RFP4A_DANRE
ID RFP4A_DANRE Reviewed; 621 AA.
AC Q3LGD4; Q3LGD3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Rab11 family-interacting protein 4A;
DE Short=FIP4-Rab11;
DE Short=Rab11-FIP4-A;
DE Short=zRab11-FIP4-A;
GN Name=rab11fip4a; Synonyms=rab11fip4;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16457799; DOI=10.1016/j.ydbio.2005.12.050;
RA Muto A., Arai K., Watanabe S.;
RT "Rab11-FIP4 is predominantly expressed in neural tissues and involved in
RT proliferation as well as in differentiation during zebrafish retinal
RT development.";
RL Dev. Biol. 292:90-102(2006).
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. {ECO:0000250, ECO:0000269|PubMed:16457799}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q3LGD4-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q3LGD4-2; Sequence=VSP_038669;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in neural
CC tissues. Isoform B is expressed ubiquitously. In the developing retina,
CC it is expressed in progenitors throughout the retina at early stages
CC and becomes restricted to the ganglion cell layer and ciliary marginal
CC zone as differentiation proceeds. {ECO:0000269|PubMed:16457799}.
CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (rab11a
CC or rab11b). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major form.
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DR EMBL; AB208638; BAE45289.1; -; mRNA.
DR EMBL; AB208639; BAE45290.1; -; mRNA.
DR RefSeq; NP_001002533.2; NM_001002533.2. [Q3LGD4-1]
DR RefSeq; XP_009297806.1; XM_009299531.2. [Q3LGD4-1]
DR RefSeq; XP_009297807.1; XM_009299532.2. [Q3LGD4-2]
DR AlphaFoldDB; Q3LGD4; -.
DR SMR; Q3LGD4; -.
DR STRING; 7955.ENSDARP00000108296; -.
DR PaxDb; Q3LGD4; -.
DR Ensembl; ENSDART00000123505; ENSDARP00000108296; ENSDARG00000090170. [Q3LGD4-1]
DR GeneID; 436806; -.
DR KEGG; dre:436806; -.
DR CTD; 436806; -.
DR ZFIN; ZDB-GENE-040718-266; rab11fip4a.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_018925_2_0_1; -.
DR InParanoid; Q3LGD4; -.
DR OMA; FAIKGFE; -.
DR OrthoDB; 1419449at2759; -.
DR PhylomeDB; Q3LGD4; -.
DR PRO; PR:Q3LGD4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000090170; Expressed in retina and 27 other tissues.
DR ExpressionAtlas; Q3LGD4; baseline.
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:0048592; P:eye morphogenesis; IMP:ZFIN.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ZFIN.
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 Alternative splicing; Calcium; Cell cycle; Cell division; Coiled coil;
KW Cytoplasmic vesicle; Endosome; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..621
FT /note="Rab11 family-interacting protein 4A"
FT /id="PRO_0000390972"
FT DOMAIN 14..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 47..82
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 558..620
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 132..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..556
FT /evidence="ECO:0000255"
FT COMPBIAS 218..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16457799"
FT /id="VSP_038669"
SQ SEQUENCE 621 AA; 70946 MW; 2CA8CADA2BEA00F1 CRC64;
MDGNVFPDQE QLLAFLKKLK EVFDVCDEDA DGYIRVEHFV DLGLQFGQGD EVKKFAKYLD
PNAHGRINFK DFCHGVFAIK GCEEILKSAL GTPTIAAQPY QTDNGYYYQH QEGSLGPPII
VCTRPYPECQ LYSDEEGMGG RDMQESDMDS AADSGAGSES SEGGRQDDKE EGLGGFFLRG
NNCGQMVSSA AASVISVEEQ FEDYGEGEDV DFTPSSPIPD DDTRTNGFSD LGSSLPSSAG
QTPQKIRHLY NSELLDVYCS QCCKKVNLLN DLEARLKNLK ANSPNRKISS TAFGRQLFHH
SNFSSSQGST EDLFRDSIDS CDVDITEKVS YLEKKISELE NDSLANGDLK SKLKQENTQL
VHRVHELEEQ IKDQETRAEQ CLEEELKRHR EAYSKMERDK STEIELLSNR VQQLEEENAE
MKVNVCRLKS QTEKLDQEKQ RMTDKLEDTS LRLKDEMDLY RKMMDKLWQN RHEFQKEREA
MQELIEDLRR ELEHLQLFKL ETEKPGRGRT AAGLSEYNAK TREIELEHEV KRLKQENHKL
RDQNDDLNGQ ILSLSLYEAK NLFACHTKAQ SLAAEIDNAS RDELVDALKE QEEINFRLRQ
YMDKIILAIL DHNPSILEIK H
