RFIP1_HUMAN
ID RFIP1_HUMAN Reviewed; 1283 AA.
AC Q6WKZ4; J3KNP0; Q307T1; Q6AZK4; Q6WKZ2; Q6WKZ6; Q86YV4; Q8TDL1; Q9H642;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rab11 family-interacting protein 1;
DE Short=Rab11-FIP1;
DE AltName: Full=Rab-coupling protein;
GN Name=RAB11FIP1; Synonyms=RCP;
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 IN ENDOSOMAL RECYCLING
RP PROCESS, VARIANT THR-1185, INTERACTION WITH RAB4A AND RAB11A, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11786538; DOI=10.1074/jbc.m108665200;
RA Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B.,
RA Bucci C., McCaffrey M.W.;
RT "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein.";
RL J. Biol. Chem. 277:12190-12199(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE SPLICING, AND VARIANTS LYS-622; VAL-651 AND THR-1185.
RC TISSUE=Gastric antrum;
RX PubMed=16920206; DOI=10.1016/j.bbaexp.2006.06.001;
RA Jin M., Goldenring J.R.;
RT "The Rab11-FIP1/RCP gene codes for multiple protein transcripts related to
RT the plasma membrane recycling system.";
RL Biochim. Biophys. Acta 1759:281-295(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 603-1283, AND VARIANTS LYS-622 AND THR-1185.
RC TISSUE=Placenta, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung, and Spleen;
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 [6]
RP INTERACTION WITH RAB11A; RAB11B AND RAB25.
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 [7]
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 [8]
RP INTERACTION WITH RAB4A AND RAB11A, MUTAGENESIS OF TYR-1254; ILE-1255 AND
RP ASP-1256, AND SUBCELLULAR LOCATION.
RX PubMed=15280022; DOI=10.1016/j.febslet.2004.06.068;
RA Lindsay A.J., McCaffrey M.W.;
RT "Characterisation of the Rab binding properties of Rab coupling protein
RT (RCP) by site-directed mutagenesis.";
RL FEBS Lett. 571:86-92(2004).
RN [9]
RP FUNCTION IN ENDOSOMAL RECYCLING PROCESS, INTERACTION WITH RAB11A, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15181150; DOI=10.1091/mbc.e03-12-0918;
RA Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H.,
RA Prekeris R.;
RT "The RCP-Rab11 complex regulates endocytic protein sorting.";
RL Mol. Biol. Cell 15:3530-3541(2004).
RN [10]
RP FUNCTION IN PHAGOSOME TRAFFICKING AND PHAGOCYTOSIS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15355514; DOI=10.1111/j.1600-0854.2004.00220.x;
RA Damiani M.T., Pavarotti M., Leiva N., Lindsay A.J., McCaffrey M.W.,
RA Colombo M.I.;
RT "Rab coupling protein associates with phagosomes and regulates recycling
RT from the phagosomal compartment.";
RL Traffic 5:785-797(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-477; SER-545;
RP SER-758 AND SER-1135, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-339; SER-343;
RP SER-345; SER-435 AND SER-545, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-206; SER-234;
RP SER-300; SER-315; SER-339; SER-345; SER-356; SER-357; SER-435; SER-529 AND
RP SER-545, AND 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: A Rab11 effector protein involved in the endosomal recycling
CC process. Also involved in controlling membrane trafficking along the
CC phagocytic pathway and in phagocytosis. {ECO:0000269|PubMed:11786538,
CC ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514,
CC ECO:0000269|PubMed:16920206}.
CC -!- SUBUNIT: Homooligomer (isoform 2). Isoform 2 interacts with RAB4A,
CC RAB11A, RAB11B and RAB25. According to PubMed:15280022, RAB4A binding
CC to RAB11FIP1 is of very low affinity in vitro and in vivo.
CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:11786538,
CC ECO:0000269|PubMed:11944901, ECO:0000269|PubMed:15181150,
CC ECO:0000269|PubMed:15280022}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:11786538,
CC ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15280022,
CC ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206}. Note=Rab11A
CC rather than Rab4A mediates localization in the endocytic recycling
CC compartment (ERC).
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, phagosome
CC membrane. Note=Membrane-bound (isoform 2). Colocalizes with Rab11A at
CC phagosomes (isoform 2).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Rab11-FIP 1B;
CC IsoId=Q6WKZ4-4; Sequence=Displayed;
CC Name=2; Synonyms=Rab11-FIP 1C;
CC IsoId=Q6WKZ4-3; Sequence=VSP_013730;
CC Name=3; Synonyms=Rab11-FIP 1A;
CC IsoId=Q6WKZ4-1; Sequence=VSP_013726;
CC Name=4; Synonyms=Rab11-FIP 1H, No Rab11-binding protein 2;
CC IsoId=Q6WKZ4-2; Sequence=VSP_013727, VSP_013730, VSP_013731,
CC VSP_013732;
CC Name=5;
CC IsoId=Q6WKZ4-5; Sequence=VSP_013728, VSP_013729;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in brain, heart, testis,
CC lung, spleen, ovary and small intestine. {ECO:0000269|PubMed:11786538}.
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DR EMBL; AF368294; AAM09571.1; -; mRNA.
DR EMBL; DQ236342; ABB43161.1; -; mRNA.
DR EMBL; AY280966; AAQ18784.1; -; mRNA.
DR EMBL; AY280968; AAQ18786.1; -; mRNA.
DR EMBL; AY280970; AAQ18788.1; -; mRNA.
DR EMBL; AK026275; BAB15424.1; -; mRNA.
DR EMBL; AK122583; BAC56924.1; -; mRNA.
DR EMBL; AK291781; BAF84470.1; -; mRNA.
DR EMBL; AC130304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC077720; AAH77720.1; -; mRNA.
DR CCDS; CCDS34881.1; -. [Q6WKZ4-3]
DR CCDS; CCDS34882.1; -. [Q6WKZ4-4]
DR RefSeq; NP_001002814.2; NM_001002814.2. [Q6WKZ4-4]
DR RefSeq; NP_079427.4; NM_025151.4. [Q6WKZ4-3]
DR PDB; 4D0G; X-ray; 2.50 A; C=1216-1283.
DR PDBsum; 4D0G; -.
DR AlphaFoldDB; Q6WKZ4; -.
DR SMR; Q6WKZ4; -.
DR BioGRID; 123189; 97.
DR CORUM; Q6WKZ4; -.
DR IntAct; Q6WKZ4; 29.
DR MINT; Q6WKZ4; -.
DR STRING; 9606.ENSP00000331342; -.
DR GlyGen; Q6WKZ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6WKZ4; -.
DR MetOSite; Q6WKZ4; -.
DR PhosphoSitePlus; Q6WKZ4; -.
DR BioMuta; RAB11FIP1; -.
DR DMDM; 519668675; -.
DR EPD; Q6WKZ4; -.
DR jPOST; Q6WKZ4; -.
DR MassIVE; Q6WKZ4; -.
DR MaxQB; Q6WKZ4; -.
DR PaxDb; Q6WKZ4; -.
DR PeptideAtlas; Q6WKZ4; -.
DR PRIDE; Q6WKZ4; -.
DR ProteomicsDB; 67762; -. [Q6WKZ4-4]
DR ProteomicsDB; 67763; -. [Q6WKZ4-1]
DR ProteomicsDB; 67764; -. [Q6WKZ4-2]
DR ProteomicsDB; 67765; -. [Q6WKZ4-3]
DR ProteomicsDB; 67766; -. [Q6WKZ4-5]
DR Antibodypedia; 4467; 214 antibodies from 36 providers.
DR DNASU; 80223; -.
DR Ensembl; ENST00000287263.8; ENSP00000287263.4; ENSG00000156675.16. [Q6WKZ4-3]
DR Ensembl; ENST00000330843.9; ENSP00000331342.4; ENSG00000156675.16. [Q6WKZ4-4]
DR Ensembl; ENST00000524118.1; ENSP00000430680.1; ENSG00000156675.16. [Q6WKZ4-2]
DR GeneID; 80223; -.
DR KEGG; hsa:80223; -.
DR MANE-Select; ENST00000330843.9; ENSP00000331342.4; NM_001002814.3; NP_001002814.2.
DR UCSC; uc003xkm.3; human. [Q6WKZ4-4]
DR CTD; 80223; -.
DR DisGeNET; 80223; -.
DR GeneCards; RAB11FIP1; -.
DR HGNC; HGNC:30265; RAB11FIP1.
DR HPA; ENSG00000156675; Low tissue specificity.
DR MIM; 608737; gene.
DR neXtProt; NX_Q6WKZ4; -.
DR OpenTargets; ENSG00000156675; -.
DR PharmGKB; PA134937501; -.
DR VEuPathDB; HostDB:ENSG00000156675; -.
DR eggNOG; ENOG502QVT0; Eukaryota.
DR GeneTree; ENSGT00940000159649; -.
DR HOGENOM; CLU_015242_0_0_1; -.
DR InParanoid; Q6WKZ4; -.
DR OMA; EFGIHKP; -.
DR OrthoDB; 567750at2759; -.
DR PhylomeDB; Q6WKZ4; -.
DR TreeFam; TF326172; -.
DR PathwayCommons; Q6WKZ4; -.
DR SignaLink; Q6WKZ4; -.
DR BioGRID-ORCS; 80223; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; RAB11FIP1; human.
DR GeneWiki; RAB11FIP1; -.
DR GenomeRNAi; 80223; -.
DR Pharos; Q6WKZ4; Tbio.
DR PRO; PR:Q6WKZ4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6WKZ4; protein.
DR Bgee; ENSG00000156675; Expressed in esophagus squamous epithelium and 197 other tissues.
DR ExpressionAtlas; Q6WKZ4; baseline and differential.
DR Genevisible; Q6WKZ4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:CACAO.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0045055; P:regulated exocytosis; IBA:GO_Central.
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; Cytoplasmic vesicle; Endosome;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1283
FT /note="Rab11 family-interacting protein 1"
FT /id="PRO_0000097304"
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1211..1273
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 161..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1283
FT /note="Necessary for interaction with RAB4A and RAB11A,
FT subcellular location and endosomal recycling"
FT COMPBIAS 165..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D620"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D620"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D620"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..671
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16920206"
FT /id="VSP_013726"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16920206"
FT /id="VSP_013727"
FT VAR_SEQ 116..142
FT /note="RDQGRRKTQWYKLKSKPGKKDKERGEI -> SSLGKSFFKTLKKRAWAIFLR
FT LCLKKN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013728"
FT VAR_SEQ 143..1283
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013729"
FT VAR_SEQ 541..1174
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11786538,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16920206"
FT /id="VSP_013730"
FT VAR_SEQ 1212..1221
FT /note="KYSPSDPAFA -> VCPLRSWCVR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16920206"
FT /id="VSP_013731"
FT VAR_SEQ 1222..1283
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16920206"
FT /id="VSP_013732"
FT VARIANT 622
FT /note="Q -> K (in dbSNP:rs7341564)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16920206"
FT /id="VAR_069365"
FT VARIANT 651
FT /note="A -> V (in dbSNP:rs12541651)"
FT /evidence="ECO:0000269|PubMed:16920206"
FT /id="VAR_059714"
FT VARIANT 768
FT /note="A -> V (in dbSNP:rs16887092)"
FT /id="VAR_056977"
FT VARIANT 1185
FT /note="M -> T (in dbSNP:rs7817179)"
FT /evidence="ECO:0000269|PubMed:11786538,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16920206"
FT /id="VAR_022447"
FT MUTAGEN 1254
FT /note="Y->F: Does not abolish the interaction with RAB11A,
FT homooligomerization and subcellular location. Reduces the
FT interaction with RAB4A."
FT /evidence="ECO:0000269|PubMed:15280022"
FT MUTAGEN 1255
FT /note="I->E: Abolishes the interaction with RAB11A and
FT RAB4A, homooligomerization and subcellular location."
FT /evidence="ECO:0000269|PubMed:15280022"
FT MUTAGEN 1256
FT /note="D->N: Does not abolish the interaction with RAB11A,
FT homooligomerization and subcellular location. Reduces the
FT interaction with RAB4A."
FT /evidence="ECO:0000269|PubMed:15280022"
FT CONFLICT 330..332
FT /note="EAK -> QPT (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="H -> T (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="S -> T (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 380..381
FT /note="QL -> DV (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="S -> T (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="V -> I (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="N -> K (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="P -> L (in Ref. 1; AAM09571)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="D -> G (in Ref. 2; AAQ18788)"
FT /evidence="ECO:0000305"
FT HELIX 1233..1265
FT /evidence="ECO:0007829|PDB:4D0G"
FT HELIX 1267..1270
FT /evidence="ECO:0007829|PDB:4D0G"
SQ SEQUENCE 1283 AA; 137167 MW; 19DF0C848435780B CRC64;
MSLMVSAGRG LGAVWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS
LGAPVWREEA TFELPSLLSS GPAAAATLQL TVLHRALLGL DKFLGRAEVD LRDLHRDQGR
RKTQWYKLKS KPGKKDKERG EIEVDIQFMR NNMTASMFDL SMKDKSRNPF GKLKDKIKGK
NKDSGSDTAS AIIPSTTPSV DSDDESVVKD KKKKSKIKTL LSKSNLQKTP LSQSMSVLPT
SKPEKVLLRP GDFQSQWDED DNEDESSSAS DVMSHKRTAS TDLKQLNQVN FTLPKKEGLS
FLGGLRSKND VLSRSNVCIN GNHVYLEQPE AKGEIKDSSP SSSPSPKGFR KKHLFSSTEN
LAAGSWKEPA EGGGLSSDRQ LSESSTKDSL KSMTLPSYRP APLVSGDLRE NMAPANSEAT
KEAKESKKPE SRRSSLLSLM TGKKDVAKGS EGENPLTVPG REKEGMLMGV KPGEDASGPA
EDLVRRSEKD TAAVVSRQGS SLNLFEDVQI TEPEAEPESK SEPRPPISSP RAPQTRAVKP
RLEVSPEAQP TARLPSPTDS PSSLPPLPSS SGQASVPSEL GHGADTQSSE SPSVFSSLSS
PIAAPISTST PIESWPLVDR GQAKSEGPPL LPKAELQTES LTPVPNSGSS ALGSLFKQPS
FPANKGTEDS LMGRTRETGT EKNTSSLELE ESLPEQPETG RQEEELPRFP CKKQDYSPSS
GEAQEVPFAL SLSSDGAVSP VGELAAGGDR DLESQAGSLV ESKARDAAEE VAPPLPMGAS
VPSIDSMMRK LEEMGLNLRK DQKKTKKRVS FSEQLFTEEA VAGAALLVEG HSSCPQELNP
AWSVAGNASD GEPPESPHAE DSERESVTTP GPATCGAPAS PADHLLLPSQ EESFSEVPMS
EASSAKDTPL FRMEGEDALV TQYQSKASDH EGLLSDPLSD LQLVSDFKSP IMADLNLSLP
SIPEVASDDE RIDQVEDDGD QVEDDGETAK SSTLDIGALS LGLVVPCPER GKGPSGEADR
LVLGEGLCDF RLQAPQASVT APSEQTTEFG IHKPHLGKSS SLDKQLPGPS GGEEEKPMGN
GSPSPPPGTS LDNPVPSPSP SEIFPVTHSF PSSAHSDTHH TSTAESQKKA TAEGSAGRVE
NFGKRKPLLQ AWVSPSETHP VSAQPGAGTG SAKHRLHPVK PMNAMATKVA NCSLGTATII
SENLNNEVMM KKYSPSDPAF AYAQLTHDEL IQLVLKQKET ISKKEFQVRE LEDYIDNLLV
RVMEETPNIL RIPTQVGKKA GKM
