RFIP3_MOUSE
ID RFIP3_MOUSE Reviewed; 1047 AA.
AC Q8CHD8; Q8JZT3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Rab11 family-interacting protein 3;
DE Short=FIP3-Rab11;
DE Short=Rab11-FIP3;
GN Name=Rab11fip3; Synonyms=Kiaa0665;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-1047 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH ASAP1.
RX PubMed=18685082; DOI=10.1091/mbc.e08-03-0290;
RA Inoue H., Ha V.L., Prekeris R., Randazzo P.A.;
RT "Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and
RT regulates pericentrosomal localization of transferrin receptor-positive
RT recycling endosome.";
RL Mol. Biol. Cell 19:4224-4237(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). Also required for the structural integrity of the
CC endosomal recycling compartment during interphase. Acts as an adapter
CC protein linking the dynein motor complex to various cargos and converts
CC dynein from a non-processive to a highly processive motor in the
CC presence of dynactin. Facilitates the interaction between dynein and
CC dynactin and activates dynein processivity (the ability to move along a
CC microtubule for a long distance without falling off the track) (By
CC similarity). {ECO:0000250|UniProtKB:O75154,
CC ECO:0000269|PubMed:18685082}.
CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and
CC ARF6. Interacts with RAB11A; the interaction is direct. Interacts with
CC RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6. Interacts with
CC RACGAP1/MgcRacGAP; interaction takes place during late stage of
CC cytokinesis and is required for recruitment to the midbody. Interacts
CC with EXOC7 (By similarity). Interacts with ASAP1 (PubMed:18685082).
CC Interacts with dynein intermediate chain and dynactin (DCTN1) (By
CC similarity). {ECO:0000250|UniProtKB:O75154,
CC ECO:0000269|PubMed:18685082}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O75154}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O75154}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O75154}. Cleavage
CC furrow {ECO:0000250|UniProtKB:O75154}. Midbody
CC {ECO:0000250|UniProtKB:O75154}. Note=In early mitosis remains diffuse
CC and distributed through the cell. The onset of anaphase sequesters
CC these vesicles to the centrosomes at the opposite poles of the cell.
CC During telophase these vesicles move from the centrosomes, to the
CC furrow, and then to the midbody to aid in abscission. Interaction with
CC Rab11 mediates localization to endosomes. Interaction with ARF6
CC mediates localization to the midbody. {ECO:0000250|UniProtKB:O75154}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CHD8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHD8-2; Sequence=VSP_038667;
CC Name=3;
CC IsoId=Q8CHD8-3; Sequence=VSP_038668;
CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A
CC or RAB11B). {ECO:0000250|UniProtKB:O75154}.
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DR EMBL; AC140047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023364; AAH23364.1; -; mRNA.
DR EMBL; BC037132; AAH37132.1; -; mRNA.
DR EMBL; AB093257; BAC41441.1; -; mRNA.
DR CCDS; CCDS50039.1; -. [Q8CHD8-2]
DR CCDS; CCDS50040.1; -. [Q8CHD8-1]
DR CCDS; CCDS50041.1; -. [Q8CHD8-3]
DR RefSeq; NP_001156340.1; NM_001162868.1. [Q8CHD8-1]
DR RefSeq; NP_001156341.1; NM_001162869.1. [Q8CHD8-3]
DR RefSeq; NP_694780.1; NM_153140.2. [Q8CHD8-2]
DR AlphaFoldDB; Q8CHD8; -.
DR SMR; Q8CHD8; -.
DR BioGRID; 229626; 2.
DR IntAct; Q8CHD8; 1.
DR MINT; Q8CHD8; -.
DR STRING; 10090.ENSMUSP00000113521; -.
DR iPTMnet; Q8CHD8; -.
DR PhosphoSitePlus; Q8CHD8; -.
DR MaxQB; Q8CHD8; -.
DR PaxDb; Q8CHD8; -.
DR PRIDE; Q8CHD8; -.
DR ProteomicsDB; 255296; -. [Q8CHD8-1]
DR ProteomicsDB; 255297; -. [Q8CHD8-2]
DR ProteomicsDB; 255298; -. [Q8CHD8-3]
DR Antibodypedia; 22705; 93 antibodies from 25 providers.
DR DNASU; 215445; -.
DR Ensembl; ENSMUST00000118828; ENSMUSP00000113048; ENSMUSG00000037098. [Q8CHD8-2]
DR Ensembl; ENSMUST00000120691; ENSMUSP00000112875; ENSMUSG00000037098. [Q8CHD8-1]
DR Ensembl; ENSMUST00000122103; ENSMUSP00000113521; ENSMUSG00000037098. [Q8CHD8-3]
DR Ensembl; ENSMUST00000148021; ENSMUSP00000119626; ENSMUSG00000037098. [Q8CHD8-2]
DR GeneID; 215445; -.
DR KEGG; mmu:215445; -.
DR UCSC; uc008bdc.2; mouse. [Q8CHD8-2]
DR UCSC; uc008bdd.2; mouse. [Q8CHD8-3]
DR UCSC; uc008bde.2; mouse. [Q8CHD8-1]
DR CTD; 9727; -.
DR MGI; MGI:2444431; Rab11fip3.
DR VEuPathDB; HostDB:ENSMUSG00000037098; -.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_018925_2_0_1; -.
DR InParanoid; Q8CHD8; -.
DR OrthoDB; 1419449at2759; -.
DR PhylomeDB; Q8CHD8; -.
DR TreeFam; TF327221; -.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 215445; 1 hit in 68 CRISPR screens.
DR ChiTaRS; Rab11fip3; mouse.
DR PRO; PR:Q8CHD8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CHD8; protein.
DR Bgee; ENSMUSG00000037098; Expressed in right kidney and 213 other tissues.
DR Genevisible; Q8CHD8; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
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 InterPro; IPR032920; Rab11-FIP3.
DR PANTHER; PTHR15726:SF6; PTHR15726:SF6; 1.
DR Pfam; PF09457; RBD-FIP; 1.
DR SUPFAM; SSF144270; SSF144270; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Endosome; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..1047
FT /note="Rab11 family-interacting protein 3"
FT /id="PRO_0000390970"
FT DOMAIN 496..531
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 528..563
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 985..1047
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..879
FT /note="ARF-binding domain (ABD)"
FT /evidence="ECO:0000250"
FT REGION 882..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 750..985
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT VAR_SEQ 1..603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_038667"
FT VAR_SEQ 712
FT /note="P -> PSSNPLASKLCDVLTDEAFEFYCSQCHKQINRLEDLSARLTDLEMN
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038668"
SQ SEQUENCE 1047 AA; 118535 MW; 4A78951AFB9696C4 CRC64;
MELCQPTSLS DHDQPASGPQ RGVMGLVGPD APRGWSEEPE EHAQLQRWPE GPNAPICWPE
EVEEPHAPSR WAKEPNAPRC SSQEPDESCH LAEELEESDS PRCWPQEPDT PCHLAKELEE
PDAPRCLPQE PDTPCYLAKE LEEPNIPRCW PQEPDVPCHL AKELEEPDAP RCWPQEPDAF
CHLLKEVEEP DALRCWLQGP DAPCHLAKEL EDLDSPRCWP QEPDESCHLA KELEEPDAPC
HLAKELEEPD APRCWPQEPD VPCLLAKKWE ESDAPCLLTE ELEEPDALHC WPQESEAPCL
LAKELEEPDA SHSCPQEADT GCLSAKEPEE PDVSHLWQGV PDAPCLLVKE PEEADALHCC
WPEESEEPDA LNPPCFWANE PDEPDPSRCW SEEPQVLCLW PEEQNTKRCW QEEPDAPCFW
PEDREEPIVS CLQFKEPEKP KVRSSWPEEL EDCCPTRGLP LEPLLADGEL LQACPGPPSD
PGPALSLPSE PGTAQEEGAR LRAVFDALDR DGDGFVRIED FIQFATVYGA EQVKDLTQYL
DPSGLGVISF EDFYQGIVAI RNGDPDGQLY SVEPVQDEET PACADEFDDF VTYEANEVTD
SAYMGSESTY SECETFTDED TSTLVHPELQ PEGDVDSAGG SGVPSECLDT MEEPDHGALL
LLPGRSRPHS QAVVMVIGSE EHFEDYGEGN EAELSPETLC DGDGEDPAFL TPSPAKRLSS
RKVARYLHQS GTLTMEALED PPPEPVECPE EDIADKVIFL ERRVSELEKD SAAAGEQHGR
LRQENLQLVH RANALEEQLK EQEFRAQEKV LEETRKQKEL LCKMEREKSI EIENLQARLQ
QLDEENSELR SCTPCLKANI ERLEEEKQKM LDEIEELTQR LSEEQENKRK MGDRLSHERH
QFQRDKEATQ ELIEDLRKQL EHLQLLRLEV EQRRGRSSSL GLQEYNSRAR ESELEQEVRR
LKQDNRNLKE QNDELNGQII TLSIQGAKSL FSTSFSESLA AEISSVSRDE LMEAIQKQEE
INFRLQDYID RIIVAILETN PSILEVK
