RIN2_MOUSE
ID RIN2_MOUSE Reviewed; 903 AA.
AC Q9D684; A8Y5L0; Q3U6Z8; Q3UAK3; Q3UC54; Q99K06;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ras and Rab interactor 2;
DE AltName: Full=Ras interaction/interference protein 2;
GN Name=Rin2;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 427-903 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
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. May function as an upstream activator
CC and/or downstream effector for RAB5B in endocytic pathway. May function
CC as a guanine nucleotide exchange (GEF) of RAB5B, required for
CC activating the RAB5 proteins by exchanging bound GDP for free GTP (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer; probably composed of anti-parallel linkage of
CC two parallel dimers. Interacts with Ras. Interacts with RAB5B, with a
CC much higher affinity for GTP-bound activated RAB5B. Does not interact
CC with other members of the Rab family (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D684-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D684-2; Sequence=VSP_007581;
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH40390.3; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAB29425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC30697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE29760.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAE30311.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAE31576.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK014548; BAB29425.1; ALT_INIT; mRNA.
DR EMBL; AK040763; BAC30697.1; ALT_INIT; mRNA.
DR EMBL; AK150680; BAE29760.1; ALT_SEQ; mRNA.
DR EMBL; AK151332; BAE30311.1; ALT_SEQ; mRNA.
DR EMBL; AK152893; BAE31576.1; ALT_SEQ; mRNA.
DR EMBL; AL672100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005529; AAH05529.1; ALT_INIT; mRNA.
DR EMBL; BC040390; AAH40390.3; ALT_SEQ; mRNA.
DR EMBL; BI660407; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_083000.5; NM_028724.4.
DR RefSeq; XP_006500332.1; XM_006500269.1. [Q9D684-1]
DR RefSeq; XP_006500333.1; XM_006500270.3. [Q9D684-1]
DR RefSeq; XP_006500334.1; XM_006500271.3. [Q9D684-1]
DR AlphaFoldDB; Q9D684; -.
DR SMR; Q9D684; -.
DR STRING; 10090.ENSMUSP00000105632; -.
DR iPTMnet; Q9D684; -.
DR PhosphoSitePlus; Q9D684; -.
DR MaxQB; Q9D684; -.
DR PaxDb; Q9D684; -.
DR PRIDE; Q9D684; -.
DR ProteomicsDB; 255275; -. [Q9D684-1]
DR ProteomicsDB; 255276; -. [Q9D684-2]
DR Antibodypedia; 24653; 81 antibodies from 20 providers.
DR DNASU; 74030; -.
DR Ensembl; ENSMUST00000110005; ENSMUSP00000105632; ENSMUSG00000001768. [Q9D684-1]
DR GeneID; 74030; -.
DR KEGG; mmu:74030; -.
DR CTD; 54453; -.
DR MGI; MGI:1921280; Rin2.
DR VEuPathDB; HostDB:ENSMUSG00000001768; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000154866; -.
DR InParanoid; Q9D684; -.
DR OrthoDB; 251004at2759; -.
DR PhylomeDB; Q9D684; -.
DR TreeFam; TF331067; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 74030; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Rin2; mouse.
DR PRO; PR:Q9D684; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D684; protein.
DR Bgee; ENSMUSG00000001768; Expressed in thoracic mammary gland and 244 other tissues.
DR ExpressionAtlas; Q9D684; baseline and differential.
DR Genevisible; Q9D684; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISO:MGI.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd10394; SH2_RIN2; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR035868; RIN2_SH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF00788; RA; 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; SSF54236; SSF54236; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endocytosis; GTPase activation;
KW Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..903
FT /note="Ras and Rab interactor 2"
FT /id="PRO_0000191321"
FT DOMAIN 97..190
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 627..766
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 796..887
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 44..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..775
FT /note="Interaction with RAB5B"
FT /evidence="ECO:0000250"
FT COMPBIAS 285..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP3"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007581"
FT CONFLICT 180
FT /note="D -> G (in Ref. 1; BAE29760)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> I (in Ref. 1; BAE29760/BAE31576)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> P (in Ref. 3; AAH40390)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="R -> S (in Ref. 3; AAH40390)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> Y (in Ref. 1; BAB29425)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="K -> R (in Ref. 1; BAB29425)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="M -> V (in Ref. 1; BAE30311)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="Y -> C (in Ref. 1; BAE29760)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="T -> A (in Ref. 1; BAE30311)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="R -> Q (in Ref. 1; BAC30697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 903 AA; 101559 MW; A79017A8B4E7949B CRC64;
MSAWTMGAQG LDKRGSFFKL IDTIASEIGE LKREMVQTDI SRENGLEPSE THSMVRHKDG
GYSEDKDGKT CPRDSGYDSL SNRLSILDRL LHTHPIWLQL SLSEEEAAEV LQAQPPGIFL
VRKSSKMQKK VLSLRLPCEF GAPLKEFTIK ESTYTFSLEG SGISFADLFR LIAFYCISRD
VLPFTLKLPY AISTAKTESQ LEELAQLGLN FWSSSADNKP LNSPPPHRPL PSAGICPASL
RQLCLINGVH SIKTRTPSEL ECSQTNGALC FINPLFLKVH SQDLSTGPKR PSTRTPNANG
TERPRSPPPR PPPPAINSLH TSPGLSRTEP QTSMPETVNH SKHGNVALLG TKPTPIPPPR
LKKQASFLEA ESSAKTLTAR RPSRRSEPEP ELELELEMGT AGHAGGAPPR DAPGDCTRAP
PPGSESQPPP CHGARQRLSD MSLSTSSSDS LEFDRSMPLY GYEADTTSSL EDYEGESDQE
TMAPPIKSKK KRNSSFVLPK LVKSQLRKMS GVFSSFMTPE KRMVRRIAEL SRDKCTYFGC
LVQDYVSFLK ENKECHVSST DMLQTIRQFM TQVKNYLSQS SELDPPIESL IPEDQIDVVL
EKAMHKCILK PLKGHVEAML KDFHTADGSW KQLKENLQLV RQRNPQELGV FAPTPDLMEL
EKIKLKFMTM QKMYSPEKKV MLLLRVCKLI YTVMENNSGR MYGADDFLPV LTYVIAQCDM
LELDTEIEYM MELLDPSLLH GEGGYYLTSA YGALSLIKNF QEEQAARLLS SEARDTLRQW
HKRRTTNRTI PSVDDFQNYL RVAFQEVNSG CTGKTLLVRP YITTEDVCQL CAEKFKVEDP
EEYSLFLFVD ETWQQLAEDT YPQKIKAELH SRPQPHIFHF VYKRIKSDPY GVIFQNGEDL
TPS
