CIP4_PONAB
ID CIP4_PONAB Reviewed; 601 AA.
AC Q5RCJ1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Cdc42-interacting protein 4;
DE AltName: Full=Thyroid receptor-interacting protein 10;
DE Short=TR-interacting protein 10;
DE Short=TRIP-10;
GN Name=TRIP10; Synonyms=CIP4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
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. Also acts
CC as a link between CDC42 signaling and regulation of the actin
CC cytoskeleton. Binds to lipids such as phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylserine and promotes membrane invagination
CC and the formation of tubules. Also enhances actin polymerization in the
CC vicinity of membrane tubules by recruiting WASL/N-WASP which in turn
CC activates the Arp2/3 complex. Actin polymerization and dynamin may
CC promote the fission of membrane tubules to form endocytic vesicles.
CC Required for the formation of podosomes, actin-rich adhesion structures
CC specific to monocyte-derived cells. Required for translocation of GLUT4
CC to the plasma membrane in response to insulin signaling. May be
CC required for the lysosomal retention of FASLG/FASL (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1,
CC DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and
CC WAS/WASP. Interacts with the ligand binding domain of the thyroid
CC receptor (TR) in the presence of thyroid hormone. May interact with
CC CTNNB1 and HD/HTT (By similarity). Interacts specifically with GTP-
CC bound CDC42 and RHOQ. Interacts with DNM2 and WASL (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000250}. Lysosome {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, phagocytic
CC cup {ECO:0000250}. Note=Localizes to cortical regions coincident with
CC F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also
CC localizes to the Golgi, and this requires AKAP9. Translocates to the
CC plasma membrane in response to insulin stimulation, and this may
CC require active RHOQ (By similarity). {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 -!- PTM: Tyrosine phosphorylated. Also phosphorylated by PKA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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; CR858279; CAH90516.1; -; mRNA.
DR RefSeq; NP_001125273.1; NM_001131801.1.
DR AlphaFoldDB; Q5RCJ1; -.
DR BMRB; Q5RCJ1; -.
DR SMR; Q5RCJ1; -.
DR STRING; 9601.ENSPPYP00000010610; -.
DR GeneID; 100172170; -.
DR KEGG; pon:100172170; -.
DR CTD; 9322; -.
DR eggNOG; KOG3565; Eukaryota.
DR InParanoid; Q5RCJ1; -.
DR OrthoDB; 348563at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; 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; 1.
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; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Golgi apparatus; Lipid-binding; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..601
FT /note="Cdc42-interacting protein 4"
FT /id="PRO_0000261440"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 393..470
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 540..601
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..117
FT /note="Required for translocation to the plasma membrane in
FT response to insulin, podosome formation and interaction
FT with AKAP9 and microtubules"
FT /evidence="ECO:0000250"
FT REGION 280..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..601
FT /note="Interaction with PDE6G"
FT /evidence="ECO:0000250"
FT REGION 293..537
FT /note="Interaction with CDC42"
FT /evidence="ECO:0000250"
FT REGION 390..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..601
FT /note="Required for interaction with FASLG and localization
FT to lysosomes"
FT /evidence="ECO:0000250"
FT REGION 478..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..541
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000250"
FT REGION 529..601
FT /note="Interaction with DNM1 and WASL"
FT /evidence="ECO:0000250"
FT REGION 538..601
FT /note="Required for podosome formation"
FT /evidence="ECO:0000250"
FT REGION 544..601
FT /note="Interaction with WAS"
FT /evidence="ECO:0000250"
FT REGION 546..601
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000250"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 388..481
FT /evidence="ECO:0000250"
FT COMPBIAS 327..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
SQ SEQUENCE 601 AA; 68403 MW; 40CB45B55D79E8FA CRC64;
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK
DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG
RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS
HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE
VVPIIAKCLE GMKVAANAVD PKNDSQVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA
ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ
REALKKMKDV YEKTPQMGDP ASLEPQITET LSNIERLKLE VQKYEAWLAE AESRVLSNRG
DSLSRHARPP DPPTSAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS
PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL
N
