RFIP4_XENTR
ID RFIP4_XENTR Reviewed; 633 AA.
AC A4IIE8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Rab11 family-interacting protein 4;
DE Short=FIP4-Rab11;
DE Short=Rab11-FIP4;
GN Name=rab11fip4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (rab11a or rab11b) and
CC arf6 (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 -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (rab11a
CC or rab11b). {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; BC135989; AAI35990.1; -; mRNA.
DR RefSeq; NP_001096170.1; NM_001102700.1.
DR AlphaFoldDB; A4IIE8; -.
DR SMR; A4IIE8; -.
DR DNASU; 100124715; -.
DR GeneID; 100124715; -.
DR KEGG; xtr:100124715; -.
DR CTD; 84440; -.
DR Xenbase; XB-GENE-6454385; rab11fip4.
DR InParanoid; A4IIE8; -.
DR OrthoDB; 1419449at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
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 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 2: Evidence at transcript level;
KW Calcium; Cell cycle; Cell division; Coiled coil; Cytoplasmic vesicle;
KW Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..633
FT /note="Rab11 family-interacting protein 4"
FT /id="PRO_0000390974"
FT DOMAIN 17..52
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 570..632
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 152..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 410..613
FT /evidence="ECO:0000255"
FT COMPBIAS 232..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 71734 MW; 0EDEDE8A97E26C88 CRC64;
MERGSCSAPG DPGHLGLFLQ RLRQVFDACD GDADGFIKVE HFVALGLQFA QGDEVKKLAK
RLDPNAQGRI GFKDFCHGVL AMKGCDKFVK GILGVTGTAP QHYEAPYTPY YYQSPETIEG
PFLDTESSYS DSEFFAYEDG LTLSHRDAQH ESDLDSAMYS TPSSEASDEG RNEDKAGGLG
SLYLPGEQNL LKPSAGSGFS THSTASLISN EEQFEDYGEG EDIDYSPGSP CPDDESRTNA
LSDLGSSVPS SAGQTPRKAR LMYNTDLLDI YCTQCSKKIT LLNDLEARLK NLKANSPNRK
ISSTAFGRQL LHNSNLSSSN GSTEDLFRDS IDSCENDITE KVSFLEKKVT ELENDNLTNG
DVKNKLKHEN IHLVHRVHEL EEFLRDQETK SEQVLDEESK RHRETYSKLA REKGTEIVLL
SARVQELQEE NEDLLTSLTR LKSHTVRIDE ERQRVWDKLE DTSLRLKDET DLYKRLMDKL
RQNRLHFQKE REATQELIED LRRELDHLQI YKLECERSGR GPPSGLTELN VKSREVELEQ
EIRRLKQDNQ KLRDQNDDLN GQILSLSLYE AKSLFSTQTK AQSLAAEIDS ASKDELMEAL
KEQEEINYRL RQYMDKIILA ILDHNPSILE IKN
