ID   RFP4B_DANRE             Reviewed;         502 AA.
AC   B3DGU2;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Rab11 family-interacting protein 4B;
DE            Short=FIP4-Rab11-B;
DE            Short=Rab11-FIP4-B;
GN   Name=rab11fip4b;
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 [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) 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}.
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DR   EMBL; BC162520; AAI62520.1; -; mRNA.
DR   RefSeq; NP_001122297.1; NM_001128825.1.
DR   AlphaFoldDB; B3DGU2; -.
DR   SMR; B3DGU2; -.
DR   STRING; 7955.ENSDARP00000125009; -.
DR   PaxDb; B3DGU2; -.
DR   Ensembl; ENSDART00000159747; ENSDARP00000132572; ENSDARG00000103207.
DR   Ensembl; ENSDART00000167798; ENSDARP00000135008; ENSDARG00000103207.
DR   Ensembl; ENSDART00000171097; ENSDARP00000139004; ENSDARG00000103207.
DR   GeneID; 100151129; -.
DR   KEGG; dre:100151129; -.
DR   CTD; 100151129; -.
DR   ZFIN; ZDB-GENE-080722-8; rab11fip4b.
DR   eggNOG; KOG0982; Eukaryota.
DR   GeneTree; ENSGT00440000033742; -.
DR   HOGENOM; CLU_018925_1_0_1; -.
DR   InParanoid; B3DGU2; -.
DR   OMA; HASRDQK; -.
DR   OrthoDB; 1419449at2759; -.
DR   PhylomeDB; B3DGU2; -.
DR   TreeFam; TF327221; -.
DR   PRO; PR:B3DGU2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 6.
DR   Bgee; ENSDARG00000103207; Expressed in granulocyte and 20 other tissues.
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: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; IPR037245; FIP-RBD_C_sf.
DR   InterPro; IPR019018; Rab-bd_FIP-RBD.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SUPFAM; SSF144270; SSF144270; 1.
DR   PROSITE; PS51511; FIP_RBD; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasmic vesicle; Endosome;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..502
FT                   /note="Rab11 family-interacting protein 4B"
FT                   /id="PRO_0000390973"
FT   DOMAIN          439..501
FT                   /note="FIP-RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          228..482
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  57908 MW;  29783ACA0378C9D4 CRC64;
     MSIQECPESP MLEGEEGRGV ERDSDRDSAV DSASEISDGG RTGEKEEGIG ICLPREKGDL
     MHNHFEISDQ SALSSASLNE EQFEDYGEGE DGDCTTSSPC PDDEIRINGC SDLGSSVSSS
     AGQTPRKIHN VDDQMEVFCS QCCKRVSLLS DLENRLKNLK TSSPNRKISS TAFGRKLLHN
     SNISSSNGST EDLFHDSTDS SDLDITEKVS YLDKKVTELE NEILMSGDVK TKLKQENIQL
     VHRIHELEEQ LKDQETRAEK IMEDELRRHR DAYIRLEKDK NTQIELLRNR LHQLEDENGK
     MAMNMNRLKS QTEKLDEEKQ RMTDKLEDTS LRLKDEMDLY KKMMDKLRQN RQEFQRERDT
     MQELIEDLRR ELEHLQLYKL EAERAGRGRR SSISLSEYSS RTRESELEQE VRRLKQDNQK
     LREQNEDLNG QLLSLSLHEA KNLFATQTKA QSLAMEIDHA SRDQLLEALK QQEEINLRLR
     QYMDKIILSI LDHNPSILEI KN