RFIP1_RAT
ID RFIP1_RAT Reviewed; 648 AA.
AC Q3B7T9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Rab11 family-interacting protein 1;
DE Short=Rab11-FIP1;
DE AltName: Full=Rab-coupling protein;
GN Name=Rab11fip1 {ECO:0000250|UniProtKB:Q6WKZ4};
GN Synonyms=Rcp {ECO:0000250|UniProtKB:Q6WKZ4};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-347; SER-349 AND
RP SER-361, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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).
CC {ECO:0000250|UniProtKB:Q6WKZ4}.
CC -!- SUBUNIT: Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and RAB25
CC (By similarity). {ECO:0000250|UniProtKB:Q6WKZ4}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC107469; AAI07470.1; -; mRNA.
DR RefSeq; NP_001178484.1; NM_001191555.1.
DR RefSeq; NP_001184170.1; NM_001197241.1.
DR AlphaFoldDB; Q3B7T9; -.
DR SMR; Q3B7T9; -.
DR BioGRID; 269960; 1.
DR IntAct; Q3B7T9; 1.
DR STRING; 10116.ENSRNOP00000067013; -.
DR iPTMnet; Q3B7T9; -.
DR jPOST; Q3B7T9; -.
DR PRIDE; Q3B7T9; -.
DR Ensembl; ENSRNOT00000086082; ENSRNOP00000073557; ENSRNOG00000058940.
DR GeneID; 498650; -.
DR KEGG; rno:498650; -.
DR UCSC; RGD:1562965; rat.
DR CTD; 80223; -.
DR RGD; 1562965; Rab11fip1.
DR eggNOG; ENOG502QVT0; Eukaryota.
DR GeneTree; ENSGT00940000159649; -.
DR HOGENOM; CLU_015242_0_0_1; -.
DR InParanoid; Q3B7T9; -.
DR OrthoDB; 567750at2759; -.
DR PRO; PR:Q3B7T9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000058940; Expressed in jejunum and 18 other tissues.
DR ExpressionAtlas; Q3B7T9; baseline and differential.
DR Genevisible; Q3B7T9; RN.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:RGD.
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..648
FT /note="Rab11 family-interacting protein 1"
FT /id="PRO_0000234531"
FT DOMAIN 1..129
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 576..638
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 164..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..648
FT /note="Necessary for interaction with RAB4A and RAB11A,
FT subcellular location and endosomal recycling"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D620"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D620"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ4"
SQ SEQUENCE 648 AA; 71143 MW; A4C70DDB1A540F3A CRC64;
MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS
LGAPVWREEA TFELPPLLSS GTAPAAAAAT LQLTVLHRAL LGLDKFLGRA EVDLRELHRD
QSRRKKQWYT LKSKPGKKDK ERGEIEVDIQ FMRNNMTASM FDLSMKDKSR NPFGKLKDKI
KGKNKDNTSD TASAIVPSTT PSVDSDDESF SKDKKKKSKI KTLFSKPSLQ KTPLSQSMSV
LPTSKPDKVL LRPGDFQSRW GDEGDNEDES SSASEVMSQK RTSSTDHTQP NQSNFSLPKK
EGLSFLGGLR SKNDSLSRSN VCINGNHVYM EQPEAKSEIR ESSPSNSPSP QGFRKRHLFS
STENLAARSP KEPGEGGGMS SDRRLSDSST KDSMKSMSLP SYRPLTTADS REGLSPANME
VATKETKDSK KQESKKSSLL SLVTGKKDVA KGSEGEPLPP VSEKEKGRKG VLVEAQLREE
DLVRRPEKDA VPVASQWGSS QNPFEDAQIS DLEASVESKC EPKPPVPVPR TPQTRAVKPR
PHPVKPMNTT APKITNSSLG TATIISENLI NEALMKKYQP SDPAFAYAQL THDELIQLVL
KQKETISKKE FQVRELEDYI DNLLVRVMEE TPNILRVPAQ TGKKAGKM
