CIP4_RAT
ID CIP4_RAT Reviewed; 547 AA.
AC P97531; Q6P744;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cdc42-interacting protein 4;
DE AltName: Full=Salt tolerant protein;
DE AltName: Full=Thyroid receptor-interacting protein 10;
DE Short=TR-interacting protein 10;
DE Short=TRIP-10;
GN Name=Trip10; Synonyms=Cip4, Stp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=8954095; DOI=10.1006/bbrc.1996.1769;
RA Tsuji E., Tsuji Y., Misumi Y., Fujita A., Sasaguri M., Ideishi M.,
RA Arakawa K.;
RT "Molecular cloning of a novel rat salt-tolerant protein by functional
RT complementation in yeast.";
RL Biochem. Biophys. Res. Commun. 229:134-138(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 391-402, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP INTERACTION WITH PDE6G.
RX PubMed=14502124;
RA Morin F., Vannier B., Houdart F., Regnacq M., Berges T., Voisin P.;
RT "A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates
RT interaction with SH3-containing proteins.";
RL Mol. Vis. 9:449-459(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 specifically with GTP-bound CDC42 and
CC RHOQ. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1,
CC DNM2, FASLG/FASL, GAPVD1, LYN, microtubules, SRC, WAS/WASP and WASL/N-
CC WASP. Interacts with the ligand binding domain of the thyroid receptor
CC (TR) in the presence of thyroid hormone. May interact with CTNNB1 and
CC HD/HTT (By similarity). Interacts with PDE6G. {ECO:0000250,
CC ECO:0000269|PubMed:14502124}.
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 -!- TISSUE SPECIFICITY: Expressed in adrenal gland, aorta, brain, heart,
CC kidney, liver, skeletal muscle and spleen.
CC {ECO:0000269|PubMed:8954095}.
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; AB006914; BAA22191.1; -; mRNA.
DR EMBL; BC061840; AAH61840.1; -; mRNA.
DR PIR; JC5261; JC5261.
DR RefSeq; NP_446372.1; NM_053920.1.
DR AlphaFoldDB; P97531; -.
DR SMR; P97531; -.
DR BioGRID; 250584; 1.
DR iPTMnet; P97531; -.
DR PhosphoSitePlus; P97531; -.
DR SwissPalm; P97531; -.
DR jPOST; P97531; -.
DR PRIDE; P97531; -.
DR GeneID; 116717; -.
DR KEGG; rno:116717; -.
DR CTD; 9322; -.
DR RGD; 621145; Trip10.
DR InParanoid; P97531; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; P97531; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR PRO; PR:P97531; -.
DR Proteomes; UP000002494; 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:0042802; F:identical protein binding; ISO:RGD.
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:0001837; P:epithelial to mesenchymal transition; IMP:RGD.
DR GO; GO:0042538; P:hyperosmotic salinity response; IDA:RGD.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endocytosis; Golgi apparatus; Lipid-binding;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..547
FT /note="Cdc42-interacting protein 4"
FT /id="PRO_0000261441"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 337..414
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 486..547
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 293..547
FT /note="Interaction with PDE6G"
FT /evidence="ECO:0000269|PubMed:14502124"
FT REGION 293..483
FT /note="Interaction with CDC42"
FT /evidence="ECO:0000250"
FT REGION 294..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..547
FT /note="Required for interaction with FASLG and localization
FT to lysosomes"
FT /evidence="ECO:0000250"
FT REGION 420..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..487
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000250"
FT REGION 476..547
FT /note="Interaction with DNM1 and WASL"
FT /evidence="ECO:0000250"
FT REGION 484..547
FT /note="Required for podosome formation"
FT /evidence="ECO:0000250"
FT REGION 490..547
FT /note="Interaction with WAS"
FT /evidence="ECO:0000250"
FT REGION 492..547
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000250"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 332..425
FT /evidence="ECO:0000250"
FT COMPBIAS 442..458
FT /note="Polar 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:0007744|PubMed:22673903"
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 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT CONFLICT 402..403
FT /note="KL -> NV (in Ref. 1; BAA22191)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="S -> T (in Ref. 1; BAA22191)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="K -> M (in Ref. 1; BAA22191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 62799 MW; EE995A691E661DE5 CRC64;
MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERVEVEQ SYAKQLRSLV KKYLPKRPAK
DDPEIKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL ELAKYSQEMK QERKMHFQEG
RRAQQQLENG FKQLENSKRK FERDCREAEK AAHTAERLDQ DINATKADVE KAKQQAHLRN
HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ
VVPIIGKCLE GMKVAAESVD AKNDSKVLIE LHKSGFARPG DLEFEDFSQV MNRVPSDSSL
GTPDGRPELR AASSRSRAKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERNRELQK
EEDQREALKK MKDVYEKTPQ MGDPASLEPR IAETLGNIER LKLEVQKYEA WLAEAESRVL
SNRGDSLSRH TRPPDPPTTA PPDSSSSSNN SGSQDNKESS EEPPSEEGQD TPIYTEFDED
FEEPASPIGQ CVAIYHFEGS SEGTVSMSEG EDLSLMEEDK GDGWTRVRRK QGGEGYVPTS
YLRVTLN
