RAIN_HUMAN
ID RAIN_HUMAN Reviewed; 963 AA.
AC Q5U651; Q6U676;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ras-interacting protein 1;
DE Short=Rain;
GN Name=RASIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HRAS; RAP1A; RAP2;
RP RAF1; RRAS AND RRAS2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT
RP CYS-601.
RC TISSUE=Skeletal muscle;
RX PubMed=15031288; DOI=10.1074/jbc.m312867200;
RA Mitin N.Y., Ramocki M.B., Zullo A.J., Der C.J., Konieczny S.F.,
RA Taparowsky E.J.;
RT "Identification and characterization of Rain, a novel Ras-interacting
RT protein with a unique subcellular localization.";
RL J. Biol. Chem. 279:22353-22361(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP FUNCTION.
RX PubMed=22354037; DOI=10.1038/emboj.2012.36;
RA McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
RA Johansen T., Tooze S.A.;
RT "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy
RT requires SCOC and WAC.";
RL EMBO J. 31:1931-1946(2012).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-419, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Required for the proper formation of vascular structures that
CC develop via both vasculogenesis and angiogenesis. Acts as a critical
CC and vascular-specific regulator of GTPase signaling, cell architecture,
CC and adhesion, which is essential for endothelial cell morphogenesis and
CC blood vessel tubulogenesis. Regulates the activity of Rho GTPases in
CC part by recruiting ARHGAP29 and suppressing RhoA signaling and
CC dampening ROCK and MYH9 activities in endothelial cells (By
CC similarity). May act as effector for Golgi-bound HRAS and other Ras-
CC like proteins. May promote HRAS-mediated transformation. Negative
CC regulator of amino acid starvation-induced autophagy. {ECO:0000250,
CC ECO:0000269|PubMed:15031288, ECO:0000269|PubMed:22354037}.
CC -!- SUBUNIT: Interacts with Ras family members that have been activated by
CC GTP binding. Interacts with HRAS, RAP1A, RAP2, RRAS, RAF1 and RRAS2.
CC Interacts with MYH9 and ARHGAP29 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15031288}. Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:15031288}. Note=Associated with perinuclear
CC vesicles. Is recruited to Golgi stacks by activated HRAS.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart. Detected at lower levels
CC in placenta and pancreas. {ECO:0000269|PubMed:15031288}.
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DR EMBL; AY378097; AAR24580.1; -; mRNA.
DR EMBL; BC028614; AAH28614.1; -; mRNA.
DR CCDS; CCDS12731.1; -.
DR RefSeq; NP_060275.2; NM_017805.2.
DR PDB; 5KHO; X-ray; 2.78 A; A/B=134-285.
DR PDB; 5KHQ; X-ray; 2.80 A; A/B=134-285.
DR PDBsum; 5KHO; -.
DR PDBsum; 5KHQ; -.
DR AlphaFoldDB; Q5U651; -.
DR SMR; Q5U651; -.
DR BioGRID; 120263; 18.
DR DIP; DIP-29457N; -.
DR IntAct; Q5U651; 19.
DR STRING; 9606.ENSP00000222145; -.
DR iPTMnet; Q5U651; -.
DR PhosphoSitePlus; Q5U651; -.
DR BioMuta; RASIP1; -.
DR DMDM; 74736209; -.
DR EPD; Q5U651; -.
DR jPOST; Q5U651; -.
DR MassIVE; Q5U651; -.
DR PaxDb; Q5U651; -.
DR PeptideAtlas; Q5U651; -.
DR PRIDE; Q5U651; -.
DR ProteomicsDB; 65240; -.
DR Antibodypedia; 31787; 106 antibodies from 30 providers.
DR DNASU; 54922; -.
DR Ensembl; ENST00000222145.9; ENSP00000222145.3; ENSG00000105538.10.
DR GeneID; 54922; -.
DR KEGG; hsa:54922; -.
DR MANE-Select; ENST00000222145.9; ENSP00000222145.3; NM_017805.3; NP_060275.2.
DR UCSC; uc002pki.4; human.
DR CTD; 54922; -.
DR DisGeNET; 54922; -.
DR GeneCards; RASIP1; -.
DR HGNC; HGNC:24716; RASIP1.
DR HPA; ENSG00000105538; Low tissue specificity.
DR MIM; 609623; gene.
DR neXtProt; NX_Q5U651; -.
DR OpenTargets; ENSG00000105538; -.
DR PharmGKB; PA134875519; -.
DR VEuPathDB; HostDB:ENSG00000105538; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000160072; -.
DR HOGENOM; CLU_010386_1_0_1; -.
DR InParanoid; Q5U651; -.
DR OMA; ERRFEIH; -.
DR OrthoDB; 447883at2759; -.
DR PhylomeDB; Q5U651; -.
DR TreeFam; TF315987; -.
DR PathwayCommons; Q5U651; -.
DR SignaLink; Q5U651; -.
DR BioGRID-ORCS; 54922; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; RASIP1; human.
DR GenomeRNAi; 54922; -.
DR Pharos; Q5U651; Tbio.
DR PRO; PR:Q5U651; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q5U651; protein.
DR Bgee; ENSG00000105538; Expressed in right lung and 139 other tissues.
DR ExpressionAtlas; Q5U651; baseline and differential.
DR Genevisible; Q5U651; HS.
DR GO; GO:0005911; C:cell-cell junction; IMP:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:BHF-UCL.
DR GO; GO:1905709; P:negative regulation of membrane permeability; IDA:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0033625; P:positive regulation of integrin activation; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR CDD; cd15472; Myo5p-like_CBD_Rasip1; 1.
DR InterPro; IPR037983; CBD_Rasip1/Radil.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Cytoplasm; Golgi apparatus; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..963
FT /note="Ras-interacting protein 1"
FT /id="PRO_0000097163"
FT DOMAIN 144..259
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 600..897
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U0S6"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 601
FT /note="R -> C (in dbSNP:rs2287922)"
FT /evidence="ECO:0000269|PubMed:15031288"
FT /id="VAR_051302"
FT CONFLICT 500
FT /note="P -> R (in Ref. 1; AAR24580)"
FT /evidence="ECO:0000305"
FT CONFLICT 511..517
FT /note="PPGPGWA -> RQPWLG (in Ref. 1; AAR24580)"
FT /evidence="ECO:0000305"
FT CONFLICT 736..737
FT /note="EL -> DW (in Ref. 1; AAR24580)"
FT /evidence="ECO:0000305"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:5KHO"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:5KHO"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:5KHO"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:5KHO"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5KHO"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:5KHO"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:5KHO"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:5KHO"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5KHO"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:5KHO"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:5KHO"
SQ SEQUENCE 963 AA; 103457 MW; 470021F91B59EC52 CRC64;
MLSGERKEGG SPRFGKLHLP VGLWINSPRK QLAKLGRRWP SAASVKSSSS DTGSRSSEPL
PPPPPHVELR RVGAVKAAGG ASGSRAKRIS QLFRGSGTGT TGSSGAGGPG TPGGAQRWAS
EKKLPELAAG VAPEPPLATR ATAPPGVLKI FGAGLASGAN YKSVLATARS TARELVAEAL
ERYGLAGSPG GGPGESSCVD AFALCDALGR PAAAGVGSGE WRAEHLRVLG DSERPLLVQE
LWRARPGWAR RFELRGREEA RRLEQEAFGA ADSEGTGAPS WRPQKNRSRA ASGGAALASP
GPGTGSGAPA GSGGKERSEN LSLRRSVSEL SLQGRRRRQQ ERRQQALSMA PGAADAQIGT
ADPGDFDQLT QCLIQAPSNR PYFLLLQGYQ DAQDFVVYVM TREQHVFGRG GNSSGRGGSP
APYVDTFLNA PDILPRHCTV RAGPEHPAMV RPSRGAPVTH NGCLLLREAE LHPGDLLGLG
EHFLFMYKDP RTGGSGPARP PWLPARPGAT PPGPGWAFSC RLCGRGLQER GEALAAYLDG
REPVLRFRPR EEEALLGEIV RAAAAGSGDL PPLGPATLLA LCVQHSAREL ELGHLPRLLG
RLARLIKEAV WEKIKEIGDR QPENHPEGVP EVPLTPEAVS VELRPLMLWM ANTTELLSFV
QEKVLEMEKE ADQEDPQLCN DLELCDEAMA LLDEVIMCTF QQSVYYLTKT LYSTLPALLD
SNPFTAGAEL PGPGAELGAM PPGLRPTLGV FQAALELTSQ CELHPDLVSQ TFGYLFFFSN
ASLLNSLMER GQGRPFYQWS RAVQIRTNLD LVLDWLQGAG LGDIATEFFR KLSMAVNLLC
VPRTSLLKAS WSSLRTDHPT LTPAQLHHLL SHYQLGPGRG PPAAWDPPPA EREAVDTGDI
FESFSSHPPL ILPLGSSRLR LTGPVTDDAL HRELRRLRRL LWDLEQQELP ANYRHGPPVA
TSP
