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 22-JUL-2015, entry version 34. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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/6; 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 RT project: 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 RT granule exocytosis."; RL Genes Cells 14:445-456(2009). CC -!- FUNCTION: A Rab11 effector binding preferentially CC phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and CC phosphatidic acid (PA) and acting in the regulation of the CC transport of vesicles from the endosomal recycling compartment CC (ERC) to the plasma membrane. Involved in insulin granule CC exocytosis. Also involved in receptor-mediated endocytosis and CC membrane trafficking of recycling endosomes, probably originating CC from clathrin-coated vesicles. Required in a complex with MYO5B CC and RAB11 for the transport of NPC1L1 to the plasma membrane. Also CC acts as a regulator of cell polarity. CC {ECO:0000269|PubMed:19335615}. CC -!- SUBUNIT: Homooligomerizes in a Rab11-independent manner. Forms a CC heterooligomeric complex with RAB11FIP4. Interacts with AP2A1, CC MYO5B, RAB25 and REPS1. Interacts with RAB11A and RAB11B CC (activated GTP-bound form). Interacts with NPC1L1. Interacts (via CC NPF motifs) with EHD1 and EHD3 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC Recycling endosome membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. Note=Translocates with RAB11A from the CC vesicles of the endocytic recycling compartment (ERC) to the CC plasma membrane. {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 -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00041}. CC -!- SIMILARITY: Contains 1 FIP-RBD domain. {ECO:0000255|PROSITE- CC ProRule:PRU00844}. 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 UniGene; Mm.24167; -. DR ProteinModelPortal; G3XA57; -. DR SMR; G3XA57; 449-502. DR BioGrid; 217140; 2. DR IntAct; G3XA57; 1. DR STRING; 10090.ENSMUSP00000059978; -. DR MaxQB; G3XA57; -. DR PRIDE; G3XA57; -. 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; NOG148219; -. DR GeneTree; ENSGT00530000063203; -. DR HOGENOM; HOG000234700; -. DR HOVERGEN; HBG054920; -. DR KO; K12484; -. DR OMA; RASNIMP; -. DR TreeFam; TF326172; -. DR Reactome; REACT_286837; Vasopressin regulates renal water homeostasis via Aquaporins. DR ChiTaRS; Rab11fip2; mouse. DR NextBio; 341982; -. DR PRO; PR:G3XA57; -. DR Proteomes; UP000000589; Chromosome 19. DR Bgee; Q5HZI0; -. DR ExpressionAtlas; G3XA57; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central. 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:0045055; P:regulated secretory pathway; IMP:UniProtKB. DR Gene3D; 2.60.40.150; -; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR019018; Rab-bd_FIP-RBD. DR Pfam; PF00168; C2; 1. DR Pfam; PF09457; RBD-FIP; 1. DR SMART; SM00239; C2; 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; Complete proteome; Endosome; KW Membrane; Phosphoprotein; Protein transport; Reference proteome; KW Repeat; Transport. FT CHAIN 1 512 Rab11 family-interacting protein 2. FT /FTId=PRO_0000424063. FT DOMAIN 1 102 C2. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 437 499 FIP-RBD. {ECO:0000255|PROSITE- FT ProRule:PRU00844}. FT REGION 15 102 Necessary for its cellular translocation FT to the plasma membrane. {ECO:0000250}. FT REGION 465 512 Necessary for the interaction with AP2A1, FT RAB11A, subcellular location, endocytosis FT activity and homooligomerization. FT {ECO:0000250}. FT MOTIF 323 325 NPF 1. {ECO:0000250}. FT MOTIF 406 408 NPF 2. {ECO:0000250}. FT MOTIF 440 442 NPF 2. {ECO:0000250}. FT MOD_RES 227 227 Phosphoserine; by MARK2. {ECO:0000250}. FT VAR_SEQ 507 512 GKFTNS -> VYTQDHLSPGPPHLCGEATSTHS (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=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 //