RASSF9

RASSF9
Identifikatori
Aliasi	RASSF9
Vanjski ID-jevi	OMIM: 610383 MGI: 2384307 HomoloGene: 3976 GeneCards: RASSF9
Lokacija gena (čovjek)
Hrom.	Hromosom 12 (čovjek)
Kraj	85,836,409 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	102,385,597 bp
Ontologija gena
Molekularna funkcija	• GO:0001948, GO:0016582 vezivanje za proteine; • transporter activity;
Ćelijska komponenta	• citosol; • endozom; • trans-Golgi network transport vesicle membrane; • Egzosom; • reciklirajući endosom;
Biološki proces	• Ciljanje proteina; • GO:0072468 Transdukcija signala; • endosomal transport; • intracellular transport;
	Izvori:Amigo / QuickGO
Ortolozi
	9182
	237504
	ENSG00000198774
	ENSMUSG00000044921
	O75901
	Q8K342
	NM_005447
	NM_146240
	NP_005438
	NP_666352
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Ras-pridruženi protein 9 sa domenom (RASSF9), znan i kao PAM COOH-terminalni interactorski protein 1 (PCIP1) ili peptidilglicin alpha-amidacijski monooksigenazni COOH-terminalni interaktor (PAMCI) je protein koji je kod ljudi kodiran genom RASSF9.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 435 aminokiselina, a molekulska težina 50.021 Da.^[6].

10	20	30	40	50
MAPFGRNLLK	TRHKNRSPTK	DMDSEEKEIV	VWVCQEEKLV	CGLTKRTTSA
DVIQALLEEH	EATFGEKRFL	LGKPSDYCII	EKWRGSERVL	PPLTRILKLW
KAWGDEQPNM	QFVLVKADAF	LPVPLWRTAE	AKLVQNTEKL	WELSPANYMK
TLPPDKQKRI	VRKTFRKLAK	IKQDTVSHDR	DNMETLVHLI	ISQDHTIHQQ
VKRMKELDLE	IEKCEAKFHL	DRVENDGENY	VQDAYLMPSF	SEVEQNLDLQ
YEENQTLEDL	SESDGIEQLE	ERLKYYRILI	DKLSAEIEKE	VKSVCIDINE
DAEGEAASEL	ESSNLESVKC	DLEKSMKAGL	KIHSHLSGIQ	KEIKYSDSLL
QMKAKEYELL	AKEFNSLHIS	NKDGCQLKEN	RAKESEVPSS	NGEIPPFTQR
VFSNYTNDTD	SDTGISSNHS	QDSETTVGDV	VLLST

Simboli

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

Funkcija

RASSF9 je N-terminalni RASSF član porodice Ras-pridruženog (RalGDS / AF-6) domena porodice (N-terminalnih proteina), član 9 sekvenca 12q21.31,^[7]^[8] jedan od dva nova divlja tipa RASSF9 i RASSF10^[8] proteina. Tri proteina koji stupaju u interakciju s fragmentom PAM citosolnog domena, koji sadrži signalizaciju kompleksa RA1 i RA2ras, prekidač I i II.^[9] RASSF7, prvi član porodice N-terminaliziranih RASSF potreban je za mitozu.^[8] Nedavno je otkriveno da je RASSF9 uključen u regulaciju epidermne homeostaze.^[10]

Regulacija

Mutantska regija koja kodira PAM COOH-terminalni interakcijski protein-1 (P-CIP1) uporediva je s onom ljudske hromosomske pruge 4.1 TF (protein krvne plazme), kao endosomni put za recikliranje^[7] na lokacijama mikrotubula, da NOT veže RasGTP.^[11] Specifičnost interakcije može biti povezana s lokacijama mikrotubula u sistemu endosomno – lizosomsko lokaliziranim unutar centrosoma s transferinom i različitim Ras proteinima ili s tim (N-Ras), ali s druge strane, stupa u interakciju s tri^[12] (Ha-Ras, potporodica RasKi-Ras,^[13] i Rap^[14]) funkcije ostataka,^[15] blokiran mutacijom koja utiče na funkciju Ras efektora ^[16] je kritični proizvod t (6:11) abnormalnosti povezane s nekim ljudskim leukemijama, sa oba (6:11) prekidača I i II^[13] regija ras^[9] i molekule kvaščevih adenilil-ciklaza, koja nose ove mutacije postaju neaktivibilni Ras in vitro.^[17] Ostaci u interakciji s Rasom znatno se razlikuju od ostataka iz RalGDS-RBD ^[18] preko svojih C-terminalnih Ras-vezujućih domena (RBD)).^[19] Utvrđeno je da takvi izdvajači kao afadin/AF-6 i Rin1^[17] inhibiraju vezivanje Raf za Ras.^[15] Molekula adenilil-ciklaza koje nose ove mutacije postaju onemogućene Ras-om in vitro, sa Ras-pridruženim domenpm-RA,^[17] ne vezujući se svi RA domeni RasGTP, što je primarno mjesto koje veže Ras.

Interakcije

PAM P prekidač monooksigenaze amidirajuće Peptidil-glicin alfa (PAM)
Protein 7 koji sadrži domen RASSF7 Ras asocijacije (HRAS1-srodni klaster proteina 1)
BLOC1S2: Biogeneza lizozomskih srodnih organela kompleksa-1, podjedinica 2 (BLOC podjedinica 2)
Prekursor TF serotransferina (transferin) (globulin koji veže beta-1-metal)
RAB11A protein povezan s Rasom Rab-11A^[20]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000198774 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000044921 - 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.
^ "Entrez Gene: Ras association (RalGDS/AF-6) domain family (N-terminal) member 9".
^ "UniProt, O75901". Pristupljeno 14. 8. 2021.
^ ^a ^b Chen L, Johnson RC, Milgram SL (decembar 1998). "P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes". J Biol Chem. 273 (50): 33524–32. doi:10.1074/jbc.273.50.33524. PMID 9837933.
^ ^a ^b ^c Sherwood V, Manbodh R, Sheppard C, Chalmers AD (april 2008). "RASSF7 is a member of a new family of RAS association domain-containing proteins and is required for completing mitosis". Mol Biol Cell. 19 (4): 1772–82. doi:10.1091/mbc.E07-07-0652. PMC 2291435. PMID 18272789.
^ ^a ^b Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M (februar 2006). "Structural and mechanistic insights into ras association domains of phospholipase C epsilon". Mol Cell. 21 (4): 495–507. doi:10.1016/j.molcel.2006.01.008. PMID 16483931.
^ Lee, CM; Yang P; Chen LC; Chen CC; Wu SC; Cheng HY; Chang YS (21. 3. 2011). "A Novel Role of RASSF9 in Maintaining Epidermal Homeostasis". PLOS ONE. 6 (3): e17867. doi:10.1371/journal.pone.0017867. PMC 3061870. PMID 21445300.
^ Wojcik J, Girault JA, Labesse G, Chomilier J, Mornon JP, Callebaut I (maj 1999). "Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family". Biochem Biophys Res Commun. 259 (1): 113–20. doi:10.1006/bbrc.1999.0727. PMID 10334925.
^ Huang L, Weng X, Hofer F, Martin GS, Kim SH (august 1997). "Three-dimensional structure of the Ras-interacting domain of RalGDS". Nature Structural & Molecular Biology. 4 (8): 609–15. doi:10.1038/nsb0897-609. PMID 9253406. S2CID 1328881.
^ ^a ^b Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K (januar 1996). "Identification of AF-6 and canoe as putative targets for Ras". J Biol Chem. 271 (2): 607–10. doi:10.1074/jbc.271.2.607. PMID 8557659.
^ Katagiri K, Imamura M, Kinashi T (septembar 2006). "Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion". Nat Immunol. 7 (9): 919–28. doi:10.1038/ni1374. PMID 16892067. S2CID 12337748.
^ ^a ^b Hofer F, Fields S, Schneider C, Martin GS (novembar 1994). "Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator". Proc Natl Acad Sci U S A. 91 (23): 11089–93. doi:10.1073/pnas.91.23.11089. PMC 45172. PMID 7972015.
^ Wang J, Williams RW, Manly KF (2003). " BioGPS: NM_005447,. WebQTL: web-based complex trait analysis". Neuroinformatics. 1 (4): 299–08. doi:10.1385/NI:1:4:299. PMID 15043217. Arhivirano s originala, 10. 8. 2017. Pristupljeno 14. 8. 2021.
^ ^a ^b ^c Kido M, Shima F, Satoh T, Asato T, Kariya K, Kataoka T (februar 2002). "Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase". J Biol Chem. 277 (5): 3117–23. doi:10.1074/jbc.M109526200. PMID 11723130.
^ Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S (decembar 1998). "Solution structure of the Ras-binding domain of RGL". FEBS Lett. 441 (3): 413–8. doi:10.1016/S0014-5793(98)01596-8. PMID 9891982. S2CID 23727331.
^ Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P (septembar 1998). "Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf". Biochemistry. 37 (39): 13453–62. doi:10.1021/bi9811664. PMID 9753431.
^ von Mering C, Jensen LJ, Snel B, Hooper SD, Krupp M, Foglierini M, Jouffre N, Huynen MA, Bork P (decembar 2004). "STRING: known and predicted protein-protein associations, integrated and transferred across organisms". Nucleic Acids Res. 33 (Database issue): D433–D437. doi:10.1093/nar/gki005. PMC 539959. PMID 15608232.^{[mrtav link]}

Dopunska literatura

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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.

Vanjski linkovi

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000198774 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000044921 - 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.

[entrez-5] "Entrez Gene: Ras association (RalGDS/AF-6) domain family (N-terminal) member 9".

[UniProt-6] "UniProt, O75901". Pristupljeno 14. 8. 2021.

[pmid9837933-7] Chen L, Johnson RC, Milgram SL (decembar 1998). "P-CIP1, a novel protein that interacts with the cytosolic domain of peptidylglycine alpha-amidating monooxygenase, is associated with endosomes". J Biol Chem. 273 (50): 33524–32. doi:10.1074/jbc.273.50.33524. PMID 9837933.

[pmid18272789-8] Sherwood V, Manbodh R, Sheppard C, Chalmers AD (april 2008). "RASSF7 is a member of a new family of RAS association domain-containing proteins and is required for completing mitosis". Mol Biol Cell. 19 (4): 1772–82. doi:10.1091/mbc.E07-07-0652. PMC 2291435. PMID 18272789.

[pmid16483931-9] Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M (februar 2006). "Structural and mechanistic insights into ras association domains of phospholipase C epsilon". Mol Cell. 21 (4): 495–507. doi:10.1016/j.molcel.2006.01.008. PMID 16483931.

[10] Lee, CM; Yang P; Chen LC; Chen CC; Wu SC; Cheng HY; Chang YS (21. 3. 2011). "A Novel Role of RASSF9 in Maintaining Epidermal Homeostasis". PLOS ONE. 6 (3): e17867. doi:10.1371/journal.pone.0017867. PMC 3061870. PMID 21445300.

[pmid10334925-11] Wojcik J, Girault JA, Labesse G, Chomilier J, Mornon JP, Callebaut I (maj 1999). "Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family". Biochem Biophys Res Commun. 259 (1): 113–20. doi:10.1006/bbrc.1999.0727. PMID 10334925.

[pmid9253406-12] Huang L, Weng X, Hofer F, Martin GS, Kim SH (august 1997). "Three-dimensional structure of the Ras-interacting domain of RalGDS". Nature Structural & Molecular Biology. 4 (8): 609–15. doi:10.1038/nsb0897-609. PMID 9253406. S2CID 1328881.

[pmid8557659-13] Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K (januar 1996). "Identification of AF-6 and canoe as putative targets for Ras". J Biol Chem. 271 (2): 607–10. doi:10.1074/jbc.271.2.607. PMID 8557659.

[14] Katagiri K, Imamura M, Kinashi T (septembar 2006). "Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion". Nat Immunol. 7 (9): 919–28. doi:10.1038/ni1374. PMID 16892067. S2CID 12337748.

[pmid7972015-15] Hofer F, Fields S, Schneider C, Martin GS (novembar 1994). "Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator". Proc Natl Acad Sci U S A. 91 (23): 11089–93. doi:10.1073/pnas.91.23.11089. PMC 45172. PMID 7972015.

[pmid15043217-16] Wang J, Williams RW, Manly KF (2003). " BioGPS: NM_005447,. WebQTL: web-based complex trait analysis". Neuroinformatics. 1 (4): 299–08. doi:10.1385/NI:1:4:299. PMID 15043217. Arhivirano s originala, 10. 8. 2017. Pristupljeno 14. 8. 2021.

[pmid11723130-17] Kido M, Shima F, Satoh T, Asato T, Kariya K, Kataoka T (februar 2002). "Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase". J Biol Chem. 277 (5): 3117–23. doi:10.1074/jbc.M109526200. PMID 11723130.

[pmid9891982-18] Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S (decembar 1998). "Solution structure of the Ras-binding domain of RGL". FEBS Lett. 441 (3): 413–8. doi:10.1016/S0014-5793(98)01596-8. PMID 9891982. S2CID 23727331.

[pmid9753431-19] Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P (septembar 1998). "Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf". Biochemistry. 37 (39): 13453–62. doi:10.1021/bi9811664. PMID 9753431.

[pmid-20] von Mering C, Jensen LJ, Snel B, Hooper SD, Krupp M, Foglierini M, Jouffre N, Huynen MA, Bork P (decembar 2004). "STRING: known and predicted protein-protein associations, integrated and transferred across organisms". Nucleic Acids Res. 33 (Database issue): D433–D437. doi:10.1093/nar/gki005. PMC 539959. PMID 15608232.^{[mrtav link]}

[5]

[1]

[2]

[3]

[4]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]