RFIP5_HUMAN
ID RFIP5_HUMAN Reviewed; 653 AA.
AC Q9BXF6; O94939; Q9P0M1;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Rab11 family-interacting protein 5 {ECO:0000312|HGNC:HGNC:24845};
DE Short=Rab11-FIP5 {ECO:0000303|PubMed:33315947};
DE AltName: Full=Gamma-SNAP-associated factor 1 {ECO:0000312|HGNC:HGNC:24845};
DE Short=Gaf-1 {ECO:0000303|PubMed:11278501};
DE AltName: Full=Phosphoprotein pp75 {ECO:0000312|HGNC:HGNC:24845};
DE AltName: Full=Rab11-interacting protein Rip11 {ECO:0000303|PubMed:11163216};
GN Name=RAB11FIP5 {ECO:0000312|HGNC:HGNC:24845};
GN Synonyms=GAF1 {ECO:0000312|HGNC:HGNC:24845},
GN KIAA0857 {ECO:0000312|HGNC:HGNC:24845},
GN RIP11 {ECO:0000312|HGNC:HGNC:24845};
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], FUNCTION, INTERACTION WITH RAB11A, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11163216; DOI=10.1016/s1097-2765(00)00140-4;
RA Prekeris R., Klumperman J., Scheller R.H.;
RT "A Rab11/Rip11 protein complex regulates apical membrane trafficking via
RT recycling endosomes.";
RL Mol. Cell 6:1437-1448(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
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. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 105-653, INTERACTION WITH RO60,
RP IDENTIFICATION AS ANTIGEN IN AUTOIMMUNE DISEASES, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RC TISSUE=Keratinocyte;
RX PubMed=10545525; DOI=10.1172/jci8003;
RA Wang D., Buyon J.P., Zhu W., Chan E.K.L.;
RT "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and
RT identification of distinct human autoantibodies.";
RL J. Clin. Invest. 104:1265-1275(1999).
RN [5]
RP INTERACTION WITH NAPG, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11278501; DOI=10.1074/jbc.m009424200;
RA Chen D., Xu W., He P., Medrano E.E., Whiteheart S.W.;
RT "Gaf-1, a gamma-SNAP-binding protein associated with the mitochondria.";
RL J. Biol. Chem. 276:13127-13135(2001).
RN [6]
RP INTERACTION WITH RAB11FIP4.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-307; SER-494 AND
RP SER-538, AND IDENTIFICATION BY 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 [12]
RP FUNCTION.
RX PubMed=20717956; DOI=10.1002/jcp.22388;
RA Oehlke O., Martin H.W., Osterberg N., Roussa E.;
RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-
RT ATPase in salivary ducts.";
RL J. Cell. Physiol. 226:638-651(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-307; SER-357;
RP SER-367; SER-391; SER-395 AND SER-494, AND IDENTIFICATION BY MASS
RP 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 [14]
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).
RN [15]
RP INTERACTION WITH KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS/HHV-8 PROTEIN
RP ORF45 (MICROBIAL INFECTION).
RX PubMed=33315947; DOI=10.1371/journal.ppat.1009099;
RA Wei X., Dong J., Cheng C.C., Ji M., Yu L., Luo S., Wu S., Bai L., Lan K.;
RT "Host RAB11FIP5 protein inhibits the release of Kaposi's sarcoma-associated
RT herpesvirus particles by promoting lysosomal degradation of ORF45.";
RL PLoS Pathog. 16:e1009099-e1009099(2020).
CC -!- FUNCTION: Rab effector involved in protein trafficking from apical
CC recycling endosomes to the apical plasma membrane. Involved in insulin
CC granule exocytosis. May regulate V-ATPase intracellular transport in
CC response to extracellular acidosis. {ECO:0000269|PubMed:11163216,
CC ECO:0000269|PubMed:20717956}.
CC -!- SUBUNIT: Interacts with RAB11FIP4 (PubMed:11278501, PubMed:12470645).
CC Interacts with NAPG (PubMed:11278501). Interacts with RO60
CC (PubMed:10545525). Interacts with RAB11A that has been activated by GTP
CC binding (PubMed:11163216). {ECO:0000269|PubMed:10545525,
CC ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:11278501,
CC ECO:0000269|PubMed:12470645}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Kaposi's sarcoma-
CC associated herpesvirus/HHV-8 protein ORF45; this interaction results in
CC the lysosomal degradation of ORF45 and the inhibition of viral particle
CC release. {ECO:0000269|PubMed:33315947}.
CC -!- INTERACTION:
CC Q9BXF6; Q9Y496: KIF3A; NbExp=2; IntAct=EBI-1387068, EBI-1104844;
CC Q9BXF6; P62491: RAB11A; NbExp=4; IntAct=EBI-1387068, EBI-745098;
CC Q9BXF6; Q96RF0: SNX18; NbExp=3; IntAct=EBI-1387068, EBI-298169;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane;
CC Peripheral membrane protein. Early endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Mitochondrion membrane; Peripheral membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Detected at low levels in heart, brain, placenta,
CC lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas.
CC {ECO:0000269|PubMed:10545525, ECO:0000269|PubMed:11278501}.
CC -!- DOMAIN: Binds to vesicles enriched in neutral phospholipids via its C2
CC domain. The interaction is favored by Mg(2+) rather than Ca(2+).
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylation
CC at Ser-357 is PKA-dependent. {ECO:0000269|PubMed:10545525}.
CC -!- MISCELLANEOUS: Antibodies against RIP11 are found in sera from patients
CC with autoimmune diseases such as systemic lupus erythematosus (SLE) or
CC Sjoegren syndrome (SS). It is also found in the sera from mothers of
CC children with neonatal lupus erythematosus (NLE).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF334812; AAK20892.1; -; mRNA.
DR EMBL; AB020664; BAA74880.1; ALT_INIT; mRNA.
DR EMBL; BC035013; AAH35013.1; -; mRNA.
DR EMBL; AF153085; AAF34356.1; -; mRNA.
DR CCDS; CCDS1923.1; -.
DR PIR; T17312; T17312.
DR RefSeq; NP_056285.1; NM_015470.2.
DR AlphaFoldDB; Q9BXF6; -.
DR SMR; Q9BXF6; -.
DR BioGRID; 117518; 147.
DR IntAct; Q9BXF6; 36.
DR MINT; Q9BXF6; -.
DR STRING; 9606.ENSP00000258098; -.
DR iPTMnet; Q9BXF6; -.
DR PhosphoSitePlus; Q9BXF6; -.
DR BioMuta; RAB11FIP5; -.
DR DMDM; 34223002; -.
DR EPD; Q9BXF6; -.
DR jPOST; Q9BXF6; -.
DR MassIVE; Q9BXF6; -.
DR MaxQB; Q9BXF6; -.
DR PaxDb; Q9BXF6; -.
DR PeptideAtlas; Q9BXF6; -.
DR PRIDE; Q9BXF6; -.
DR ProteomicsDB; 79420; -.
DR Antibodypedia; 31309; 126 antibodies from 26 providers.
DR DNASU; 26056; -.
DR Ensembl; ENST00000258098.6; ENSP00000258098.6; ENSG00000135631.17.
DR GeneID; 26056; -.
DR KEGG; hsa:26056; -.
DR UCSC; uc002siu.4; human.
DR CTD; 26056; -.
DR DisGeNET; 26056; -.
DR GeneCards; RAB11FIP5; -.
DR HGNC; HGNC:24845; RAB11FIP5.
DR HPA; ENSG00000135631; Tissue enhanced (testis).
DR MIM; 605536; gene.
DR neXtProt; NX_Q9BXF6; -.
DR OpenTargets; ENSG00000135631; -.
DR PharmGKB; PA134971129; -.
DR VEuPathDB; HostDB:ENSG00000135631; -.
DR eggNOG; ENOG502QQKU; Eukaryota.
DR GeneTree; ENSGT00940000158783; -.
DR HOGENOM; CLU_015242_2_0_1; -.
DR InParanoid; Q9BXF6; -.
DR OrthoDB; 567750at2759; -.
DR PhylomeDB; Q9BXF6; -.
DR TreeFam; TF326172; -.
DR PathwayCommons; Q9BXF6; -.
DR SignaLink; Q9BXF6; -.
DR SIGNOR; Q9BXF6; -.
DR BioGRID-ORCS; 26056; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; RAB11FIP5; human.
DR GeneWiki; RAB11FIP5; -.
DR GenomeRNAi; 26056; -.
DR Pharos; Q9BXF6; Tbio.
DR PRO; PR:Q9BXF6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BXF6; protein.
DR Bgee; ENSG00000135631; Expressed in sperm and 205 other tissues.
DR ExpressionAtlas; Q9BXF6; baseline and differential.
DR Genevisible; Q9BXF6; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:CACAO.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
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; 2.
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 Cytoplasm; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Host-virus interaction; Membrane; Mitochondrion; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..653
FT /note="Rab11 family-interacting protein 5"
FT /id="PRO_0000097307"
FT DOMAIN 5..146
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 586..648
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 269..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R361"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R361"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R361"
FT CONFLICT 176
FT /note="Missing (in Ref. 3; AAH35013)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="E -> G (in Ref. 3; AAH35013)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="H -> N (in Ref. 3; AAH35013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 70415 MW; 716725537AA9D86E CRC64;
MALVRGAEPA AGPSRWLPTH VQVTVLRARG LRGKSSGAGS TSDAYTVIQV GREKYSTSVV
EKTHGCPEWR EECSFELPPG ALDGLLRAQE ADAGPAPWAA SSAAACELVL TTMHRSLIGV
DKFLGQATVA LDEVFGAGRA QHTQWYKLHS KPGKKEKERG EIEVTIQFTR NNLSASMFDL
SMKDKPRSPF SKIRDKMKGK KKYDLESASA ILPSSAIEDP DLGSLGKMGK AKGFFLRNKL
RKSSLTQSNT SLGSDSTLSS ASGSLAYQGP GAELLTRSPS RSSWLSTEGG RDSAQSPKLF
THKRTYSDEA NQMRVAPPRA LLDLQGHLDA ASRSSLCVNG SHIYNEEPQG PVRHRSSISG
SLPSSGSLQA VSSRFSEEGP RSTDDTWPRG SRSNSSSEAV LGQEELSAQA KVLAPGASHP
GEEEGARLPE GKPVQVATPI VASSEAVAEK EGARKEERKP RMGLFHHHHQ GLSRSELGRR
SSLGEKGGPI LGASPHHSSS GEEKAKSSWF GLREAKDPTQ KPSPHPVKPL SAAPVEGSPD
RKQSRSSLSI ALSSGLEKLK TVTSGSIQPV TQAPQAGQMV DTKRLKDSAV LDQSAKYYHL
THDELISLLL QRERELSQRD EHVQELESYI DRLLVRIMET SPTLLQIPPG PPK
