ID   CIP4_DANRE              Reviewed;         542 AA.
AC   Q5U3Q6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cdc42-interacting protein 4 homolog;
DE   AltName: Full=Thyroid receptor-interacting protein 10 homolog;
GN   Name=trip10; Synonyms=cip4; ORFNames=zgc:101777;
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].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required to coordinate membrane tubulation with
CC       reorganization of the actin cytoskeleton during endocytosis.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC       filamentous structures. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       cell cortex {ECO:0000250}. Lysosome {ECO:0000250}. Cell membrane
CC       {ECO:0000250}.
CC   -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC       concave surface. The end-to-end polymerization of dimers of these
CC       domains provides a curved surface that fits best membranes with around
CC       600 A diameter, and may drive tubulation (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR   EMBL; BC085435; AAH85435.1; -; mRNA.
DR   RefSeq; NP_001007404.1; NM_001007403.1.
DR   AlphaFoldDB; Q5U3Q6; -.
DR   SMR; Q5U3Q6; -.
DR   STRING; 7955.ENSDARP00000105597; -.
DR   PRIDE; Q5U3Q6; -.
DR   GeneID; 492762; -.
DR   KEGG; dre:492762; -.
DR   CTD; 492762; -.
DR   ZFIN; ZDB-GENE-041114-105; trip10a.
DR   eggNOG; KOG3565; Eukaryota.
DR   InParanoid; Q5U3Q6; -.
DR   PhylomeDB; Q5U3Q6; -.
DR   Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR   PRO; PR:Q5U3Q6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR028498; CIP4.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15735:SF17; PTHR15735:SF17; 2.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW   Lipid-binding; Lysosome; Membrane; Reference proteome; SH3 domain.
FT   CHAIN           1..542
FT                   /note="Cdc42-interacting protein 4 homolog"
FT                   /id="PRO_0000261442"
FT   DOMAIN          1..264
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          340..417
FT                   /note="REM-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          480..541
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   COILED          67..259
FT                   /evidence="ECO:0000250"
FT   COILED          335..423
FT                   /evidence="ECO:0000250"
FT   SITE            166
FT                   /note="Mediates end-to-end attachment of dimers"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  62195 MW;  6BF6D6EDE2279409 CRC64;
     MDWGTELWDQ YDILDKHTQS GLDLVDKYMK FVKERTDIEQ NYAKQLRNLT KKYSPKRGSK
     EEQECRFSNH QAFLDILNEM NDYAGQRELI AENMMINICV ELNKYLQELK QERKMHLSEA
     KKSQQSLEAM YKQLDNSKKR FEREWREAEK AAQYADKTDQ DLNATKADVE KAKQQAHLRT
     HIAEDCKNDY AAQLQKYNKG QSQFYFTDMP QIFNKLQDMD ERRIKKMAQG YILFADTERH
     VMPIIGKCLE GMTRAGTNVN ARNDSMVLIE QHKSGFERPG DLDFEDYSQG INRASSDSSL
     GTPKGPLELL GKNKNKTFRL FNKKSKFTPE KPVDTEGFTH LPPEQRRKRL QQKIDDMSKE
     LQKEMDQSEA LGKMKDVYEK NPQMGDPASL APQIGQTAQN MDRLRGELNK YESWLAEAGG
     RGDSIRYSTH SINNNGAHNP NSHDGSCTLF SPGALSDETD PSQAIYTEFD DEFEEEELAT
     PIGQCTALYN FPGSSEGTIS MQEGEVLAVV EEDKGDGWTR VRRNNGDEGY IPTSYATITL
     NK