ID   RASF1_MOUSE             Reviewed;         340 AA.
AC   Q99MK9; Q9WUF5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Ras association domain-containing protein 1;
DE   AltName: Full=Protein 123F2;
GN   Name=Rassf1 {ECO:0000312|EMBL:AAK21200.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAK21201.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX   PubMed=11333291; DOI=10.1093/jnci/93.9.691;
RA   Burbee D.G., Forgacs E., Zochbauer-Muller S., Shivakumar L., Fong K.,
RA   Gao B., Randle D., Kondo M., Virmani A., Bader S., Sekido Y., Latif F.,
RA   Milchgrub S., Toyooka S., Gazdar A.F., Lerman M.I., Zabarovsky E.,
RA   White M., Minna J.D.;
RT   "Epigenetic inactivation of RASSF1A in lung and breast cancers and
RT   malignant phenotype suppression.";
RL   J. Natl. Cancer Inst. 93:691-699(2001).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAK21200.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE PROMOTER USAGE.
RC   STRAIN=129/Sv {ECO:0000312|EMBL:AAK21200.1};
RA   Dammann R., Pfeifer G.P.;
RT   "A mouse locus containing the ortholog of the human RASSF1 tumor suppressor
RT   gene.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAH02173.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH02173.1};
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).
RN   [4]
RP   INTERACTION WITH ECM2.
RX   PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA   Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA   Modyanov N.N., Pestov N.B.;
RT   "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL   Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN   [5]
RP   INTERACTION WITH RAB39A AND RAB39B.
RX   PubMed=23294242; DOI=10.1111/gtc.12028;
RA   Takenaka M., Inoue H., Takeshima A., Kakura T., Hori T.;
RT   "C. elegans Rassf homolog, rasf-1, is functionally associated with rab-39
RT   Rab GTPase in oxidative stress response.";
RL   Genes Cells 18:203-210(2013).
CC   -!- FUNCTION: Potential tumor suppressor. Required for death receptor-
CC       dependent apoptosis. Mediates activation of Mediates activation of
CC       STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing
CC       their dephosphorylation. When associated with MOAP1, promotes BAX
CC       conformational change and translocation to mitochondrial membranes in
CC       response to TNF and TNFSF10 stimulation. Isoform A interacts with
CC       CDC20, an activator of the anaphase-promoting complex, APC, resulting
CC       in the inhibition of APC activity and mitotic progression. Inhibits
CC       proliferation by negatively regulating cell cycle progression at the
CC       level of G1/S-phase transition by regulating accumulation of cyclin D1
CC       protein. Isoform C has been shown not to perform these roles, no
CC       function has been identified for this isoform. Isoform A disrupts
CC       interactions among MDM2, DAXX and USP7, thus contributing to the
CC       efficient activation of TP53 by promoting MDM2 self-ubiquitination in
CC       cell-cycle checkpoint control in response to DNA damage (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MAP1S and XPA (By similarity). Binds to the N-
CC       terminal of CDC20 during prometaphase (By similarity). Binds to
CC       STK3/MST2 and STK4/MST1 (By similarity). Recruited to the TNFRSF1A and
CC       TNFRSF10A complexes in response to their respective cognate ligand,
CC       after internalization (By similarity). Can self-associate (By
CC       similarity). Part of a complex with MDM2, DAXX, RASSF1 and USP7 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NS23}.
CC   -!- SUBUNIT: [Isoform A]: Interacts with MOAP1 and E4F1 (By similarity).
CC       Interacts with RSSF5 and probably associates with HRAS via a RSSF1
CC       isoform A-RSSF5 heterodimer (By similarity). Interacts (via C-terminus)
CC       with DAXX (via N-terminus); the interaction is independent of MDM2 and
CC       TP53 (By similarity). Interacts (via N-terminus) with MDM2 (via C-
CC       terminus); the interaction is independent of TP53 (By similarity).
CC       Interacts with RAB39A (PubMed:23294242). Interacts with RAB39B; the
CC       interaction is weak (PubMed:23294242). {ECO:0000250|UniProtKB:Q9NS23,
CC       ECO:0000269|PubMed:23294242}.
CC   -!- SUBUNIT: [Isoform C]: Interacts with ECM2 (PubMed:17335777). Interacts
CC       with RAB39B; the interaction is strong (PubMed:23294242). Does not
CC       interact with RAB39A (PubMed:23294242). {ECO:0000269|PubMed:17335777,
CC       ECO:0000269|PubMed:23294242}.
CC   -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC       centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC       Note=Localizes to cytoplasmic microtubules during interphase, to
CC       bipolar centrosomes associated with microtubules during prophase, to
CC       spindle fibers and spindle poles at metaphase and anaphase, to the
CC       midzone during early telophase, and to the midbody in late telophase in
CC       cells. Colocalizes with MDM2 in the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform C]: Nucleus {ECO:0000250}.
CC       Note=Predominantly nuclear. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q99MK9-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=Q99MK9-2; Sequence=VSP_050779, VSP_050780;
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DR   EMBL; AF132851; AAD30061.1; -; mRNA.
DR   EMBL; AF333027; AAK21200.1; -; Genomic_DNA.
DR   EMBL; AF333027; AAK21201.1; -; Genomic_DNA.
DR   EMBL; BC002173; AAH02173.1; -; mRNA.
DR   CCDS; CCDS23494.1; -. [Q99MK9-2]
DR   CCDS; CCDS57699.1; -. [Q99MK9-1]
DR   RefSeq; NP_001230677.1; NM_001243748.1. [Q99MK9-1]
DR   RefSeq; NP_062687.1; NM_019713.4. [Q99MK9-2]
DR   AlphaFoldDB; Q99MK9; -.
DR   SMR; Q99MK9; -.
DR   BioGRID; 207877; 32.
DR   IntAct; Q99MK9; 31.
DR   MINT; Q99MK9; -.
DR   STRING; 10090.ENSMUSP00000091301; -.
DR   GlyGen; Q99MK9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99MK9; -.
DR   PhosphoSitePlus; Q99MK9; -.
DR   EPD; Q99MK9; -.
DR   MaxQB; Q99MK9; -.
DR   PaxDb; 10090-ENSMUSP00000010211; -.
DR   ProteomicsDB; 255104; -. [Q99MK9-1]
DR   ProteomicsDB; 255105; -. [Q99MK9-2]
DR   Pumba; Q99MK9; -.
DR   Antibodypedia; 30900; 638 antibodies from 36 providers.
DR   DNASU; 56289; -.
DR   Ensembl; ENSMUST00000010211.7; ENSMUSP00000010211.5; ENSMUSG00000010067.14. [Q99MK9-2]
DR   Ensembl; ENSMUST00000093786.9; ENSMUSP00000091301.3; ENSMUSG00000010067.14. [Q99MK9-1]
DR   GeneID; 56289; -.
DR   KEGG; mmu:56289; -.
DR   UCSC; uc009rlq.2; mouse. [Q99MK9-2]
DR   UCSC; uc012hag.2; mouse. [Q99MK9-1]
DR   AGR; MGI:1928386; -.
DR   CTD; 11186; -.
DR   MGI; MGI:1928386; Rassf1.
DR   VEuPathDB; HostDB:ENSMUSG00000010067; -.
DR   eggNOG; KOG4239; Eukaryota.
DR   GeneTree; ENSGT00940000155664; -.
DR   HOGENOM; CLU_045544_0_1_1; -.
DR   InParanoid; Q99MK9; -.
DR   OMA; PAFEMTW; -.
DR   OrthoDB; 4260488at2759; -.
DR   PhylomeDB; Q99MK9; -.
DR   TreeFam; TF319243; -.
DR   BioGRID-ORCS; 56289; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Rassf1; mouse.
DR   PRO; PR:Q99MK9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q99MK9; Protein.
DR   Bgee; ENSMUSG00000010067; Expressed in optic fissure and 252 other cell types or tissues.
DR   ExpressionAtlas; Q99MK9; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR   CDD; cd20885; C1_RASSF1; 1.
DR   CDD; cd17218; RA_RASSF1; 1.
DR   CDD; cd21890; SARAH_RASSF1; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR033614; RASSF1-6.
DR   InterPro; IPR033600; RASSF1_RA.
DR   InterPro; IPR011524; SARAH_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR22738:SF12; RAS ASSOCIATION DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22738; RASSF; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF16517; Nore1-SARAH; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50951; SARAH; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR   Genevisible; Q99MK9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative promoter usage; Cell cycle; Cytoplasm;
KW   Cytoskeleton; Metal-binding; Microtubule; Nucleus; Phosphoprotein;
KW   Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT   CHAIN           2..340
FT                   /note="Ras association domain-containing protein 1"
FT                   /id="PRO_0000068892"
FT   DOMAIN          194..288
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   DOMAIN          290..337
FT                   /note="SARAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT   ZN_FING         51..101
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          2..115
FT                   /note="Mediates interaction with E4F1"
FT                   /evidence="ECO:0000250"
FT   REGION          175..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..314
FT                   /note="MOAP1-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT   VAR_SEQ         1..70
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:11333291,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_050779"
FT   VAR_SEQ         71..119
FT                   /note="FIWGVVRKGLQCAHCKFTCHYRCRALVCLDCCGPRDLGWDSALERDTNV ->
FT                   MGEAETPSFEMTWSSTTSSGYCSQEDSDSELEQYFTARTSLVRRPRRDQ (in
FT                   isoform C)"
FT                   /evidence="ECO:0000303|PubMed:11333291,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_050780"
SQ   SEQUENCE   340 AA;  38789 MW;  7DEBA4AEE705757F CRC64;
     MSAEPELIEL RELAPSGRIG PGRTRLERAN ALRIAPGTTR NPSQQHVPGR GHRFQPAGPT
     THTWCDLCGD FIWGVVRKGL QCAHCKFTCH YRCRALVCLD CCGPRDLGWD SALERDTNVD
     EAVERETPDL SQAETEQKIK DYNGQINSNL FMSLNKDGSY TGFIKVQLKL VRPVSVPSSK
     KPPSLQDARR GTGRSTAVKR RTSFYLPKDA IKHLHVLSRT RAREVIEALL RKFMVVDDPR
     KFALFERTER HGQVYLRKLS DDEQPLKLRL LAGPSEKALS FVLKENDSGE VNWDAFSMPE
     LHNFLRILQR EEEEHLRQIL QKYSRCRQKI QEALHACPLG
//