RFIP1_MOUSE
ID RFIP1_MOUSE Reviewed; 645 AA.
AC Q9D620; Q05A58; Q3UBC2; Q8BN24;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Rab11 family-interacting protein 1;
DE Short=Rab11-FIP1;
DE AltName: Full=Rab-coupling protein;
GN Name=Rab11fip1; Synonyms=Rcp;
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=Bone marrow, and Head;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-344 AND SER-346, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-204; SER-236;
RP SER-340; SER-342; SER-344; SER-346 AND SER-383, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: A Rab11 effector protein involved in the endosomal recycling
CC process. Also involved in controlling membrane trafficking along the
CC phagocytic pathway and phagocytosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and RAB25
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000250}. Note=Membrane-bound. RAB11A
CC rather than RAB4A mediates RAB11FIP1 localization in the endocytic
CC recycling compartment (ERC). Colocalizes with RAB11A at phagosomes (By
CC similarity). {ECO:0000250}.
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DR EMBL; AK014696; BAB29507.1; -; mRNA.
DR EMBL; AK151024; BAE30042.1; -; mRNA.
DR EMBL; CH466580; EDL32793.1; -; Genomic_DNA.
DR EMBL; BC125400; AAI25401.1; -; mRNA.
DR EMBL; BC132094; AAI32095.1; -; mRNA.
DR CCDS; CCDS52534.1; -.
DR RefSeq; NP_083699.2; NM_029423.2.
DR AlphaFoldDB; Q9D620; -.
DR SMR; Q9D620; -.
DR BioGRID; 217725; 14.
DR IntAct; Q9D620; 12.
DR STRING; 10090.ENSMUSP00000058042; -.
DR iPTMnet; Q9D620; -.
DR EPD; Q9D620; -.
DR jPOST; Q9D620; -.
DR MaxQB; Q9D620; -.
DR PaxDb; Q9D620; -.
DR PeptideAtlas; Q9D620; -.
DR PRIDE; Q9D620; -.
DR ProteomicsDB; 254919; -.
DR Antibodypedia; 4467; 214 antibodies from 36 providers.
DR DNASU; 75767; -.
DR Ensembl; ENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
DR GeneID; 75767; -.
DR KEGG; mmu:75767; -.
DR UCSC; uc009lia.2; mouse.
DR CTD; 80223; -.
DR MGI; MGI:1923017; Rab11fip1.
DR VEuPathDB; HostDB:ENSMUSG00000031488; -.
DR eggNOG; ENOG502QVT0; Eukaryota.
DR GeneTree; ENSGT00940000159649; -.
DR HOGENOM; CLU_015242_0_0_1; -.
DR InParanoid; Q9D620; -.
DR BioGRID-ORCS; 75767; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rab11fip1; mouse.
DR PRO; PR:Q9D620; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D620; protein.
DR Bgee; ENSMUSG00000031488; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; Q9D620; baseline and differential.
DR Genevisible; Q9D620; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0045055; P:regulated exocytosis; IBA:GO_Central.
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 Cytoplasmic vesicle; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..645
FT /note="Rab11 family-interacting protein 1"
FT /id="PRO_0000097305"
FT DOMAIN 1..128
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 573..635
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 171..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..645
FT /note="Necessary for interaction with RAB4A and RAB11A,
FT subcellular location and endosomal recycling"
FT /evidence="ECO:0000250"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT CONFLICT 60
FT /note="S -> T (in Ref. 1; BAB29507)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> K (in Ref. 1; BAE30042)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Q -> H (in Ref. 1; BAE30042)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="T -> A (in Ref. 1; BAE30042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 70684 MW; 667E0D12EC5FBD3B CRC64;
MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS
LGAPVWREEA TFELPPLLSS GAAPAAAATL QLTVLHRALL GLDKFLGRAE VDLRELHRDQ
GRRKKQWYTL KSKPGKKDKE RGEIEVDIQF MRNNMTASMF DLSMKDKSRN PFGKLKDKIK
GKNKDSASDT ASAIVPSVTP SVDSDDESFS KDKKKKSKIK TLFSKSSLQK TPLSQSMSVL
PTSKSDKVLL RAGDFQSQWD DDAHEDESSS ASDVMSHKRT SSTDQQPNQS NFSLPKKEGL
SFLGGLRSKN DSLSRSTVCI NGNHVYMEQP EARSEIRESS PSNSPSPQGF RRKHLFSSTE
NLAARSPKEP GEGGGTSSDR RLSDSSTKDS MKSMSLPSYR PLTSGDNRES MSPANVEAAR
ETKDSKKQES KKSSLLSLVT GKRDAAAKGS ESEPLPTVSE KEKERKGALV EAQLREEDLM
RRPEKDALPV ASQWGSSLNP FEDVQISDPG ATTESRSEPK PPVPAARVPQ TKAVKPRPHP
VKPMNTTATK IANSSLGTAT IITENLISEA LMKKYQPSDP AFAYAQLTHD ELIQLVLKQK
ETISKKEFQV RELEDYIDNL LVRVMEETPN ILRVPAQMGK KAGKM
