ID RFIP2_HUMAN Reviewed; 512 AA. AC Q7L804; A6NEI4; Q3I768; Q9Y2F0; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-DEC-2020, entry version 167. DE RecName: Full=Rab11 family-interacting protein 2; DE Short=Rab11-FIP2; DE AltName: Full=NRip11; GN Name=RAB11FIP2; Synonyms=KIAA0941; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH EHD1 RP AND EHD3. RX PubMed=16251358; DOI=10.1091/mbc.e05-05-0466; RA Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S.; RT "Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early RT endosomal transport."; RL Mol. Biol. Cell 17:163-177(2006). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Prekeris R., Davies J.M., Scheller R.H.; RT "Rip11 and nRip11 are Rab11/25 interacting proteins."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC 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 [7] RP INTERACTION WITH MYO5B; RAB11A; RAB11B AND RAB25, AND SUBCELLULAR LOCATION. RX PubMed=11495908; DOI=10.1074/jbc.m104831200; RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., RA Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.; RT "Identification and characterization of a family of Rab11-interacting RT proteins."; RL J. Biol. Chem. 276:39067-39075(2001). RN [8] RP SUBUNIT. RX PubMed=11944901; DOI=10.1006/bbrc.2002.6736; RA Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.; RT "The novel Rab11-FIP/Rip/RCP family of proteins displays extensive RT homo- and hetero-interacting abilities."; RL Biochem. Biophys. Res. Commun. 292:909-915(2002). RN [9] RP SUBUNIT. RX PubMed=12470645; DOI=10.1016/s0006-291x(02)02720-1; RA Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.; RT "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its RT overexpression condenses the Rab11 positive compartment in HeLa cells."; RL Biochem. Biophys. Res. Commun. 299:770-779(2002). RN [10] RP SUBUNIT, INTERACTION WITH RAB11A, AND SUBCELLULAR LOCATION. RX PubMed=11994279; DOI=10.1074/jbc.m200757200; RA Lindsay A.J., McCaffrey M.W.; RT "Rab11-FIP2 functions in transferrin recycling and associates with RT endosomal membranes via its COOH-terminal domain."; RL J. Biol. Chem. 277:27193-27199(2002). RN [11] RP FUNCTION IN RECEPTOR-MEDIATED ENDOCYTOSIS, SUBUNIT, INTERACTION WITH REPS1 RP AND AP2A1, MUTAGENESIS OF 406-ASN--PHE-408 AND 480-TYR--ASP-482, NPF MOTIF, RP AND SUBCELLULAR LOCATION. RX PubMed=12364336; DOI=10.1074/jbc.m206316200; RA Cullis D.N., Philip B., Baleja J.D., Feig L.A.; RT "Rab11-FIP2, an adaptor protein connecting cellular components involved in RT internalization and recycling of epidermal growth factor receptors."; RL J. Biol. Chem. 277:49158-49166(2002). RN [12] RP SUBUNIT, AND INTERACTION WITH GTP-BOUND RAB11A AND GTP-BOUND RAB11B. RX PubMed=15173169; DOI=10.1074/jbc.m404633200; RA Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., RA Prekeris R.; RT "Molecular characterization of Rab11 interactions with members of the RT family of Rab11-interacting proteins."; RL J. Biol. Chem. 279:33430-33437(2004). RN [13] RP FUNCTION IN ENDOSOME TRAFFICKING, INTERACTION WITH PTDINSP3 AND PA, AND RP SUBCELLULAR LOCATION. RX PubMed=15304524; DOI=10.1242/jcs.01280; RA Lindsay A.J., McCaffrey M.W.; RT "The C2 domains of the class I Rab11 family of interacting proteins target RT recycling vesicles to the plasma membrane."; RL J. Cell Sci. 117:4365-4375(2004). RN [14] RP FUNCTION, PHOSPHORYLATION AT SER-227, AND MUTAGENESIS OF SER-223; SER-224; RP SER-227 AND SER-229. RX PubMed=16775013; DOI=10.1091/mbc.e05-08-0736; RA Ducharme N.A., Hales C.M., Lapierre L.A., Ham A.J., Oztan A., Apodaca G., RA Goldenring J.R.; RT "MARK2/EMK1/Par-1Balpha phosphorylation of Rab11-family interacting protein RT 2 is necessary for the timely establishment of polarity in Madin-Darby RT canine kidney cells."; RL Mol. Biol. Cell 17:3625-3637(2006). RN [15] RP FUNCTION, AND INTERACTION WITH NPC1L1. RX PubMed=19542231; DOI=10.1074/jbc.m109.034355; RA Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., RA Song B.-L.; RT "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol- RT regulated translocation of NPC1L1 to the cell surface."; RL J. Biol. Chem. 284:22481-22490(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-277, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP FUNCTION, INTERACTION WITH TICAM2, AND SUBCELLULAR LOCATION. RX PubMed=30883606; DOI=10.1371/journal.ppat.1007684; RA Skjesol A., Yurchenko M., Boesl K., Gravastrand C., Nilsen K.E., RA Groevdal L.M., Agliano F., Patane F., Lentini G., Kim H., Teti G., RA Kumar Sharma A., Kandasamy R.K., Sporsheim B., Starheim K.K., RA Golenbock D.T., Stenmark H., McCaffrey M., Espevik T., Husebye H.; RT "The TLR4 adaptor TRAM controls the phagocytosis of Gram-negative bacteria RT by interacting with the Rab11-family interacting protein 2."; RL PLoS Pathog. 15:E1007684-E1007684(2019). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 410-512, INTERACTION WITH RAB11A, RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-480 AND ILE-481. RX PubMed=16905101; DOI=10.1016/j.str.2006.06.010; RA Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.; RT "Crystal structure of rab11 in complex with rab11 family interacting RT protein 2."; RL Structure 14:1273-1283(2006). 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:0000269|PubMed:12364336, CC ECO:0000269|PubMed:15304524, ECO:0000269|PubMed:16251358, CC ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:19542231, CC ECO:0000269|PubMed:30883606}. 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 (PubMed:30883606). {ECO:0000269|PubMed:11495908, CC ECO:0000269|PubMed:11944901, ECO:0000269|PubMed:11994279, CC ECO:0000269|PubMed:12364336, ECO:0000269|PubMed:12470645, CC ECO:0000269|PubMed:15173169, ECO:0000269|PubMed:15304524, CC ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:16905101, CC ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:30883606}. CC -!- INTERACTION: CC Q7L804; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1049676, EBI-6658203; CC Q7L804; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-1049676, EBI-2510157; CC Q7L804; O75344: FKBP6; NbExp=3; IntAct=EBI-1049676, EBI-744771; CC Q7L804; O75031: HSF2BP; NbExp=3; IntAct=EBI-1049676, EBI-7116203; CC Q7L804; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-1049676, EBI-2556193; CC Q7L804; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-1049676, EBI-14066006; CC Q7L804; P62491: RAB11A; NbExp=12; IntAct=EBI-1049676, EBI-745098; CC Q7L804; Q15907: RAB11B; NbExp=4; IntAct=EBI-1049676, EBI-722234; CC Q7L804; Q7L804: RAB11FIP2; NbExp=8; IntAct=EBI-1049676, EBI-1049676; CC Q7L804; P57735: RAB25; NbExp=5; IntAct=EBI-1049676, EBI-1050500; CC Q7L804; P62258: YWHAE; NbExp=3; IntAct=EBI-1049676, EBI-356498; CC -!- SUBCELLULAR LOCATION: Cell projection, phagocytic cup CC {ECO:0000269|PubMed:30883606}. Cell membrane; Peripheral membrane CC protein. Recycling endosome membrane; Peripheral membrane protein. CC Note=Translocates with RAB11A from the vesicles of the endocytic CC recycling compartment (ERC) to the plasma membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7L804-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L804-2; Sequence=VSP_056649; CC -!- PTM: Phosphorylation at Ser-227 by MARK2 regulates epithelial cell CC polarity. {ECO:0000269|PubMed:16775013}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA76785.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; DQ013303; AAY67796.1; -; mRNA. DR EMBL; AY037299; AAK68635.1; -; mRNA. DR EMBL; AB023158; BAA76785.2; ALT_INIT; mRNA. DR EMBL; AC022395; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49423.1; -; Genomic_DNA. DR EMBL; BC075073; AAH75073.1; -; mRNA. DR EMBL; BC075074; AAH75074.1; -; mRNA. DR CCDS; CCDS7602.1; -. [Q7L804-1] DR CCDS; CCDS81512.1; -. [Q7L804-2] DR RefSeq; NP_001317096.1; NM_001330167.1. [Q7L804-2] DR RefSeq; NP_055719.1; NM_014904.2. [Q7L804-1] DR PDB; 2GZD; X-ray; 2.44 A; C/D=410-512. DR PDB; 2GZH; X-ray; 2.47 A; B=410-512. DR PDB; 2K6S; NMR; -; A/B=450-489. DR PDB; 3TSO; X-ray; 1.80 A; C/D=440-512. DR PDB; 4C4P; X-ray; 2.00 A; B=410-512. DR PDB; 6S8X; X-ray; 2.29 A; A/B/D/E=439-512. DR PDBsum; 2GZD; -. DR PDBsum; 2GZH; -. DR PDBsum; 2K6S; -. DR PDBsum; 3TSO; -. DR PDBsum; 4C4P; -. DR PDBsum; 6S8X; -. DR BMRB; Q7L804; -. DR SMR; Q7L804; -. DR BioGRID; 116514; 67. DR CORUM; Q7L804; -. DR DIP; DIP-29139N; -. DR IntAct; Q7L804; 37. DR MINT; Q7L804; -. DR STRING; 9606.ENSP00000347839; -. DR iPTMnet; Q7L804; -. DR PhosphoSitePlus; Q7L804; -. DR BioMuta; RAB11FIP2; -. DR DMDM; 67472131; -. DR EPD; Q7L804; -. DR jPOST; Q7L804; -. DR MassIVE; Q7L804; -. DR MaxQB; Q7L804; -. DR PaxDb; Q7L804; -. DR PeptideAtlas; Q7L804; -. DR PRIDE; Q7L804; -. DR ProteomicsDB; 61692; -. DR ProteomicsDB; 68832; -. [Q7L804-1] DR Antibodypedia; 46274; 153 antibodies. DR Ensembl; ENST00000355624; ENSP00000347839; ENSG00000107560. [Q7L804-1] DR Ensembl; ENST00000369199; ENSP00000358200; ENSG00000107560. [Q7L804-2] DR GeneID; 22841; -. DR KEGG; hsa:22841; -. DR UCSC; uc001ldj.2; human. [Q7L804-1] DR CTD; 22841; -. DR DisGeNET; 22841; -. DR EuPathDB; HostDB:ENSG00000107560.10; -. DR GeneCards; RAB11FIP2; -. DR HGNC; HGNC:29152; RAB11FIP2. DR HPA; ENSG00000107560; Low tissue specificity. DR MIM; 608599; gene. DR neXtProt; NX_Q7L804; -. DR OpenTargets; ENSG00000107560; -. DR PharmGKB; PA134961225; -. DR eggNOG; ENOG502QUFJ; Eukaryota. DR GeneTree; ENSGT00940000158482; -. DR HOGENOM; CLU_015242_0_0_1; -. DR InParanoid; Q7L804; -. DR OMA; LCLIVMH; -. DR OrthoDB; 567750at2759; -. DR PhylomeDB; Q7L804; -. DR TreeFam; TF326172; -. DR PathwayCommons; Q7L804; -. DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR SIGNOR; Q7L804; -. DR BioGRID-ORCS; 22841; 6 hits in 849 CRISPR screens. DR ChiTaRS; RAB11FIP2; human. DR EvolutionaryTrace; Q7L804; -. DR GeneWiki; RAB11FIP2; -. DR GenomeRNAi; 22841; -. DR Pharos; Q7L804; Tbio. DR PRO; PR:Q7L804; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q7L804; protein. DR Bgee; ENSG00000107560; Expressed in cauda epididymis and 248 other tissues. DR Genevisible; Q7L804; HS. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central. DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB. DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0006909; P:phagocytosis; IMP:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB. DR GO; GO:0003091; P:renal water homeostasis; TAS:Reactome. DR GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; IDA:UniProtKB. DR DisProt; DP02062; -. 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 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Endosome; Membrane; Phosphoprotein; Polymorphism; Protein transport; KW Reference proteome; Repeat; Transport. FT CHAIN 1..512 FT /note="Rab11 family-interacting protein 2" FT /id="PRO_0000097306" 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 REGION 465..512 FT /note="Necessary for interaction with AP2A1, RAB11A, FT subcellular location, endocytosis activity and FT homooligomerization" FT /evidence="ECO:0000269|PubMed:12364336" FT MOTIF 323..325 FT /note="NPF 1" FT MOTIF 406..408 FT /note="NPF 2" FT MOTIF 440..442 FT /note="NPF 3" FT MOD_RES 227 FT /note="Phosphoserine; by MARK2" FT /evidence="ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:16775013" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT VAR_SEQ 422 FT /note="S -> RNTLLTPAVAEWRGSLRWAEL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16251358" FT /id="VSP_056649" FT VARIANT 152 FT /note="F -> V (in dbSNP:rs34028100)" FT /id="VAR_051316" FT MUTAGEN 223 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:16775013" FT MUTAGEN 224 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:16775013" FT MUTAGEN 227 FT /note="S->A: Abolishes phosphorylation by MARK2 and induces FT defects in the reestablishment of junctional complexes." FT /evidence="ECO:0000269|PubMed:16775013" FT MUTAGEN 229 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:16775013" FT MUTAGEN 406..408 FT /note="NPF->AAA: Severe reduction of the interaction with FT REPS1 and AP2A1. No effects on its subcellular location. FT Modifies the endocytosis activity." FT /evidence="ECO:0000269|PubMed:12364336" FT MUTAGEN 480..482 FT /note="YID->AAA: Abolishes the interaction with REPS1 and FT AP2A1. Modifies its subcellular location and the FT endocytosis activity. Enhances homooligomerization." FT /evidence="ECO:0000269|PubMed:12364336" FT MUTAGEN 480 FT /note="Y->F: No effect on the interaction with RAB11A. FT Abolishes the vesicular localization." FT /evidence="ECO:0000269|PubMed:16905101" FT MUTAGEN 481 FT /note="I->E: Abolishes the interaction with RAB11A and the FT vesicular localization." FT /evidence="ECO:0000269|PubMed:16905101" FT HELIX 453..491 FT /evidence="ECO:0000244|PDB:3TSO" FT HELIX 493..496 FT /evidence="ECO:0000244|PDB:3TSO" FT STRAND 497..499 FT /evidence="ECO:0000244|PDB:3TSO" SQ SEQUENCE 512 AA; 58279 MW; 9EC2DAB0A585BCD3 CRC64; MMLSEQAQKW FPTHVQVTVL QAKDLKPKGK SGTNDTYTII QLGKEKYSTS VAEKTLEPVW KEEASFELPG LLIQGSPEKY ILFLIVMHRS LVGLDKFLGQ VAINLNDIFE DKQRRKTEWF RLESKQGKRI KNRGEIKVNI QFMRNNMTAS MFDLSMKDKT RSPFAKLKDK MKGRKNDGTF SDTSSAIIPS THMPDANSEF SSGEIQMKSK PKKPFLLGPQ RLSSAHSMSD LSGSHMSSEK LKAGTIGQTH LLGHQLDSFG TVPESGSLKS PHRRTLSFDT SKMNQPDSIV DEGELCFGRQ NDPFTNVTAS LPQKFATLPR KKNPFEESSE TWDSSMNLFS KPIEIRKENK REKREKVSLF ERVTGKKDSR RSDKLNNGGS DSPCDLKSPN AFSENRQDYF DYESTNPFTA KFRASNIMPS SSFHMSPTSN EDLRKIPDSN PFDATAGYRS LTYEEVLQEL VKHKELLRRK DTHIRELEDY IDNLLVRVME ETPSILRVPY EPSRKAGKFS NS //