RFIP4_MOUSE
ID RFIP4_MOUSE Reviewed; 635 AA.
AC Q8BQP8; Q80T87;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Rab11 family-interacting protein 4;
DE Short=FIP4-Rab11;
DE Short=Rab11-FIP4;
DE Short=mRab11-FIP4A;
GN Name=Rab11fip4; Synonyms=Kiaa1821;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-635.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP INTERACTION WITH RAB11A.
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17089410; DOI=10.1002/dvdy.21009;
RA Muto A., Aoki Y., Watanabe S.;
RT "Mouse Rab11-FIP4 regulates proliferation and differentiation of retinal
RT progenitors in a Rab11-independent manner.";
RL Dev. Dyn. 236:214-225(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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). May play a role in differentiation during retinal
CC development, in a Rab11-independent manner. {ECO:0000250,
CC ECO:0000269|PubMed:17089410}.
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 (By
CC similarity). Interacts with ECPAS (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cleavage furrow
CC {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Recruited to the cleavage furrow and the midbody
CC during cytokinesis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the developing retina.
CC Expressed predominantly in neural tissues.
CC {ECO:0000269|PubMed:17089410}.
CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A
CC or RAB11B). {ECO:0000250}.
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DR EMBL; AK046734; BAC32850.1; -; mRNA.
DR EMBL; AL591174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122559; BAC65841.1; -; mRNA.
DR CCDS; CCDS25123.1; -.
DR RefSeq; NP_780752.1; NM_175543.3.
DR AlphaFoldDB; Q8BQP8; -.
DR SMR; Q8BQP8; -.
DR BioGRID; 234501; 1.
DR STRING; 10090.ENSMUSP00000017783; -.
DR ChEMBL; CHEMBL2176809; -.
DR iPTMnet; Q8BQP8; -.
DR PhosphoSitePlus; Q8BQP8; -.
DR MaxQB; Q8BQP8; -.
DR PaxDb; Q8BQP8; -.
DR PRIDE; Q8BQP8; -.
DR ProteomicsDB; 255180; -.
DR Antibodypedia; 54771; 107 antibodies from 20 providers.
DR DNASU; 268451; -.
DR Ensembl; ENSMUST00000017783; ENSMUSP00000017783; ENSMUSG00000017639.
DR GeneID; 268451; -.
DR KEGG; mmu:268451; -.
DR UCSC; uc007kku.1; mouse.
DR CTD; 84440; -.
DR MGI; MGI:2442920; Rab11fip4.
DR VEuPathDB; HostDB:ENSMUSG00000017639; -.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_018925_1_1_1; -.
DR InParanoid; Q8BQP8; -.
DR OMA; CDNDLTE; -.
DR OrthoDB; 1419449at2759; -.
DR PhylomeDB; Q8BQP8; -.
DR TreeFam; TF327221; -.
DR BioGRID-ORCS; 268451; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rab11fip4; mouse.
DR PRO; PR:Q8BQP8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BQP8; protein.
DR Bgee; ENSMUSG00000017639; Expressed in post-embryonic organism and 248 other tissues.
DR ExpressionAtlas; Q8BQP8; baseline and differential.
DR Genevisible; Q8BQP8; MM.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS: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 Calcium; Cell cycle; Cell division; Coiled coil; Cytoplasmic vesicle;
KW Endosome; Membrane; Metal-binding; Reference proteome; Transport.
FT CHAIN 1..635
FT /note="Rab11 family-interacting protein 4"
FT /id="PRO_0000073881"
FT DOMAIN 49..84
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 572..634
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 82..635
FT /note="Necessary for interaction with RAB11A, subcellular
FT location, homo- or heterooligomerization"
FT /evidence="ECO:0000250"
FT REGION 147..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..615
FT /evidence="ECO:0000255"
FT COMPBIAS 233..258
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 CONFLICT 368..377
FT /note="KQENMQLVHR -> WGTVAPGSAE (in Ref. 3; BAC65841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 71901 MW; 85F3C779A2963AAD CRC64;
MAGGAGWAGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ GEEVEKLVKC
LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL PCSPDIPDCV EQGSDFSGST
DGEQLPREPD FFQEDEEEAM TLALPEGPQE LDMDSPMESS QGPEGSVKGC GEEKEPELGG
LFLPEDKCLV LTPSVTTSDL STHSTASLIS NEEQFEDYGE GDDVDCAPSS PCPDDETRTN
VYSDLGSSVS SSAGQTPRKM RHAYNSELLD VYCSQCCKKI NLLNDLEARL KNLKANSPNR
KISSTAFGRQ LMHNSNFSSS NGSTEDLFRD SIDSCDNDIT EKVSFLEKKV TELENDSLTS
GGLKSKLKQE NMQLVHRVHE LEEMVKDQET TAEQALEEEA RRHREVYCKL EREKSTELEL
LNTRVQQLEE ENTDLRTTVA RLKSQTEKLD EERQRMSDRL EDTSLRLKDE MDLYKRMMDK
LRQNRLEFQK EREATQELIE DLRRELEHLQ MYKLDCERPG RGRSSSGLGE FNARAREVEL
EHEVKRLKQE NHKLRDQNDD LNGQILSLSL YEAKNLFATQ TKAQSLAAEI DTASRDELME
ALKEQEEINF RLRQYMDKII LAILDHNPSI LEIKH
