RUFY1_MOUSE
ID RUFY1_MOUSE Reviewed; 712 AA.
AC Q8BIJ7; Q8BKQ4; Q8BL21; Q9EPM6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=RUN and FYVE domain-containing protein 1;
DE AltName: Full=Rab4-interacting protein;
GN Name=Rufy1; Synonyms=Rabip4;
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 STRAIN=C57BL/6J; TISSUE=Adipose tissue;
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 [MRNA] OF 107-712, TISSUE SPECIFICITY, INTERACTION WITH
RP RAB4, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Skeletal muscle;
RX PubMed=11172003; DOI=10.1073/pnas.98.4.1637;
RA Cormont M., Mari M., Galmiche A., Hofman P., Le Marchand-Brustel Y.;
RT "A FYVE-finger-containing protein, Rabip4, is a Rab4 effector involved in
RT early endosomal traffic.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1637-1642(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND BINDING TO PHOSPHATIDYLINOSITOL-3-PHOSPHATE.
RX PubMed=11509568; DOI=10.1074/jbc.m104885200;
RA Mari M., Macia E., Le Marchand-Brustel Y., Cormont M.;
RT "Role of the FYVE finger and the RUN domain for the subcellular
RT localization of Rabip4.";
RL J. Biol. Chem. 276:42501-42508(2001).
RN [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16522682; DOI=10.1242/jcs.02850;
RA Mari M., Monzo P., Kaddai V., Keslair F., Gonzalez T.,
RA Le Marchand-Brustel Y., Cormont M.;
RT "The Rab4 effector Rabip4 plays a role in the endocytotic trafficking of
RT Glut 4 in 3T3-L1 adipocytes.";
RL J. Cell Sci. 119:1297-1306(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Binds phospholipid vesicles containing phosphatidylinositol
CC 3-phosphate and participates in early endosomal trafficking.
CC {ECO:0000269|PubMed:11172003, ECO:0000269|PubMed:16522682}.
CC -!- SUBUNIT: Interacts with BMX. May interact with SSB (By similarity).
CC Interacts with RAB4 and RAB5 that have been activated by GTP-binding.
CC {ECO:0000250, ECO:0000269|PubMed:11172003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:11172003}.
CC -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions with
CC phosphatidylinositol 3-phosphate in membranes of early endosomes and
CC penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched
CC membranes is substantially increased in acidic conditions (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation on Tyr-393 and/or Tyr-404 is required for
CC interaction with BMX and endosomal targeting. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC17732.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK046625; BAC32811.2; -; mRNA.
DR EMBL; AK046633; BAC32815.1; -; mRNA.
DR EMBL; AK051178; BAC34548.1; -; mRNA.
DR EMBL; AL645904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ250024; CAC17732.1; ALT_INIT; mRNA.
DR CCDS; CCDS24635.1; -.
DR RefSeq; NP_766145.1; NM_172557.2.
DR AlphaFoldDB; Q8BIJ7; -.
DR SMR; Q8BIJ7; -.
DR BioGRID; 229774; 1.
DR IntAct; Q8BIJ7; 2.
DR MINT; Q8BIJ7; -.
DR STRING; 10090.ENSMUSP00000020643; -.
DR iPTMnet; Q8BIJ7; -.
DR PhosphoSitePlus; Q8BIJ7; -.
DR SwissPalm; Q8BIJ7; -.
DR EPD; Q8BIJ7; -.
DR MaxQB; Q8BIJ7; -.
DR PaxDb; Q8BIJ7; -.
DR PeptideAtlas; Q8BIJ7; -.
DR PRIDE; Q8BIJ7; -.
DR ProteomicsDB; 260873; -.
DR Antibodypedia; 29480; 227 antibodies from 32 providers.
DR DNASU; 216724; -.
DR Ensembl; ENSMUST00000020643; ENSMUSP00000020643; ENSMUSG00000020375.
DR GeneID; 216724; -.
DR KEGG; mmu:216724; -.
DR UCSC; uc007isn.1; mouse.
DR CTD; 80230; -.
DR MGI; MGI:2429762; Rufy1.
DR VEuPathDB; HostDB:ENSMUSG00000020375; -.
DR eggNOG; KOG1729; Eukaryota.
DR eggNOG; KOG4381; Eukaryota.
DR GeneTree; ENSGT00940000158334; -.
DR HOGENOM; CLU_014576_3_1_1; -.
DR InParanoid; Q8BIJ7; -.
DR OMA; KQDGGIT; -.
DR OrthoDB; 753155at2759; -.
DR PhylomeDB; Q8BIJ7; -.
DR TreeFam; TF323904; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 216724; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Rufy1; mouse.
DR PRO; PR:Q8BIJ7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BIJ7; protein.
DR Bgee; ENSMUSG00000020375; Expressed in primary oocyte and 254 other tissues.
DR Genevisible; Q8BIJ7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IDA:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR Gene3D; 1.20.58.900; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..712
FT /note="RUN and FYVE domain-containing protein 1"
FT /id="PRO_0000245829"
FT DOMAIN 143..275
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT ZN_FING 646..704
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..629
FT /note="Interaction with RAB4"
FT /evidence="ECO:0000269|PubMed:11172003"
FT COILED 325..378
FT /evidence="ECO:0000255"
FT COILED 409..621
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 393
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96T51"
FT MOD_RES 404
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96T51"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T51"
FT CONFLICT 493
FT /note="G -> R (in Ref. 3; CAC17732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 80376 MW; 71416057ADB71222 CRC64;
MAARGECRRA GQDSEPEPER EPESEPGPEP EPQAGLESGE AFEIVDRSQL PSPGELRSAS
RPRVADSWSA PILTLARRAT GNLSASCGSA LRAAAGLGDG GGGGERAASK GQMMEERANL
MHMMKLSIKV LLQSALSLGR SLDADYAPLQ QFFVVMEHCL KHGLKVKKSF IGQNKSFFGP
LELVEKLCPE ASDIATSVRN LPELKTAVGR GRAWLYLALM QKKLADYLKV LIDNKQLLSE
FYEPEALMME EEGMVIVGLL VGLNVLDANL CLKGEDLDSQ VGVIDFSLCL KDAQDLDSGR
EHERITDVLD QKNYVEELNR HLSCTVGDLQ TKIDGLEKTN SKLQEELSAA TDRICSLQKE
QQQLREQNEV IRERSEKSVE ITKQDTKVEL ETYKQTRQGL DEMYSDVWKQ LKEEKKVRLE
LEKELELQIG MKTEMEIAMK LLEKDTHEKQ DTLVALRQQL EEVKAINLQM FHKVQSAESS
LQQKNEAIAS FEGKTTQVMS SMKQMEERLQ QAERARQAAE ERSHKLQQEL SGRGSALQLQ
LSQLRDQCSG LEKELKSEKE QRQALQRELQ REKDTSCLLQ TELQQVEGLK KELRELQDEK
AELRKVCEEQ EQALQEMGLH LSQSKLKMED IKEVNKALKG HTWLKDDEAT HCKQCEKDFS
ISRRKHHCRN CGHIFCNTCS SNELALPSYP KPVRVCDSCH TLLLQRCSST AS
