RAP1A

RAP1A
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1C1Y, 1GUA, 3KUC, 4KVG
Identifikatori
Aliasi	RAP1A
Vanjski ID-jevi	OMIM: 179520 MGI: 97852 HomoloGene: 2162 GeneCards: RAP1A
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	111,716,691 bp
Lokacija gena (miš)
Hrom.	Hromosom 3 (miš)
Kraj	105,708,652 bp
Ontologija gena
Molekularna funkcija	• nucleotide binding; • GO:0032403 protein-containing complex binding; • GTP binding; • GO:0001948, GO:0016582 vezivanje za proteine; • GO:0006184 GTPase activity; • GDP binding;
Ćelijska komponenta	• citosol; • endozom; • membrana; • myelin sheath; • ćelijska membrana; • guanyl-nucleotide exchange factor complex; • neuron projection; • Egzosom; • early endosome; • late endosome; • citoplazma; • međućelijske veze; • perinuklearno područje citoplazme; • specific granule membrane; • phagocytic vesicle; • glutamatergic synapse;
Biološki proces	• establishment of endothelial barrier; • positive regulation of glucose import; • microvillus assembly; • regulation of cell junction assembly; • regulation of insulin secretion; • small GTPase mediated signal transduction; • Rap protein signal transduction; • GO:1904579 cellular response to organic cyclic compound; • nervous system development; • negative regulation of synaptic vesicle exocytosis; • liver regeneration; • protein transport; • response to antineoplastic agent; • response to carbohydrate; • negative regulation of collagen biosynthetic process; • cellular response to glucose stimulus; • GO:0072468 Transdukcija signala; • cellular response to nerve growth factor stimulus; • nerve growth factor signaling pathway; • positive regulation of ERK1 and ERK2 cascade; • positive regulation of protein kinase activity; • positive regulation of vasculogenesis; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • cellular response to cAMP; • positive regulation of neuron projection development; • neutrophil degranulation; • positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; • regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; • protein localization to plasma membrane;
	Izvori:Amigo / QuickGO
Ortolozi
	5906
	109905
	ENSG00000116473
	ENSMUSG00000068798
	P62834
	P62835
NM_001010935; NM_001291896; NM_002884; NM_001370216; NM_001370217;
	NM_001394066
	NM_145541
	NP_001010935; NP_001278825; NP_002875; NP_001357145; NP_001357146
	NP_663516
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Ras-srodni protein Rap-1A jest protein koji je kod ljudi kodiran genom RAP1A sa hromosoma 1.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 184 aminokiseline, a molekulska težina 20.987 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
MREYKLVVLG	SGGVGKSALT	VQFVQGIFVE	KYDPTIEDSY	RKQVEVDCQQ
CMLEILDTAG	TEQFTAMRDL	YMKNGQGFAL	VYSITAQSTF	NDLQDLREQI
LRVKDTEDVP	MILVGNKCDL	EDERVVGKEQ	GQNLARQWCN	CAFLESSAKS
KINVNEIFYD	LVRQINRKTP	VEKKKPKKKS	CLLL

Funkcija

Proizvod ovog gena pripada porodici Ras-srodnih proteina. Ovi proteini dijele približno 50% aminokiselinskog identiteta s klasičnim RAS proteinima i imaju brojne zajedničke strukturne karakteristike. Najupečatljivija razlika između RAP proteina i RAS proteina je u njihovoj 61. aminokiselini: glutamin u RAS je zamijenjen treoninom u RAP proteinima. Proizvod ovog gena suprotstavlja se mitogenoj funkciji RAS-a jer može komunicirati sa RAS GAP-ovima i RAF-om na kompetitivni način. Za ovaj gen su identificirane dvije varijante transkripta koje kodiraju isti protein.^[7]

Interakcije

Pokazalo se da je RAP1A u interakciji sa:

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116473 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000068798 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (Dec 1988). "A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization". The Journal of Biological Chemistry. 263 (35): 18965–71. doi:10.1016/S0021-9258(18)37376-9. PMID 3143720.
^ "UniProt, P62834" (jezik: eng.). Pristupljeno 4. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family".
^ Han L, Colicelli J (Mar 1995). "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1". Molecular and Cellular Biology. 15 (3): 1318–23. doi:10.1128/mcb.15.3.1318. PMC 230355. PMID 7862125.
^ Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A (Jun 1995). "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue". Nature. 375 (6532): 554–60. doi:10.1038/375554a0. PMID 7791872. S2CID 4347807.
^ Hu CD, Kariya K, Okada T, Qi X, Song C, Kataoka T (Jan 1999). "Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation". The Journal of Biological Chemistry. 274 (1): 48–51. doi:10.1074/jbc.274.1.48. PMID 9867809.
^ Okada T, Hu CD, Jin TG, Kariya K, Yamawaki-Kataoka Y, Kataoka T (Sep 1999). "The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases". Molecular and Cellular Biology. 19 (9): 6057–64. doi:10.1128/mcb.19.9.6057. PMC 84512. PMID 10454553.
^ ^a ^b Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
^ Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
^ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (maj 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
^ Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (Mar 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". The Journal of Biological Chemistry. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.
^ Rebhun JF, Castro AF, Quilliam LA (Nov 2000). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". The Journal of Biological Chemistry. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204.
^ Castro AF, Rebhun JF, Clark GJ, Quilliam LA (Aug 2003). "Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner". The Journal of Biological Chemistry. 278 (35): 32493–6. doi:10.1074/jbc.C300226200. PMID 12842888.
^ Yamamoto Y, Jones KA, Mak BC, Muehlenbachs A, Yeung RS (Aug 2002). "Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin". Archives of Biochemistry and Biophysics. 404 (2): 210–7. doi:10.1016/s0003-9861(02)00300-4. PMID 12147258.

Vanjski linkovi

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000116473 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000068798 - 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.

[pmid3143720-5] Kawata M, Matsui Y, Kondo J, Hishida T, Teranishi Y, Takai Y (Dec 1988). "A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization". The Journal of Biological Chemistry. 263 (35): 18965–71. doi:10.1016/S0021-9258(18)37376-9. PMID 3143720.

[UniProt-6] "UniProt, P62834" (jezik: eng.). Pristupljeno 4. 12. 2021.CS1 održavanje: nepoznati jezik (link)

[7] "Entrez Gene: RAP1A RAP1A, member of RAS oncogene family".

[pmid7862125-8] Han L, Colicelli J (Mar 1995). "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1". Molecular and Cellular Biology. 15 (3): 1318–23. doi:10.1128/mcb.15.3.1318. PMC 230355. PMID 7862125.

[pmid7791872-9] Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A (Jun 1995). "The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue". Nature. 375 (6532): 554–60. doi:10.1038/375554a0. PMID 7791872. S2CID 4347807.

[pmid9867809-10] Hu CD, Kariya K, Okada T, Qi X, Song C, Kataoka T (Jan 1999). "Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation". The Journal of Biological Chemistry. 274 (1): 48–51. doi:10.1074/jbc.274.1.48. PMID 9867809.

[pmid10454553-11] Okada T, Hu CD, Jin TG, Kariya K, Yamawaki-Kataoka Y, Kataoka T (Sep 1999). "The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases". Molecular and Cellular Biology. 19 (9): 6057–64. doi:10.1128/mcb.19.9.6057. PMC 84512. PMID 10454553.

[pmid10922060-12] Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.

[pmid11786539-13] Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.

[pmid11980706-14] Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (maj 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.

[pmid10085114-15] Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (Mar 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". The Journal of Biological Chemistry. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.

[pmid10934204-16] Rebhun JF, Castro AF, Quilliam LA (Nov 2000). "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction". The Journal of Biological Chemistry. 275 (45): 34901–8. doi:10.1074/jbc.M005327200. PMID 10934204.

[pmid12842888-17] Castro AF, Rebhun JF, Clark GJ, Quilliam LA (Aug 2003). "Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner". The Journal of Biological Chemistry. 278 (35): 32493–6. doi:10.1074/jbc.C300226200. PMID 12842888.

[pmid12147258-18] Yamamoto Y, Jones KA, Mak BC, Muehlenbachs A, Yeung RS (Aug 2002). "Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin". Archives of Biochemistry and Biophysics. 404 (2): 210–7. doi:10.1016/s0003-9861(02)00300-4. PMID 12147258.

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