RIN1_MOUSE
ID RIN1_MOUSE Reviewed; 763 AA.
AC Q921Q7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras and Rab interactor 1;
DE AltName: Full=Ras interaction/interference protein 1;
GN Name=Rin1;
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 TISSUE=Mammary gland;
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 [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12574403; DOI=10.1523/jneurosci.23-03-00748.2003;
RA Dhaka A., Costa R.M., Hu H., Irvin D.K., Patel A., Kornblum H.I.,
RA Silva A.J., O'Dell T.J., Colicelli J.;
RT "The RAS effector RIN1 modulates the formation of aversive memories.";
RL J. Neurosci. 23:748-757(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ras effector protein, which may serve as an inhibitory
CC modulator of neuronal plasticity in aversive memory formation. Can
CC affect Ras signaling at different levels. First, by competing with RAF1
CC protein for binding to activated Ras. Second, by enhancing signaling
CC from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by
CC activating RAB5A, possibly by functioning as a guanine nucleotide
CC exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP,
CC and facilitating Ras-activated receptor endocytosis (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12574403}.
CC -!- SUBUNIT: Interacts with the GTP-bound form of Ras proteins (NRAS, HRAS
CC and KRAS). This interaction prevents the association between RAF1 and
CC Ras. Interacts with 14-3-3 proteins YWHAB, YWHAE and YWHAZ when
CC phosphorylated on Ser-340. Interacts with the SH3 domain of ABL1 and
CC ABL2. Interacts with RAB5A. The interaction with Ras is probably
CC regulated and antagonized by the interaction with 14-3-3 proteins. The
CC interaction with 14-3-3 proteins is regulated by phosphorylation on
CC Ser-340 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q921Q7; Q03137: Epha4; NbExp=2; IntAct=EBI-15724937, EBI-1539152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Some amount is membrane-
CC associated. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Weakly or no expressed
CC in other tissues, except in testis, where it is expressed at
CC intermediate level. In brain, it is mainly expressed in postnatal
CC forebrain neurons in which it is localized in dendrites and colocalizes
CC with Ras. {ECO:0000269|PubMed:12574403}.
CC -!- PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2.
CC Phosphorylation at Ser-340 by PRKD1 induces interaction with 14-3-3
CC proteins (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000305}.
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DR EMBL; BC011277; AAH11277.1; -; mRNA.
DR CCDS; CCDS29447.1; -.
DR RefSeq; NP_663470.1; NM_145495.2.
DR AlphaFoldDB; Q921Q7; -.
DR SMR; Q921Q7; -.
DR BioGRID; 230435; 8.
DR DIP; DIP-46280N; -.
DR IntAct; Q921Q7; 1.
DR STRING; 10090.ENSMUSP00000025818; -.
DR iPTMnet; Q921Q7; -.
DR PhosphoSitePlus; Q921Q7; -.
DR SwissPalm; Q921Q7; -.
DR MaxQB; Q921Q7; -.
DR PaxDb; Q921Q7; -.
DR PeptideAtlas; Q921Q7; -.
DR PRIDE; Q921Q7; -.
DR ProteomicsDB; 255274; -.
DR Antibodypedia; 30128; 213 antibodies from 30 providers.
DR DNASU; 225870; -.
DR Ensembl; ENSMUST00000225427; ENSMUSP00000153189; ENSMUSG00000024883.
DR GeneID; 225870; -.
DR KEGG; mmu:225870; -.
DR UCSC; uc008gca.1; mouse.
DR CTD; 9610; -.
DR MGI; MGI:2385695; Rin1.
DR VEuPathDB; HostDB:ENSMUSG00000024883; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000161834; -.
DR HOGENOM; CLU_011829_1_0_1; -.
DR InParanoid; Q921Q7; -.
DR OrthoDB; 251004at2759; -.
DR PhylomeDB; Q921Q7; -.
DR TreeFam; TF331067; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 225870; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q921Q7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q921Q7; protein.
DR Bgee; ENSMUSG00000024883; Expressed in nucleus accumbens and 187 other tissues.
DR ExpressionAtlas; Q921Q7; baseline and differential.
DR Genevisible; Q921Q7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd10393; SH2_RIN1; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR035867; RIN1_SH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Endocytosis; GTPase activation;
KW Membrane; Methylation; Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..763
FT /note="Ras and Rab interactor 1"
FT /id="PRO_0000191318"
FT DOMAIN 68..151
FT /note="SH2"
FT DOMAIN 445..587
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 613..695
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 35
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 340
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 681
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
SQ SEQUENCE 763 AA; 83014 MW; 0CE76F66A4773438 CRC64;
MEDPGETGAH PLGATNLNFV PGHQQKEKPS TDPLYDTPDT RGVQAGGSQQ PARTVSLRER
LLITRPVWLQ LRANAAAALH VLRTEPPGTF LVRKSNTRQC QALCVRLPEA SGPSFVSSHY
IEESTGGVSL EGSELMFQDL VQLICGYCRT RAIHQAATHK ELEAISHLGM EFWSSSLNTK
DQQRPSEAPP IPRLKARSPQ ELDQGTGAAL CFFNPLFPGD LGPTKREKFK RSFKVRVSTE
TSSPLSPPAV PPPPVPVLPG TSSSQTERLP PRQLLQRESS VGYRVPGSAA SPCLPPLPSL
QEVDCCSPSS SEEEGSSGSP TTSPRLSRPR HRRPLLRSMS SAFCSLLAPE RQVGRAATML
MQNRYTAVGQ LVQDLLTQVR AGPEPRELQG IRQALSRARA MLSAELGPEK LLPPERLELV
LEKSLHRSVL KPLRPILAAR LRRRLSADGS LGRLAEGFRL ARTQGPGAFG SHLTLSSPVE
TEQVRQKLLQ LLRAYSPSAQ VKWLLQACKL LYTALKSQAG ENAGADEFLP LLSLVLAQCD
LPDLLLEAEY MSELLEPTLL TGEGGYYLTS LSASLALLSG LSQARALPLS PAQELQRSLA
LWEQRRLPAT HSFQHLLRVA YQDPSTGCTS KTLAVPPGSS IATLSQLCAT KFRVTQPDAF
GLFLYKDQGY HRLPPEALAH RLPATGYLIY RRAERPETQG AVAEKAKTGS KGPEAGAWEE
ETGGLNREGK PRIAVDQEGK DQARGGHIGP EEQKAEGSQA LEE
