RFIP3_DANRE
ID RFIP3_DANRE Reviewed; 1183 AA.
AC Q7T005;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Rab11 family-interacting protein 3;
DE Short=FIP3-Rab11;
DE Short=Rab11-FIP3;
GN Name=rab11fip3; ORFNames=si:ch211-153c20.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(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. Also required
CC for the structural integrity of the endosomal recycling compartment
CC during interphase. May act as an adapter protein linking the dynein
CC motor complex to various cargos. {ECO:0000250|UniProtKB:O75154}.
CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (rab11a or rab11b) and
CC arf6. {ECO:0000250|UniProtKB:O75154}.
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.
CC {ECO:0000250|UniProtKB:O75154}.
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; AL772148; CAE30388.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7T005; -.
DR SMR; Q7T005; -.
DR PaxDb; Q7T005; -.
DR PRIDE; Q7T005; -.
DR Ensembl; ENSDART00000136836; ENSDARP00000120017; ENSDARG00000016490.
DR ZFIN; ZDB-GENE-040724-138; rab11fip3.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_272729_0_0_1; -.
DR PRO; PR:Q7T005; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000016490; Expressed in retina and 18 other tissues.
DR ExpressionAtlas; Q7T005; baseline.
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:0030496; C:midbody; ISS:UniProtKB.
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: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: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 Pfam; PF09457; RBD-FIP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF144270; SSF144270; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 3: Inferred from homology;
KW Calcium; Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..1183
FT /note="Rab11 family-interacting protein 3"
FT /id="PRO_0000390971"
FT DOMAIN 706..741
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 738..773
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1121..1183
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 423..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1015
FT /note="ARF-binding domain (ABD)"
FT /evidence="ECO:0000250"
FT REGION 1005..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 902..1121
FT /evidence="ECO:0000255"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 723
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 730
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 751
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 753
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 762
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 131440 MW; 8D03C70D03F8EC80 CRC64;
MEQVLSSPQG CSEWEVNGKT EWESDQNPLG FLLVDKENSS VADPTNEIFQ ENAINLDDLF
WASQTYSWEN GLDCVYPEWK AQPPPSQDLK GDGNSGISQL VEGDLICFNS RSASPSLADR
PVQDNNLYDH AEQVEVTATS STLNVCTGEL GINAPTLHTD KTLLQDTHLM LEESHLTNCE
FSCNSGVENE SQNFLSHGTR NILESEGLFA VSPVEVSCVD TNSNPKPTIV CQTPPLASEH
IYLSSSALPC EPVFPMTCTK PHVPPYHAGS ATLPMDEVEM MLPKLQGGEG ESSKPSANNR
TLEPQRLDAN TDTTHLSVCP LGESDISPEH CEEMLHELST KCTVEMVEEE VNKKSVSSNT
TNTAFSKPKT ELCEELSGCT LGVLLETVSG DVKEEAASDS RTDHVFPETQ TDLAPVALID
SQAEDPSTES LPRKNGQEES KSALPVSTPE HNALFELSSG NVVLPEDHSQ STFSAQTQAL
SEVDHDGDLT PDGMLTDNIV CEAVTSIDSV ILSLTDSFEL PKLSDCDLSS HDFESHALTL
EIQNNVTCVQ TGSVDNNPEE MSTPFTCTDN QLTVTGGLAG LDLTETTSQS GEASGEGEAG
LPVLPTHQED FHQLTPSEIN LAQEQQVSSV VPSSPPSHRD VFPCGASLDG EAYLTLMENN
PDTLKHAEMT LDLCKASDAL PTKSLQIAPV DLIHVPIVSA TAPRSEEQSA LRAVFQALDQ
DGDGFVHIEE FIEFAKAYGA EQVKDLTRFL DPSGLGVISF EDFHRGISAI SNEESAYSEC
ETFTDEDTTA LVHPELHEDV ETDSGIENTL TDGDDRNSPS SFPASFQNFL QSEALEFFCT
HCHKQISRLE DLSTRLQLLE MNRHLQQSNN LDVMGDLTQD ILDLADRDIT DKVLLLEKRV
CELEKDSLES EEQHARLRQE NLTLVHRANA LEEQLKEQEL RTEEDLLAQT RKHRDALNKL
QRERDLEIEN LQARLHQLDE ENSELRSCVP CLRANIERLE EEKRKLQDEA DDITQRLNEE
SESRRKMSDK LSHERHTNQK EKECTQGLIE DLRKQLEHLQ LFKLETEARR GRSSSNGLQE
YNTHMRENEL EQEIRRLKQD NRSLKEQNDE LNGQIINLSI QGAKSLFTES LSESLAAEIN
NVSRAELMEA IHKQEEINFR LQDYIDRIIV AIMESNPSIL EVK
