RFIP5_MOUSE
ID RFIP5_MOUSE Reviewed; 645 AA.
AC Q8R361; C4IXU4;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rab11 family-interacting protein 5 {ECO:0000312|MGI:MGI:1098586};
DE Short=Rab11-FIP5 {ECO:0000312|MGI:MGI:1098586};
DE AltName: Full=Rab11-interacting protein Rip11 {ECO:0000250|UniProtKB:Q9BXF6};
GN Name=Rab11fip5 {ECO:0000312|MGI:MGI:1098586};
GN Synonyms=D6Ertd32e {ECO:0000312|MGI:MGI:1098586},
GN GAF1 {ECO:0000312|MGI:MGI:1098586}, Rip11 {ECO:0000312|MGI:MGI:1098586};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and 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 PROTEIN SEQUENCE OF 382-389, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION IN EXOCYTOSIS, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP SER-357.
RX PubMed=19335615; DOI=10.1111/j.1365-2443.2009.01285.x;
RA Sugawara K., Shibasaki T., Mizoguchi A., Saito T., Seino S.;
RT "Rab11 and its effector Rip11 participate in regulation of insulin granule
RT exocytosis.";
RL Genes Cells 14:445-456(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539; SER-545 AND SER-640, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-283; SER-307 AND
RP SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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: Rab effector involved in protein trafficking from apical
CC recycling endosomes to the apical plasma membrane. Involved in insulin
CC granule exocytosis. May regulate V-ATPase intracellular transport in
CC response to extracellular acidosis. {ECO:0000269|PubMed:19335615}.
CC -!- SUBUNIT: Interacts with RAB11FIP4 (By similarity). Interacts with NAPG
CC (By similarity). Interacts with RO60 (By similarity). Interacts with
CC RAB11A that has been activated by GTP binding (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXF6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Recycling endosome
CC membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19335615}. Early endosome membrane
CC {ECO:0000269|PubMed:19335615}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19335615}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:19335615}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19335615}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000269|PubMed:19335615}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19335615}. Mitochondrion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- DOMAIN: Binds to vesicles enriched in neutral phospholipids via its C2
CC domain. The interaction is favored by Mg(2+) rather than Ca(2+) (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylation
CC at Ser-357 is PKA-dependent. {ECO:0000269|PubMed:19335615}.
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; AC153605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026473; AAH26473.1; -; mRNA.
DR EMBL; BC044833; AAH44833.2; -; mRNA.
DR EMBL; BC051063; AAH51063.3; -; mRNA.
DR EMBL; BC141380; AAI41381.1; -; mRNA.
DR CCDS; CCDS20292.1; -.
DR RefSeq; NP_001003955.1; NM_001003955.2.
DR RefSeq; NP_803417.3; NM_177466.4.
DR AlphaFoldDB; Q8R361; -.
DR SMR; Q8R361; -.
DR BioGRID; 206353; 15.
DR IntAct; Q8R361; 1.
DR STRING; 10090.ENSMUSP00000058305; -.
DR iPTMnet; Q8R361; -.
DR PhosphoSitePlus; Q8R361; -.
DR SwissPalm; Q8R361; -.
DR jPOST; Q8R361; -.
DR MaxQB; Q8R361; -.
DR PaxDb; Q8R361; -.
DR PeptideAtlas; Q8R361; -.
DR PRIDE; Q8R361; -.
DR ProteomicsDB; 254922; -.
DR Antibodypedia; 31309; 126 antibodies from 26 providers.
DR DNASU; 52055; -.
DR Ensembl; ENSMUST00000060837; ENSMUSP00000058305; ENSMUSG00000051343.
DR GeneID; 52055; -.
DR KEGG; mmu:52055; -.
DR UCSC; uc009cpo.1; mouse.
DR CTD; 26056; -.
DR MGI; MGI:1098586; Rab11fip5.
DR VEuPathDB; HostDB:ENSMUSG00000051343; -.
DR eggNOG; ENOG502QQKU; Eukaryota.
DR GeneTree; ENSGT00940000158783; -.
DR HOGENOM; CLU_015242_2_0_1; -.
DR InParanoid; Q8R361; -.
DR OrthoDB; 567750at2759; -.
DR PhylomeDB; Q8R361; -.
DR TreeFam; TF326172; -.
DR BioGRID-ORCS; 52055; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rab11fip5; mouse.
DR PRO; PR:Q8R361; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R361; protein.
DR Bgee; ENSMUSG00000051343; Expressed in spermatid and 62 other tissues.
DR ExpressionAtlas; Q8R361; baseline and differential.
DR Genevisible; Q8R361; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0071468; P:cellular response to acidic pH; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; ISO:MGI.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISO:MGI.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037245; FIP-RBD_C_sf.
DR InterPro; IPR037789; FIP_classI.
DR InterPro; IPR019018; Rab-bd_FIP-RBD.
DR PANTHER; PTHR15746; PTHR15746; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09457; RBD-FIP; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF144270; SSF144270; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endosome;
KW Golgi apparatus; Membrane; Mitochondrion; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..645
FT /note="Rab11 family-interacting protein 5"
FT /id="PRO_0000097308"
FT DOMAIN 1..146
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 578..640
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF6"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19335615"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF6"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF6"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF6"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF6"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
SQ SEQUENCE 645 AA; 69553 MW; CBA713E9E68A042A CRC64;
MALVRDPEPA AGSSRWLPTH VQVTVLRASG LRGKSSGAGS TSDAYTVIQV GREKYSTSVV
EKTQGCPEWC EECSFELPPG ALDGLLRAQE ADAGPAPWAS GPNAACELVL TTMHRSLIGV
DKFLGRATVA LDEVFRAGRA QHTQWYRLHS KPGKKEKERG EIQVTIQFTR NNLSASMFDL
SMKDKPRSPF SKLKDRVKGK KKYDLESASA ILPSSALEDP ELGSLGKMGK AKGFFLRNKL
RKSSLTQSNT SLGSDSTLSS TSGSLVYQGP GAELLTRSPS HSSWLSTEGG RDSIQSPKLL
THKRTYSDEA SQLRAAPPRA LLELQGHLDG ASRSSLCVNG SHVYNEEPQP PLRHRSSISG
PFPPSSSLHS VPPRSSEEGS RSSDDSWGRG SHGTSSSEAV PGQEELSKQA KGASCSGEEE
GARLPEGKPV QVATPMVASS EAVAAEKDRK PRMGLFHHHH HQGLSRSEQG RRGSVGEKGS
PSLGASPHHS STGEEKAKSS WFGLRESKEP TQKPSPHPVK PLTAAPVEAS PDRKQPRTSL
STALSSGLER LKTVTSGGIQ SVLPASQLGS SVDTKRPKDS AVLDQSAKYY HLTHDELIGL
LLQRERELSQ RDEHVQELES YIDRLLVRIM ETSPTLLQIS PGPPK
