RINL_MOUSE
ID RINL_MOUSE Reviewed; 563 AA.
AC Q80UW3; Q3TRU0; Q811H9; Q8BUR6; Q8C0J1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ras and Rab interactor-like protein;
GN Name=Rinl;
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 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Thymus;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and NMRI; TISSUE=Mammary tumor;
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, INTERACTION WITH RAB5A; RAB22A AND MUSK, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=21419809; DOI=10.1016/j.bbamcr.2011.03.005;
RA Woller B., Luiskandl S., Popovic M., Prieler B.E., Ikonge G., Mutzl M.,
RA Rehmann H., Herbst R.;
RT "Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide
RT exchange factor for Rab5a and Rab22.";
RL Biochim. Biophys. Acta 1813:1198-1210(2011).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB5A and RAB22A
CC that activates RAB5A and RAB22A by exchanging bound GDP for free GTP.
CC Plays a role in endocytosis via its role in activating Rab family
CC members. {ECO:0000269|PubMed:21419809}.
CC -!- SUBUNIT: Interacts with RAB5A, RAB22A and MUSK.
CC {ECO:0000269|PubMed:21419809}.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle
CC {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21419809}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UW3-2; Sequence=VSP_031892, VSP_031893;
CC -!- TISSUE SPECIFICITY: Detected in thymus and spleen (at protein level).
CC Detected in lung, liver, kidney, spleen, thymus and skeletal muscle.
CC {ECO:0000269|PubMed:21419809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE40363.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK030993; BAC27206.1; -; mRNA.
DR EMBL; AK082828; BAC38641.1; ALT_INIT; mRNA.
DR EMBL; AK162469; BAE36936.1; -; mRNA.
DR EMBL; AK168472; BAE40363.1; ALT_INIT; mRNA.
DR EMBL; BC044878; AAH44878.1; -; mRNA.
DR EMBL; BC046530; AAH46530.1; -; mRNA.
DR CCDS; CCDS21056.1; -. [Q80UW3-1]
DR RefSeq; NP_796132.2; NM_177158.5. [Q80UW3-1]
DR RefSeq; XP_006540162.1; XM_006540099.1. [Q80UW3-1]
DR AlphaFoldDB; Q80UW3; -.
DR SMR; Q80UW3; -.
DR STRING; 10090.ENSMUSP00000058447; -.
DR iPTMnet; Q80UW3; -.
DR PhosphoSitePlus; Q80UW3; -.
DR EPD; Q80UW3; -.
DR PaxDb; Q80UW3; -.
DR PRIDE; Q80UW3; -.
DR ProteomicsDB; 255223; -. [Q80UW3-1]
DR Antibodypedia; 47998; 82 antibodies from 16 providers.
DR DNASU; 320435; -.
DR Ensembl; ENSMUST00000059857; ENSMUSP00000058447; ENSMUSG00000051735. [Q80UW3-1]
DR Ensembl; ENSMUST00000209035; ENSMUSP00000146576; ENSMUSG00000051735. [Q80UW3-1]
DR GeneID; 320435; -.
DR KEGG; mmu:320435; -.
DR UCSC; uc009fzw.3; mouse. [Q80UW3-1]
DR UCSC; uc009fzy.3; mouse. [Q80UW3-2]
DR CTD; 126432; -.
DR MGI; MGI:2444024; Rinl.
DR VEuPathDB; HostDB:ENSMUSG00000051735; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000162381; -.
DR HOGENOM; CLU_038657_0_0_1; -.
DR InParanoid; Q80UW3; -.
DR OMA; GVWHVPE; -.
DR OrthoDB; 251004at2759; -.
DR PhylomeDB; Q80UW3; -.
DR TreeFam; TF331067; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 320435; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q80UW3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80UW3; protein.
DR Bgee; ENSMUSG00000051735; Expressed in granulocyte and 152 other tissues.
DR ExpressionAtlas; Q80UW3; baseline and differential.
DR Genevisible; Q80UW3; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.80; -; 1.
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; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasmic vesicle; Endocytosis;
KW GTPase activation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..563
FT /note="Ras and Rab interactor-like protein"
FT /id="PRO_0000318974"
FT DOMAIN 381..518
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 181..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..442
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031892"
FT VAR_SEQ 443..450
FT /note="GLGGGENK -> MTRPLASL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031893"
FT CONFLICT 535
FT /note="H -> R (in Ref. 1; BAC27206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 62354 MW; 953753E2C427EA9B CRC64;
MRLAQPDMVS AAPTEVDRLV WPLADGADKS PLGVLSTTEP LLRLQRTQRV WEVPELDAQY
AKAFLELWPL GSFLVIGHEP GQVLMLKAGP SSGDINTYQI QRFPGGVSLE SSNLCMPDCP
HLLAFLSASR DVLPRTLLLP TPTVGAGDNH SDPHRLGCIQ VDTSGRVLSV VNQLYLETHG
GWGTETPQQT EPETGQKYSL APRKPTPHRV SWVEDPLRPE AHHTGQEVHH PGADAHSLGS
EVHFSCPALE EEEVNNDCYK DEDEEGCEDM LTAHIRALAR TRSSYVARQY RCLRARLISD
SGNPYSPGDP ATELLQDVRQ LLTDLQNYLA KDPDVRAVFG NRGPSILREE DLGPAVEVAL
CRAVLEPLKP ALWTKLRTLR AQELRRLRRR QIALRVGAGP EGQSPALRNR NRIHARLAHL
HAACAPRRKV ALLLAVCSDV YAGLGGGENK EPLGADAFLP ALTEELIWSP HIGETQLDVE
FLMELLDPGE LRGEAGYYLT TWFGALYHIA HYQPDTGRAP QGLSSEARAS LRQWHRRRTL
HQQAQPTAQA NQPFEEPWAI GDP
