RASF7_MOUSE
ID RASF7_MOUSE Reviewed; 359 AA.
AC Q9DD19;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ras association domain-containing protein 7;
GN Name=Rassf7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Negatively regulates stress-induced JNK activation and
CC apoptosis by promoting MAP2K7 phosphorylation and inhibiting its
CC ability to activate JNK. Following prolonged stress, anti-apoptotic
CC effect stops because of degradation of RASSF7 protein via the
CC ubiquitin-proteasome pathway. Required for the activation of AURKB and
CC chromosomal congression during mitosis where it stimulates microtubule
CC polymerization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP2K7 and GTP-bound NRAS. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=Colocalizes with gamma-tubulin.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated and degraded by the proteasome upon prolonged
CC stress stimuli. {ECO:0000250}.
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DR EMBL; AK002243; BAB21960.1; -; mRNA.
DR EMBL; BC011131; AAH11131.1; -; mRNA.
DR CCDS; CCDS40182.1; -.
DR RefSeq; NP_080162.3; NM_025886.3.
DR RefSeq; XP_006536289.1; XM_006536226.3.
DR RefSeq; XP_006536290.1; XM_006536227.3.
DR RefSeq; XP_006536291.1; XM_006536228.3.
DR AlphaFoldDB; Q9DD19; -.
DR SMR; Q9DD19; -.
DR STRING; 10090.ENSMUSP00000038444; -.
DR PhosphoSitePlus; Q9DD19; -.
DR MaxQB; Q9DD19; -.
DR PaxDb; Q9DD19; -.
DR PRIDE; Q9DD19; -.
DR ProteomicsDB; 300308; -.
DR Antibodypedia; 9750; 252 antibodies from 34 providers.
DR DNASU; 66985; -.
DR Ensembl; ENSMUST00000046890; ENSMUSP00000038444; ENSMUSG00000038618.
DR GeneID; 66985; -.
DR KEGG; mmu:66985; -.
DR UCSC; uc009kka.1; mouse.
DR CTD; 8045; -.
DR MGI; MGI:1914235; Rassf7.
DR VEuPathDB; HostDB:ENSMUSG00000038618; -.
DR eggNOG; KOG1574; Eukaryota.
DR GeneTree; ENSGT00950000182839; -.
DR HOGENOM; CLU_031151_0_1_1; -.
DR InParanoid; Q9DD19; -.
DR OMA; EREIQWE; -.
DR OrthoDB; 1442074at2759; -.
DR PhylomeDB; Q9DD19; -.
DR TreeFam; TF318385; -.
DR BioGRID-ORCS; 66985; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9DD19; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DD19; protein.
DR Bgee; ENSMUSG00000038618; Expressed in esophagus and 179 other tissues.
DR ExpressionAtlas; Q9DD19; baseline and differential.
DR Genevisible; Q9DD19; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR033593; N-RASSF.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033631; RASSF7.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15286; PTHR15286; 1.
DR PANTHER; PTHR15286:SF11; PTHR15286:SF11; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..359
FT /note="Ras association domain-containing protein 7"
FT /id="PRO_0000097174"
FT DOMAIN 6..89
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 87..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..208
FT /evidence="ECO:0000255"
FT COILED 242..301
FT /evidence="ECO:0000255"
FT COMPBIAS 100..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 53
FT /note="L -> P (in Ref. 1; BAB21960)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="V -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 353..359
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39247 MW; 39EF0BCA1D8500F1 CRC64;
MVLELVAMEL KVWVDGIQRV VCGVSEQTTC QEVVIALAQA IGQTGRFVLV QRLREKERQL
LPQECPVGAQ ATCGQFANDV QFVLRRTGPS LSGRPSSDNC PPPERCPVRA SLPPKPSAIP
GREPRKALTF NLRCPKLVPS PSIPEPAALV GPIPDGFADL QDLELRIQRN TEELGHEAFW
EQELQREQAR EREGQARLQA LSAATAEHAA RLEALDAQAC ALEAELRLAA EAPGPPSATA
SAAERLRQDL ATQERHSLEM QGTLALVSQA LEAAEHALQA QAQELEELNR ELRQCNLQQF
IQQTGAALPP PPPQLDRTIP STQDLLSPNR GELQGVPQSH ILVSSLSPEV PPMRQSSWR
