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Ras association domain-containing protein 5 (New ras effector 1) (Regulator for cell adhesion and polarization enriched in lymphoid tissues) (RAPL)

 RASF5_MOUSE             Reviewed;         413 AA.
Q5EBH1; O70407; Q6KAR0; Q8C2E8;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Ras association domain-containing protein 5;
AltName: Full=New ras effector 1;
AltName: Full=Regulator for cell adhesion and polarization enriched in lymphoid tissues;
Short=RAPL;
Name=Rassf5; Synonyms=Nore1, Rapl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HRAS.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=9488663; DOI=10.1074/jbc.273.10.5439;
Vavvas D., Li X., Avruch J., Zhang X.F.;
"Identification of Nore1 as a potential Ras effector.";
J. Biol. Chem. 273:5439-5442(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=12845325; DOI=10.1038/ni950;
Katagiri K., Maeda A., Shimonaka M., Kinashi T.;
"RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion
through spatial regulation of LFA-1.";
Nat. Immunol. 4:741-748(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Natural killer cell;
PubMed=15449545; DOI=10.1093/dnares/11.2.127;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of FLJ genes:
the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 11:127-135(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
FUNCTION IN APOPTOSIS, AND INTERACTION WITH STK4/MST1; HRAS AND KRAS.
PubMed=11864565; DOI=10.1016/S0960-9822(02)00683-8;
Khokhlatchev A., Rabizadeh S., Xavier R., Nedwidek M., Chen T.,
Zhang X.F., Seed B., Avruch J.;
"Identification of a novel Ras-regulated proapoptotic pathway.";
Curr. Biol. 12:253-265(2002).
[7]
SELF-ASSOCIATION, AND INTERACTION WITH RSSF1; HRAS; KRAS; RRAS; RRAS2;
MRAS; RAP1B; RAP2A AND RALA.
PubMed=11857081; DOI=10.1038/sj.onc.1205192;
Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
Pfeifer G.P., Avruch J.;
"The putative tumor suppressor RASSF1A homodimerizes and
heterodimerizes with the Ras-GTP binding protein Nore1.";
Oncogene 21:1381-1390(2002).
[8]
ERRATUM.
Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
Pfeifer G.P., Avruch J.;
Oncogene 21:1943-1943(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
STRUCTURE BY NMR OF 95-166, AND SUBUNIT.
PubMed=16698549; DOI=10.1016/j.str.2006.03.008;
Harjes E., Harjes S., Wohlgemuth S., Mueller K.H., Krieger E.,
Herrmann C., Bayer P.;
"GTP-Ras disrupts the intramolecular complex of C1 and RA domains of
Nore1.";
Structure 14:881-888(2006).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 200-357 OF MUTANT ASP-302 IN
COMPLEX WITH HRAS, MUTAGENESIS OF CYS-220; LEU-221; PHE-234; LYS-236;
ASP-280; LYS-283; GLN-284; LYS-302 AND LYS-303, AND INTERACTION WITH
RAP1A.
PubMed=18596699; DOI=10.1038/emboj.2008.125;
Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A.,
Khokhlatchev A., Herrmann C.;
"Novel type of Ras effector interaction established between tumour
suppressor NORE1A and Ras switch II.";
EMBO J. 27:1995-2005(2008).
-!- FUNCTION: Potental tumor suppressor. Seems to be involved in
lymphocyte adhesion by linking RAP1A activation upon T-cell
receptor or chemokine stimulation to integrin activation. Isoform
2 stimulates lymphocyte polarization and the patch-like
distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to
ICAM1. Together with RAP1A may participate in regulation of
microtubule growth. The association of isoform 2 with activated
RAP1A is required for directional movement of endothelial cells
during wound healing (By similarity). May be involved in
regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex
may mediate HRAS and KRAS induced apoptosis. {ECO:0000250,
ECO:0000269|PubMed:11864565}.
-!- SUBUNIT: Interacts directly with activated HRAS; a RASSF5-
STK4/MST1 complex probably associates with activated HRAS.
Interacts with KRAS. Probably interacts with Ras-like GTPases
RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate.
Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5
heterodimer probably mediates the association of RSSF1 with HRAS.
Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds
STK4/MST1, inhibiting STK4/MST1 autoactivation (By similarity).
{ECO:0000250}.
-!- INTERACTION:
O88904:Hipk1; NbExp=5; IntAct=EBI-960530, EBI-692945;
P01112:HRAS (xeno); NbExp=13; IntAct=EBI-960530, EBI-350145;
Q61411:Hras; NbExp=2; IntAct=EBI-960530, EBI-400273;
P23804:Mdm2; NbExp=3; IntAct=EBI-960530, EBI-641788;
P62834:RAP1A (xeno); NbExp=3; IntAct=EBI-960530, EBI-491414;
Q9JI11:Stk4; NbExp=3; IntAct=EBI-960530, EBI-1181352;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Note=Isoform 2 is mainly located in
the perinuclear region of unstimulated primary T-cells. Upon
stimulation translocates to the leading edge and colocalizes with
ITGAL/LFA-1 in the peripheral zone of the immunological synapse.
Isoform 2 is localized to growing microtubules in vascular
endothelial cells and is dissociated from microtubules by
activated RAP1A (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5EBH1-1; Sequence=Displayed;
Name=2;
IsoId=Q5EBH1-2; Sequence=VSP_019368, VSP_019369;
-!- SEQUENCE CAUTION:
Sequence=BAD21397.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF053959; AAC08580.1; -; mRNA.
EMBL; AY261333; AAP83361.1; -; mRNA.
EMBL; AK131147; BAD21397.1; ALT_INIT; mRNA.
EMBL; AK088751; BAC40546.1; -; mRNA.
EMBL; AK155534; BAE33312.1; -; mRNA.
EMBL; AK155869; BAE33472.1; -; mRNA.
EMBL; BC089605; AAH89605.1; -; mRNA.
CCDS; CCDS15268.1; -. [Q5EBH1-1]
CCDS; CCDS78675.1; -. [Q5EBH1-2]
RefSeq; NP_001298023.1; NM_001311094.2. [Q5EBH1-2]
RefSeq; NP_061220.2; NM_018750.4. [Q5EBH1-1]
UniGene; Mm.248291; -.
PDB; 1RFH; NMR; -; A=108-166.
PDB; 2FNF; NMR; -; X=95-166.
PDB; 2YMY; X-ray; 1.69 A; A/B=370-413.
PDB; 3DDC; X-ray; 1.80 A; B=200-357.
PDBsum; 1RFH; -.
PDBsum; 2FNF; -.
PDBsum; 2YMY; -.
PDBsum; 3DDC; -.
ProteinModelPortal; Q5EBH1; -.
SMR; Q5EBH1; -.
BioGrid; 207620; 1.
DIP; DIP-29107N; -.
IntAct; Q5EBH1; 19.
MINT; MINT-5177821; -.
STRING; 10090.ENSMUSP00000027688; -.
iPTMnet; Q5EBH1; -.
PhosphoSitePlus; Q5EBH1; -.
SwissPalm; Q5EBH1; -.
PaxDb; Q5EBH1; -.
PRIDE; Q5EBH1; -.
Ensembl; ENSMUST00000027688; ENSMUSP00000027688; ENSMUSG00000026430. [Q5EBH1-1]
Ensembl; ENSMUST00000068564; ENSMUSP00000067011; ENSMUSG00000026430. [Q5EBH1-2]
GeneID; 54354; -.
KEGG; mmu:54354; -.
UCSC; uc007cnc.1; mouse. [Q5EBH1-2]
UCSC; uc007cnd.1; mouse. [Q5EBH1-1]
CTD; 83593; -.
MGI; MGI:1926375; Rassf5.
eggNOG; ENOG410IPAE; Eukaryota.
eggNOG; ENOG4111HS2; LUCA.
GeneTree; ENSGT00390000003367; -.
HOGENOM; HOG000013025; -.
HOVERGEN; HBG054362; -.
InParanoid; Q5EBH1; -.
KO; K08015; -.
OrthoDB; EOG091G0EPB; -.
PhylomeDB; Q5EBH1; -.
TreeFam; TF319243; -.
EvolutionaryTrace; Q5EBH1; -.
PRO; PR:Q5EBH1; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026430; -.
ExpressionAtlas; Q5EBH1; baseline and differential.
Genevisible; Q5EBH1; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017016; F:Ras GTPase binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:MGI.
CDD; cd00029; C1; 1.
InterPro; IPR033614; C-RASSF.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000159; RA_dom.
InterPro; IPR033623; RASSF5.
InterPro; IPR011524; SARAH_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR22738; PTHR22738; 1.
PANTHER; PTHR22738:SF9; PTHR22738:SF9; 1.
Pfam; PF00130; C1_1; 1.
Pfam; PF16517; Nore1-SARAH; 1.
Pfam; PF00788; RA; 1.
SMART; SM00109; C1; 1.
SMART; SM00314; RA; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50951; SARAH; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Cytoplasm; Cytoskeleton; Metal-binding; Microtubule; Phosphoprotein;
Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
CHAIN 1 413 Ras association domain-containing protein
5.
/FTId=PRO_0000240402.
DOMAIN 265 359 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 361 408 SARAH. {ECO:0000255|PROSITE-
ProRule:PRU00310}.
ZN_FING 117 165 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WWW0}.
MOD_RES 347 347 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8WWW0}.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:12845325,
ECO:0000303|PubMed:15449545,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_019368.
VAR_SEQ 143 188 ALRCANCKFTCHSECRSLIQLDCRQKGGPALDRRSPESTLT
PTLNQ -> MTVDSSMSSGYCSLDEELEDCFFTAKTTFFRN
LQSKQPSK (in isoform 2).
{ECO:0000303|PubMed:12845325,
ECO:0000303|PubMed:15449545,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_019369.
MUTAGEN 220 220 C->A: Reduced interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 220 220 C->D: Strongly reduced interaction with
HRAS. {ECO:0000269|PubMed:18596699}.
MUTAGEN 221 221 L->A,D: Strongly reduced interaction with
HRAS. {ECO:0000269|PubMed:18596699}.
MUTAGEN 234 234 F->A: Reduced interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 236 236 K->A: Reduced interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 280 280 D->A: Reduced interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 283 283 K->A: Very strong reduction of the
interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 284 284 Q->A: Reduced interaction with HRAS.
{ECO:0000269|PubMed:18596699}.
MUTAGEN 302 302 K->D: Reduced specificity for HRAS and
diminished discrimination between HRAS
and RAP1A. {ECO:0000269|PubMed:18596699}.
MUTAGEN 303 303 K->A: Strongly reduced interaction with
HRAS. {ECO:0000269|PubMed:18596699}.
CONFLICT 179 179 E -> G (in Ref. 1; AAC08580).
{ECO:0000305}.
CONFLICT 251 257 IRPQSIY -> SGPSPSM (in Ref. 1; AAC08580).
{ECO:0000305}.
HELIX 112 114 {ECO:0000244|PDB:2FNF}.
TURN 133 135 {ECO:0000244|PDB:1RFH}.
STRAND 137 139 {ECO:0000244|PDB:1RFH}.
TURN 147 149 {ECO:0000244|PDB:1RFH}.
HELIX 155 158 {ECO:0000244|PDB:1RFH}.
HELIX 203 215 {ECO:0000244|PDB:3DDC}.
HELIX 219 221 {ECO:0000244|PDB:3DDC}.
HELIX 227 229 {ECO:0000244|PDB:3DDC}.
STRAND 231 245 {ECO:0000244|PDB:3DDC}.
STRAND 275 288 {ECO:0000244|PDB:3DDC}.
HELIX 293 303 {ECO:0000244|PDB:3DDC}.
HELIX 310 312 {ECO:0000244|PDB:3DDC}.
STRAND 313 321 {ECO:0000244|PDB:3DDC}.
STRAND 324 329 {ECO:0000244|PDB:3DDC}.
HELIX 336 343 {ECO:0000244|PDB:3DDC}.
TURN 347 349 {ECO:0000244|PDB:3DDC}.
STRAND 351 356 {ECO:0000244|PDB:3DDC}.
HELIX 370 405 {ECO:0000244|PDB:2YMY}.
SEQUENCE 413 AA; 46714 MW; E6FF7DDE6BECB180 CRC64;
MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALIPAAG ASEDRGGRRS
GRRDPEPTPR DCRHARPVRP GLQPRLRLRP GSHRPRDVRS IFEQPQDPRV LAERGEGHRF
VELALRGGPG WCDLCGREVL RQALRCANCK FTCHSECRSL IQLDCRQKGG PALDRRSPES
TLTPTLNQNV CKAVEETQHP PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK
LRRPVTVPAG IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISST TTVSEVIQGL
LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADYPLYLR LLAGPDTDVL SFVLKENETG
EVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK LEEALRESQG KPG


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