RFIP2_MOUSE
ID RFIP2_MOUSE Reviewed; 512 AA.
AC G3XA57; B9EID4; Q5HZI0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Rab11 family-interacting protein 2;
DE Short=Rab11-FIP2;
GN Name=Rab11fip2;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; 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 [4]
RP FUNCTION IN EXOCYTOSIS.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: A Rab11 effector binding preferentially phosphatidylinositol
CC 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in
CC the regulation of the transport of vesicles from the endosomal
CC recycling compartment (ERC) to the plasma membrane. Involved in insulin
CC granule exocytosis. Also involved in receptor-mediated endocytosis and
CC membrane trafficking of recycling endosomes, probably originating from
CC clathrin-coated vesicles. Required in a complex with MYO5B and RAB11
CC for the transport of NPC1L1 to the plasma membrane. Also acts as a
CC regulator of cell polarity. Plays an essential role in phagocytosis
CC through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for
CC controlling actin-dynamics. {ECO:0000250|UniProtKB:Q7L804,
CC ECO:0000269|PubMed:19335615}.
CC -!- SUBUNIT: Homooligomerizes in a Rab11-independent manner. Forms a
CC heterooligomeric complex with RAB11FIP4. Interacts with AP2A1, MYO5B,
CC RAB25 and REPS1. Interacts with RAB11A and RAB11B (activated GTP-bound
CC form). Interacts with NPC1L1. Interacts (via NPF motifs) with EHD1 and
CC EHD3. Interacts with TICAM2; this interaction directs RAB11FIP2 to the
CC phagosome. {ECO:0000250|UniProtKB:Q7L804}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=Translocates with RAB11A from the vesicles of the
CC endocytic recycling compartment (ERC) to the plasma membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G3XA57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G3XA57-2; Sequence=VSP_053310;
CC -!- PTM: Phosphorylation at Ser-227 by MARK2 regulates epithelial cell
CC polarity.
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DR EMBL; AC105061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466585; EDL01829.1; -; Genomic_DNA.
DR EMBL; BC089010; AAH89010.1; -; mRNA.
DR EMBL; BC139380; AAI39381.1; -; mRNA.
DR EMBL; BC139419; AAI39420.1; -; mRNA.
DR CCDS; CCDS38033.1; -. [G3XA57-2]
DR RefSeq; NP_001028344.2; NM_001033172.3. [G3XA57-2]
DR RefSeq; NP_001157839.1; NM_001164367.1.
DR AlphaFoldDB; G3XA57; -.
DR BMRB; G3XA57; -.
DR SMR; G3XA57; -.
DR BioGRID; 217140; 10.
DR STRING; 10090.ENSMUSP00000059978; -.
DR iPTMnet; G3XA57; -.
DR PhosphoSitePlus; G3XA57; -.
DR jPOST; G3XA57; -.
DR MaxQB; G3XA57; -.
DR PaxDb; G3XA57; -.
DR PeptideAtlas; G3XA57; -.
DR PRIDE; G3XA57; -.
DR ProteomicsDB; 254920; -. [G3XA57-1]
DR ProteomicsDB; 254921; -. [G3XA57-2]
DR Antibodypedia; 46274; 165 antibodies from 28 providers.
DR DNASU; 74998; -.
DR Ensembl; ENSMUST00000051996; ENSMUSP00000059978; ENSMUSG00000040022. [G3XA57-2]
DR Ensembl; ENSMUST00000170819; ENSMUSP00000133151; ENSMUSG00000040022. [G3XA57-1]
DR GeneID; 74998; -.
DR KEGG; mmu:74998; -.
DR UCSC; uc008ibm.1; mouse. [G3XA57-1]
DR UCSC; uc008ibn.2; mouse. [G3XA57-2]
DR CTD; 22841; -.
DR MGI; MGI:1922248; Rab11fip2.
DR VEuPathDB; HostDB:ENSMUSG00000040022; -.
DR eggNOG; ENOG502QUFJ; Eukaryota.
DR GeneTree; ENSGT00940000158482; -.
DR HOGENOM; CLU_015242_0_0_1; -.
DR OMA; VKGRKHD; -.
DR OrthoDB; 567750at2759; -.
DR TreeFam; TF326172; -.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR BioGRID-ORCS; 74998; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Rab11fip2; mouse.
DR PRO; PR:G3XA57; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; G3XA57; protein.
DR Bgee; ENSMUSG00000040022; Expressed in indifferent gonad and 228 other tissues.
DR ExpressionAtlas; G3XA57; baseline and differential.
DR Genevisible; G3XA57; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; 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; 1.
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 Alternative splicing; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..512
FT /note="Rab11 family-interacting protein 2"
FT /id="PRO_0000424063"
FT DOMAIN 1..120
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 437..499
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 15..102
FT /note="Necessary for its cellular translocation to the
FT plasma membrane"
FT /evidence="ECO:0000250"
FT REGION 174..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..512
FT /note="Necessary for interaction with AP2A1, RAB11A,
FT subcellular location, endocytosis activity and
FT homooligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 323..325
FT /note="NPF 1"
FT /evidence="ECO:0000250"
FT MOTIF 406..408
FT /note="NPF 2"
FT /evidence="ECO:0000250"
FT MOTIF 440..442
FT /note="NPF 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 178..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine; by MARK2"
FT /evidence="ECO:0000250|UniProtKB:Q7L804"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L804"
FT VAR_SEQ 507..512
FT /note="GKFTNS -> VYTQDHLSPGPPHLCGEATSTHS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053310"
SQ SEQUENCE 512 AA; 58207 MW; 5A6622C5E0B96728 CRC64;
MMLSEQAQKW FPTHVQVTVL QAKDLKPKGK SGTNDTYTII QLGKEKYSTS VAEKTLEPVW
KEEASFELPG LLMQGSPEKY ILFLIVMHRS LVGLDKFLGQ VAINLNDIFE DKQRRKTEWF
RLESKQGKRI KNRGEIKVNI QFMRNNMTAS MFDLSMKDKT RSPFAKLKDK MKGRKSDGVF
SDTSSAIVPS THMPDANPEF SSGEMQMKSK PKKPFLLGPQ RLSSAHSMSD LTGSHLSSEK
LKSSTVGPTH LLSRQIDSFG VVPESGSLKS PHRRTLSFDT SKLNQPGSIV DEGEHSFGRQ
SDPFTNVTAS LPQKFATLPR KKNPFEESSE PWDSSMNLFS KPIEVRKESK REKREKVSLF
ERVTGKRDSR RPDKLNNGGS DSPCDLKSPS AFSENRQDYF EYESTNPFTA KFRASTIMPS
SSFHVNPTSS EDLRKIPDNN PFDATAGYRS LTYEEVLQEL VKHKELLRRK DTHIRELEDY
IDNLLVRVME ETPSILRVPY EPSRKAGKFT NS
