RIN1_RAT
ID RIN1_RAT Reviewed; 774 AA.
AC P97680;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Ras and Rab interactor 1;
DE AltName: Full=Ras interaction/interference protein 1;
GN Name=Rin1;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9144171; DOI=10.1073/pnas.94.10.4954;
RA Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H.,
RA Witte O., Colicelli J.;
RT "Protein binding and signaling properties of RIN1 suggest a unique effector
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997).
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}.
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-351. 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-351 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Some amount is membrane-
CC associated. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2.
CC Phosphorylation at Ser-351 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U80076; AAB58256.1; ALT_INIT; mRNA.
DR RefSeq; NP_620607.1; NM_139038.1.
DR AlphaFoldDB; P97680; -.
DR SMR; P97680; -.
DR IntAct; P97680; 1.
DR STRING; 10116.ENSRNOP00000027335; -.
DR iPTMnet; P97680; -.
DR PhosphoSitePlus; P97680; -.
DR PaxDb; P97680; -.
DR PRIDE; P97680; -.
DR GeneID; 207119; -.
DR KEGG; rno:207119; -.
DR UCSC; RGD:620006; rat.
DR CTD; 9610; -.
DR RGD; 620006; Rin1.
DR eggNOG; KOG2320; Eukaryota.
DR InParanoid; P97680; -.
DR OrthoDB; 251004at2759; -.
DR PhylomeDB; P97680; -.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P97680; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; ISO:RGD.
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; PS50001; SH2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; Endocytosis; GTPase activation;
KW Membrane; Methylation; Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..774
FT /note="Ras and Rab interactor 1"
FT /id="PRO_0000191319"
FT DOMAIN 68..162
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 456..598
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 624..706
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 188..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..336
FT /note="Polar 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 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 35
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 351
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
FT MOD_RES 692
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13671"
SQ SEQUENCE 774 AA; 84727 MW; 33900CEEDBF8E658 CRC64;
MEDPGETEAH PLGATSLNFV PGYQQEEKPS PDPLYDTPDA RGVQAGGSQQ PARTVSLRER
LLITRPVWLQ LRANAAAALH VLRTEPPGTF LVRKSNTRQC QTLCVRLPEA SGPSFVSSHY
LQESPGGISL EGSELTFPDL VQLICAYCHT RDILLLPLPL PRAIHQAATH KELEAISHLG
MEFWSSSLNT KNQQRPSEAP QIPRLKARSP QELDQGTGAA LCFFNPLFPG DLGPTKREKF
KRSFKVRVST ETSSPLSPPA VPPPPVPVLP GTSSSQTERL PPRQLLQRES SVGYRVPGSA
SGPSLPPLPS LQEVDCCSPS SSEEEGSSGS PTTSPRLSRP RHRRPLLRSM SSAFCSLLAP
ERQVGRAATM LMQNRYTAVG QLVQDLLTQV RVGPESRELQ GIRQALSRAR AMLSAELGPE
KLLPPERLEL VLEKSLHRSV LKPLRPILAA RLRRRLSTDG SLGRLAEGFR LARTQGPGAF
GSHLNLSSPV EIEPVRQKLL QLLRAYSPSA QIKWLLQACK LLYTALKTQA GENAGADEFL
PLLSLVLAQC DLPDLLLEAE YMSELLEPTL LTGEGGYYLT SLSASLALLS GLSQAHALPL
SPAQELQRSL ALWEQRRLPA THNFQHLLRV AYQDPSTGCT SKTLAVPPGS SIATLSQLCA
TKFRVTQPDA FGLFLYKDQG YHRLPPEALV HRLPTTGYLI YRRAERPETQ RAATEKTKTG
NERPERGAWE EEKGGLNGEG KSEIAVDQEG KDQARGGHMQ LEEQKAEGCP ALEE
