RFIP4_HUMAN
ID RFIP4_HUMAN Reviewed; 637 AA.
AC Q86YS3; Q52LI1; Q8N829; Q8NDT7; Q969D8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rab11 family-interacting protein 4;
DE Short=FIP4-Rab11;
DE Short=Rab11-FIP4;
DE AltName: Full=Arfophilin-2;
GN Name=RAB11FIP4; Synonyms=ARFO2, KIAA1821;
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 1), FUNCTION IN ENDOSOMAL TRAFFICKING,
RP SUBUNIT, AND INTERACTION WITH RAB11A.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-637 (ISOFORM 1).
RX PubMed=12696059; DOI=10.1002/gcc.10206;
RA Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K.,
RA Kehrer-Sawatzki H.;
RT "Complete physical map and gene content of the human NF1 tumor suppressor
RT region in human and mouse.";
RL Genes Chromosomes Cancer 37:111-120(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-637 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-637 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12857874; DOI=10.1091/mbc.e03-03-0160;
RA Hickson G.R., Matheson J., Riggs B., Maier V.H., Fielding A.B.,
RA Prekeris R., Sullivan W., Barr F.A., Gould G.W.;
RT "Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling
RT endosome distribution and are related to Drosophila nuclear fallout.";
RL Mol. Biol. Cell 14:2908-2920(2003).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH RAB11A AND ARF6, AND MUTAGENESIS OF
RP ASP-627.
RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R.,
RA Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane
RT traffic in cytokinesis.";
RL EMBO J. 24:3389-3399(2005).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RAB11A.
RX PubMed=15601896; DOI=10.1091/mbc.e04-10-0927;
RA Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S.,
RA Frey A.M., Peden A.A., Gould G.W., Prekeris R.;
RT "The FIP3-Rab11 protein complex regulates recycling endosome targeting to
RT the cleavage furrow during late cytokinesis.";
RL Mol. Biol. Cell 16:849-860(2005).
RN [11]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS GM/UL100 (MICROBIAL INFECTION).
RX PubMed=19761540; DOI=10.1111/j.1600-0854.2009.00967.x;
RA Krzyzaniak M.A., Mach M., Britt W.J.;
RT "HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein
RT FIP4.";
RL Traffic 10:1439-1457(2009).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Acts as a regulator of endocytic traffic by participating in
CC membrane delivery. Required for the abcission step in cytokinesis,
CC possibly by acting as an 'address tag' delivering recycling endosome
CC membranes to the cleavage furrow during late cytokinesis. In case of
CC infection by HCMV (human cytomegalovirus), may participate in egress of
CC the virus out of nucleus; this function is independent of ARF6.
CC {ECO:0000269|PubMed:12470645}.
CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and
CC ARF6. Interacts with RAB11A; the interaction is direct. Forms a
CC heterooligomeric complex with RAB11FIP2, RAB11FIP3 and RAB11FIP5.
CC Interacts with ECPAS. {ECO:0000269|PubMed:11944901,
CC ECO:0000269|PubMed:12470645, ECO:0000269|PubMed:15601896,
CC ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:19761540,
CC ECO:0000269|PubMed:20682791}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 protein gM/UL100. {ECO:0000269|PubMed:19761540}.
CC -!- INTERACTION:
CC Q86YS3; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-949727, EBI-77889;
CC Q86YS3; P62331: Arf6; Xeno; NbExp=2; IntAct=EBI-949727, EBI-988682;
CC Q86YS3-1; P62491: RAB11A; NbExp=2; IntAct=EBI-15605259, EBI-745098;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:20682791}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12857874}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12857874}. Recycling endosome membrane
CC {ECO:0000269|PubMed:15601896}; Peripheral membrane protein. Cleavage
CC furrow {ECO:0000269|PubMed:15601896}. Midbody
CC {ECO:0000269|PubMed:12857874, ECO:0000269|PubMed:15601896}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:15601896}. Note=Recruited to the cleavage
CC furrow and the midbody during cytokinesis.
CC {ECO:0000269|PubMed:15601896}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YS3-2; Sequence=VSP_013724, VSP_013725;
CC -!- TISSUE SPECIFICITY: Present at high level in testis (at protein level).
CC Weakly expressed in other tissues. {ECO:0000269|PubMed:12857874}.
CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A
CC or RAB11B). {ECO:0000250}.
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DR EMBL; AY169244; AAO21970.1; -; mRNA.
DR EMBL; AK097424; BAC05045.1; -; mRNA.
DR EMBL; BC093914; AAH93914.1; -; mRNA.
DR EMBL; BC101517; AAI01518.1; -; mRNA.
DR EMBL; AJ314646; CAC44535.1; -; mRNA.
DR EMBL; AB058724; BAB47450.1; -; mRNA.
DR EMBL; AL831830; CAD38543.1; -; mRNA.
DR CCDS; CCDS11267.1; -. [Q86YS3-1]
DR CCDS; CCDS76985.1; -. [Q86YS3-2]
DR RefSeq; NP_001290471.2; NM_001303542.2. [Q86YS3-2]
DR RefSeq; NP_001333677.1; NM_001346748.1.
DR RefSeq; NP_001333678.1; NM_001346749.1.
DR RefSeq; NP_116321.2; NM_032932.5. [Q86YS3-1]
DR AlphaFoldDB; Q86YS3; -.
DR SMR; Q86YS3; -.
DR BioGRID; 124079; 24.
DR DIP; DIP-47495N; -.
DR IntAct; Q86YS3; 16.
DR MINT; Q86YS3; -.
DR STRING; 9606.ENSP00000482620; -.
DR iPTMnet; Q86YS3; -.
DR PhosphoSitePlus; Q86YS3; -.
DR BioMuta; RAB11FIP4; -.
DR DMDM; 67472134; -.
DR EPD; Q86YS3; -.
DR jPOST; Q86YS3; -.
DR MassIVE; Q86YS3; -.
DR MaxQB; Q86YS3; -.
DR PaxDb; Q86YS3; -.
DR PeptideAtlas; Q86YS3; -.
DR PRIDE; Q86YS3; -.
DR ProteomicsDB; 70461; -. [Q86YS3-1]
DR ProteomicsDB; 70462; -. [Q86YS3-2]
DR Antibodypedia; 54771; 107 antibodies from 20 providers.
DR DNASU; 84440; -.
DR Ensembl; ENST00000394744.6; ENSP00000378227.2; ENSG00000131242.18. [Q86YS3-2]
DR Ensembl; ENST00000621161.5; ENSP00000482620.1; ENSG00000131242.18. [Q86YS3-1]
DR GeneID; 84440; -.
DR KEGG; hsa:84440; -.
DR MANE-Select; ENST00000621161.5; ENSP00000482620.1; NM_032932.6; NP_116321.2.
DR UCSC; uc032fao.2; human. [Q86YS3-1]
DR CTD; 84440; -.
DR DisGeNET; 84440; -.
DR GeneCards; RAB11FIP4; -.
DR HGNC; HGNC:30267; RAB11FIP4.
DR HPA; ENSG00000131242; Tissue enhanced (brain, testis).
DR MIM; 611999; gene.
DR neXtProt; NX_Q86YS3; -.
DR OpenTargets; ENSG00000131242; -.
DR PharmGKB; PA134978007; -.
DR VEuPathDB; HostDB:ENSG00000131242; -.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_018925_1_1_1; -.
DR InParanoid; Q86YS3; -.
DR OMA; CDNDLTE; -.
DR OrthoDB; 1419449at2759; -.
DR PhylomeDB; Q86YS3; -.
DR TreeFam; TF327221; -.
DR PathwayCommons; Q86YS3; -.
DR SignaLink; Q86YS3; -.
DR BioGRID-ORCS; 84440; 22 hits in 1081 CRISPR screens.
DR ChiTaRS; RAB11FIP4; human.
DR GeneWiki; RAB11FIP4; -.
DR GenomeRNAi; 84440; -.
DR Pharos; Q86YS3; Tbio.
DR PRO; PR:Q86YS3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86YS3; protein.
DR Bgee; ENSG00000131242; Expressed in prefrontal cortex and 140 other tissues.
DR ExpressionAtlas; Q86YS3; baseline and differential.
DR Genevisible; Q86YS3; HS.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR037245; FIP-RBD_C_sf.
DR InterPro; IPR019018; Rab-bd_FIP-RBD.
DR Pfam; PF09457; RBD-FIP; 1.
DR SUPFAM; SSF144270; SSF144270; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endosome; Host-virus interaction; Membrane; Metal-binding;
KW Reference proteome; Transport.
FT CHAIN 1..637
FT /note="Rab11 family-interacting protein 4"
FT /id="PRO_0000073880"
FT DOMAIN 49..84
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 574..636
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 82..637
FT /note="Necessary for interaction with RAB11A, subcellular
FT location, homo- or heterooligomerization"
FT REGION 138..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..617
FT /evidence="ECO:0000255"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013724"
FT VAR_SEQ 103..111
FT /note="APEIPDCVE -> MRTPPALGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013725"
FT MUTAGEN 627
FT /note="D->A: Abolishes Rab11-binding."
FT /evidence="ECO:0000269|PubMed:16148947"
FT CONFLICT 417
FT /note="T -> I (in Ref. 2; BAC05045)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="E -> G (in Ref. 2; BAC05045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 71928 MW; 8A5CDB9799383342 CRC64;
MAGGAGWSGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ GEEVEKLVKY
LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL PCAPEIPDCV EQGSEVTGPT
FADGELIPRE PGFFPEDEEE AMTLAPPEGP QELYTDSPME STQSLEGSVG SPAEKDGGLG
GLFLPEDKSL VHTPSMTTSD LSTHSTTSLI SNEEQFEDYG EGDDVDCAPS SPCPDDETRT
NVYSDLGSSV SSSAGQTPRK MRHVYNSELL DVYCSQCCKK INLLNDLEAR LKNLKANSPN
RKISSTAFGR QLMHSSNFSS SNGSTEDLFR DSIDSCDNDI TEKVSFLEKK VTELENDSLT
NGDLKSKLKQ ENTQLVHRVH ELEEMVKDQE TTAEQALEEE ARRHREAYGK LEREKATEVE
LLNARVQQLE EENTELRTTV TRLKSQTEKL DEERQRMSDR LEDTSLRLKD EMDLYKRMMD
KLRQNRLEFQ KEREATQELI EDLRKELEHL QMYKLDCERP GRGRSASSGL GEFNARAREV
ELEHEVKRLK QENYKLRDQN DDLNGQILSL SLYEAKNLFA AQTKAQSLAA EIDTASRDEL
MEALKEQEEI NFRLRQYMDK IILAILDHNP SILEIKH
