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 07-APR-2021, entry version 74. 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. 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; 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 BMRB; G3XA57; -. DR SMR; G3XA57; -. DR BioGRID; 217140; 10. DR IntAct; G3XA57; 1. 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; 158 antibodies. 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 eggNOG; ENOG502QUFJ; Eukaryota. DR GeneTree; ENSGT00940000158482; -. DR HOGENOM; CLU_015242_0_0_1; -. DR OMA; LCLIVMH; -. DR OrthoDB; 567750at2759; -. DR TreeFam; TF326172; -. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR BioGRID-ORCS; 74998; 0 hits in 45 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 255 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 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 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 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 //