RFIP2_HUMAN
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 03-AUG-2022, entry version 174.
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=13; 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};
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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 AlphaFoldDB; Q7L804; -.
DR BMRB; Q7L804; -.
DR SMR; Q7L804; -.
DR BioGRID; 116514; 80.
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; 165 antibodies from 28 providers.
DR DNASU; 22841; -.
DR Ensembl; ENST00000355624.8; ENSP00000347839.3; ENSG00000107560.12. [Q7L804-1]
DR Ensembl; ENST00000369199.5; ENSP00000358200.3; ENSG00000107560.12. [Q7L804-2]
DR GeneID; 22841; -.
DR KEGG; hsa:22841; -.
DR MANE-Select; ENST00000355624.8; ENSP00000347839.3; NM_014904.3; NP_055719.1.
DR UCSC; uc001ldj.2; human. [Q7L804-1]
DR CTD; 22841; -.
DR DisGeNET; 22841; -.
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 VEuPathDB; HostDB:ENSG00000107560; -.
DR eggNOG; ENOG502QUFJ; Eukaryota.
DR GeneTree; ENSGT00940000158482; -.
DR HOGENOM; CLU_015242_0_0_1; -.
DR InParanoid; Q7L804; -.
DR OMA; VKGRKHD; -.
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 SignaLink; Q7L804; -.
DR SIGNOR; Q7L804; -.
DR BioGRID-ORCS; 22841; 18 hits in 1085 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 seminal vesicle and 208 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:0031267; F:small GTPase binding; IEA:InterPro.
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:0045055; P:regulated exocytosis; ISS:UniProtKB.
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 SUPFAM; SSF49562; SSF49562; 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; Protein transport; Reference proteome;
KW 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 169..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..392
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: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 COMPBIAS 178..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine; by MARK2"
FT /evidence="ECO:0000269|PubMed:16775013,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:3TSO"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:3TSO"
FT STRAND 497..499
FT /evidence="ECO:0007829|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
