RASF5_RAT
ID RASF5_RAT Reviewed; 413 AA.
AC O35141;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ras association domain-containing protein 5;
DE AltName: Full=Maxp1;
DE AltName: Full=New ras effector 1;
GN Name=Rassf5; Synonyms=Nore1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Slepnev V.I., De Camilli P.V.;
RT "Maxp1, protein interacting with guanine nucleotide exchange factor Mss4.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH HRAS.
RX PubMed=12676952; DOI=10.1074/jbc.m211019200;
RA Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.;
RT "The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor
RT suppressor in the lung.";
RL J. Biol. Chem. 278:21938-21943(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Potential tumor suppressor. Seems to be involved in
CC lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or
CC chemokine stimulation to integrin activation. Stimulates lymphocyte
CC polarization and the patch-like distribution of ITGAL/LFA-1, resulting
CC in an enhanced adhesion to ICAM1. Together with RAP1A may participate
CC in regulation of microtubule growth. The association with activated
CC RAP1A is required for directional movement of endothelial cells during
CC wound healing. May be involved in regulation of Ras apoptotic function.
CC The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced
CC apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts directly with activated HRAS; a RASSF5-STK4/MST1
CC complex probably associates with activated HRAS. Interacts with KRAS.
CC Probably interacts with Ras-like GTPases RRAS, MRAS, RAP1B, RAP2A and
CC RALA (By similarity). Interacts with RRAS2 (By similarity). Can self-
CC associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5
CC heterodimer probably mediates the association of RSSF1 with HRAS (By
CC similarity). Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1.
CC Binds STK4/MST1, inhibiting STK4/MST1 autoactivation (By similarity).
CC {ECO:0000250|UniProtKB:Q5EBH1, ECO:0000250|UniProtKB:Q8WWW0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Mainly located in the perinuclear region of
CC unstimulated primary T-cells; upon stimulation translocates to the
CC leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of
CC the immunological synapse. Localized to growing microtubules in
CC vascular endothelial cells and is dissociated from microtubules by
CC activated RAP1A (By similarity). {ECO:0000250}.
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DR EMBL; AF002251; AAB71821.1; -; mRNA.
DR RefSeq; NP_062238.1; NM_019365.3.
DR AlphaFoldDB; O35141; -.
DR SMR; O35141; -.
DR STRING; 10116.ENSRNOP00000008055; -.
DR iPTMnet; O35141; -.
DR PhosphoSitePlus; O35141; -.
DR PaxDb; O35141; -.
DR PRIDE; O35141; -.
DR Ensembl; ENSRNOT00000008055; ENSRNOP00000008055; ENSRNOG00000005342.
DR GeneID; 54355; -.
DR KEGG; rno:54355; -.
DR UCSC; RGD:621694; rat.
DR CTD; 83593; -.
DR RGD; 621694; Rassf5.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000159288; -.
DR HOGENOM; CLU_045544_0_0_1; -.
DR InParanoid; O35141; -.
DR OrthoDB; 1120975at2759; -.
DR PhylomeDB; O35141; -.
DR TreeFam; TF319243; -.
DR PRO; PR:O35141; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000005342; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; O35141; baseline and differential.
DR Genevisible; O35141; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046651; P:lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 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; IPR033623; RASSF5.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF9; PTHR22738:SF9; 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; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 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.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Cytoskeleton; Metal-binding; Microtubule;
KW Phosphoprotein; Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..413
FT /note="Ras association domain-containing protein 5"
FT /id="PRO_0000240403"
FT DOMAIN 265..359
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 361..408
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT ZN_FING 117..165
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW0"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW0"
SQ SEQUENCE 413 AA; 46680 MW; 4A44E5830D9F094D CRC64;
MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALISASG ASEGRGSRRN
ARGDPEPTPR DCRHARPVRP GLQQRLRRRP GSHRPRDVRS IFEQPQDPRV LAERGEGHRF
AELALRGGPG WCDLCGREVL RQALRCANCK FTCHPECRSL IQLDCRQKEG PALDRQSPES
TLTPTFNKNV CKAVEETQHP PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK
LRRPVTVPAG IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISSS TTVSEVIQGL
LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADCPLYLR LLAGPDTDVL SFVLKENETG
DVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK LEEALRESQG KPG
