Različiti ćelijski procesi su regulisani Rho GTPazama koje kruže između neaktivnog oblika vezanog za GDP i aktivnog oblika vezanog za GTP. Ovo kruženje između neaktivnih i aktivnih oblika regulirano je faktorima izmjene guaninskih nukleotida i GAP-ovima. Kodirani protein je GAP za koji je pokazano da regulira dvije GTPaze uključene u proteinsko ciljanje i ćelijski rast.^[5]

Klinički značaj

Mutacije ARHGAP31 rezultiraju gubitkom dostupnog aktivnog Cdc42 i posljedično narušavaju aktinske citoskeletne strukture, uzrokujući sindromsku aplaziju kutisa i anomalije ekstremiteta.^[7]

Reference

1. GRCh38: Ensembl release 89: ENSG00000031081 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022799 - Ensembl, maj 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene".
6. "UniProt, Q2M1Z3" (jezik: engleski). Pristupljeno 6. 11. 2021.
7. Southgate L, Machado RD, Snape KM, Primeau M, Dafou D, Ruddy DM, Branney PA, Fisher M, Lee GJ, Simpson MA, He Y, Bradshaw TY, Blaumeiser B, Winship WS, Reardon W, Maher ER, Fitzpatrick DR, Wuyts W, Zenker M, Lamarche-Vane N, Trembath RC (maj 2011). "Gain-of-Function Mutations of ARHGAP31, a Cdc42/Rac1 GTPase Regulator, Cause Syndromic Cutis Aplasia and Limb Anomalies". Am. J. Hum. Genet. 88 (5): 574–85. doi:10.1016/j.ajhg.2011.04.013. PMC 3146732. PMID 21565291.

Dopunska literatura

• Bandyopadhyay S, Chiang CY, Srivastava J, et al. (2010). "A human MAP kinase interactome". Nat. Methods. 7 (10): 801–5. doi:10.1038/nmeth.1506. PMC 2967489. PMID 20936779.
• Jenna S, Hussain NK, Danek EI, et al. (2002). "The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin". J. Biol. Chem. 277 (8): 6366–73. doi:10.1074/jbc.M105516200. PMID 11744688.
• Zhao C, Ma H, Bossy-Wetzel E, et al. (2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Danek EI, Tcherkezian J, Triki I, et al. (2007). "Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1 regulatory site". J. Biol. Chem. 282 (6): 3624–31. doi:10.1074/jbc.M610073200. PMID 17158447.
• Nagase T, Ishikawa K, Kikuno R, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (5): 337–45. doi:10.1093/dnares/6.5.337. PMID 10574462.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tcherkezian J, Triki I, Stenne R, et al. (2006). "The human orthologue of CdGAP is a phosphoprotein and a GTPase-activating protein for Cdc42 and Rac1 but not RhoA". Biol. Cell. 98 (8): 445–56. doi:10.1042/BC20050101. PMID 16519628. S2CID 25545141.
• Dubois PC, Trynka G, Franke L, et al. (2010). "Multiple common variants for celiac disease influencing immune gene expression". Nat. Genet. 42 (4): 295–302. doi:10.1038/ng.543. PMC 2847618. PMID 20190752.
• Lamarche-Vane N, Hall A (1998). "CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and Rac". J. Biol. Chem. 273 (44): 29172–7. doi:10.1074/jbc.273.44.29172. PMID 9786927.
• Horne BD, Hauser ER, Wang L, et al. (2009). "Validation study of genetic associations with coronary artery disease on chromosome 3q13-21 and potential effect modification by smoking". Ann. Hum. Genet. 73 (Pt 6): 551–8. doi:10.1111/j.1469-1809.2009.00540.x. PMC 2764812. PMID 19706030.

Vanjski linkovi

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

• Lokacija ljudskog genoma ARHGAP31 i stranica sa detaljima o genu ARHGAP31 u UCSC Genome Browseru.