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Q8CJ53

- CIP4_MOUSE

UniProt

Q8CJ53 - CIP4_MOUSE

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Protein

Cdc42-interacting protein 4

Gene

Trip10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL (By similarity). Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei166 – 1661Mediates end-to-end attachment of dimersBy similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. endocytosis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_210090. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42-interacting protein 4
Alternative name(s):
Thyroid receptor-interacting protein 10
Short name:
TR-interacting protein 10
Short name:
TRIP-10
Gene namesi
Name:Trip10
Synonyms:Cip4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:2146901. Trip10.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcell cortex. Lysosome. Golgi apparatus By similarity. Cell membrane. Cell projectionphagocytic cup By similarity
Note: Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9 (By similarity). Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ.By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. Golgi apparatus Source: UniProtKB-KW
  4. lysosome Source: UniProtKB-KW
  5. microtubule Source: MGI
  6. nucleus Source: Ensembl
  7. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi454 – 4541I → S: Impairs interaction with CDC42 and RHOQ and reduces insulin-stimulated translocation to the plasma membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Cdc42-interacting protein 4PRO_0000261439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineBy similarity

Post-translational modificationi

Tyrosine phosphorylated. Also phosphorylated by PKA (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CJ53.
PaxDbiQ8CJ53.
PRIDEiQ8CJ53.

PTM databases

PhosphoSiteiQ8CJ53.

Expressioni

Gene expression databases

BgeeiQ8CJ53.
CleanExiMM_TRIP10.
GenevestigatoriQ8CJ53.

Interactioni

Subunit structurei

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures (By similarity). Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and WAS/WASP. Interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. May interact with CTNNB1 and HD/HTT (By similarity). Interacts specifically with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL.By similarity3 Publications

Protein-protein interaction databases

BioGridi223098. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8CJ53.
SMRiQ8CJ53. Positions 10-288, 384-481, 546-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
BLAST
Repeati405 – 48177REMAdd
BLAST
Domaini542 – 60362SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 288288F-BAR domainBy similarityAdd
BLAST
Regioni1 – 117117Required for podosome formation and interaction with AKAP9 and microtubulesBy similarityAdd
BLAST
Regioni1 – 117117Required for translocation to the plasma membrane in response to insulinAdd
BLAST
Regioni293 – 603311Interaction with PDE6GBy similarityAdd
BLAST
Regioni293 – 539247Interaction with CDC42By similarityAdd
BLAST
Regioni471 – 603133Required for interaction with FASLG and localization to lysosomesBy similarityAdd
BLAST
Regioni487 – 54357Interaction with DNM2 and WASLAdd
BLAST
Regioni532 – 60372Interaction with DNM1 and WASLBy similarityAdd
BLAST
Regioni540 – 60364Required for podosome formationBy similarityAdd
BLAST
Regioni546 – 60358Interaction with WASBy similarityAdd
BLAST
Regioni548 – 60356Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 259193By similarityAdd
BLAST
Coiled coili388 – 48194By similarityAdd
BLAST

Domaini

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).By similarity

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 FCH domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG323796.
GeneTreeiENSGT00510000046403.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ8CJ53.
KOiK07196.
OMAiSPKFGRD.
OrthoDBiEOG780RQK.
PhylomeDBiQ8CJ53.
TreeFamiTF351162.

Family and domain databases

InterProiIPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF7. PTHR12602:SF7. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CJ53-1) [UniParc]FASTAAdd to Basket

Also known as: Cip4/2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERAEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPTK DDPEVKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL
110 120 130 140 150
ELAKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAHTAERLDQ DINATKADVE KAKQQAHLRN HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ VVPIIGKCLE
260 270 280 290 300
GMKVAAESVD AKNDSQVLIE LHKSGFARPG DLEFEDFSQV INRVPSDSSL
310 320 330 340 350
GTPDGRPELR AASSRSRAKR WPFGKKNKPR PPSLSLLGGH LPSTLSDGPS
360 370 380 390 400
SPRSGRDPLA ILSEISKSVK PRLASFRSFR GGRGTVATED FSHLPPEQQR
410 420 430 440 450
KRLQQQLEER NRELQKEEDQ REALKKMKDV YEKTPQMGDP ASLEPRIAET
460 470 480 490 500
LGNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPTTAPPDS
510 520 530 540 550
SSSSTNSGSQ DNKESSSEEP PSEGQDTPIY TEFDEDFEEP ASPIGQCVAI
560 570 580 590 600
YHFEGSSEGT VSMSEGEDLS LMEEDKGDGW TRVRRKQGAE GYVPTSYLRV

TLN
Length:603
Mass (Da):68,489
Last modified:November 28, 2006 - v2
Checksum:iDDA6271D5FD515AC
GO
Isoform 2 (identifier: Q8CJ53-2) [UniParc]FASTAAdd to Basket

Also known as: H

The sequence of this isoform differs from the canonical sequence as follows:
     515-515: Missing.

Show »
Length:602
Mass (Da):68,402
Checksum:i165D63A9EC6CD884
GO
Isoform 3 (identifier: Q8CJ53-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.

Show »
Length:547
Mass (Da):62,654
Checksum:i5DE65DB3D6C9B8E2
GO
Isoform 4 (identifier: Q8CJ53-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
     515-515: Missing.

Show »
Length:546
Mass (Da):62,567
Checksum:i8627CD20F0C19667
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211W → C in AAN38709. (PubMed:12242347)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei329 – 38456Missing in isoform 3 and isoform 4. 2 PublicationsVSP_021722Add
BLAST
Alternative sequencei515 – 5151Missing in isoform 2 and isoform 4. 2 PublicationsVSP_021723

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY081142 mRNA. Translation: AAL89589.1.
AF502565 mRNA. Translation: AAN38709.1.
AK088909 mRNA. Translation: BAC40648.1.
AK149902 mRNA. Translation: BAE29155.1.
BC003249 mRNA. Translation: AAH03249.1.
CCDSiCCDS28930.1. [Q8CJ53-3]
RefSeqiNP_001229318.1. NM_001242389.1. [Q8CJ53-1]
NP_001229319.1. NM_001242390.1. [Q8CJ53-2]
NP_001229320.1. NM_001242391.1. [Q8CJ53-4]
NP_598886.1. NM_134125.4. [Q8CJ53-3]
UniGeneiMm.37368.

Genome annotation databases

EnsembliENSMUST00000019631; ENSMUSP00000019631; ENSMUSG00000019487. [Q8CJ53-3]
GeneIDi106628.
KEGGimmu:106628.
UCSCiuc008dej.2. mouse. [Q8CJ53-3]
uc008dek.2. mouse. [Q8CJ53-1]
uc008del.2. mouse. [Q8CJ53-2]
uc008dem.2. mouse. [Q8CJ53-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY081142 mRNA. Translation: AAL89589.1 .
AF502565 mRNA. Translation: AAN38709.1 .
AK088909 mRNA. Translation: BAC40648.1 .
AK149902 mRNA. Translation: BAE29155.1 .
BC003249 mRNA. Translation: AAH03249.1 .
CCDSi CCDS28930.1. [Q8CJ53-3 ]
RefSeqi NP_001229318.1. NM_001242389.1. [Q8CJ53-1 ]
NP_001229319.1. NM_001242390.1. [Q8CJ53-2 ]
NP_001229320.1. NM_001242391.1. [Q8CJ53-4 ]
NP_598886.1. NM_134125.4. [Q8CJ53-3 ]
UniGenei Mm.37368.

3D structure databases

ProteinModelPortali Q8CJ53.
SMRi Q8CJ53. Positions 10-288, 384-481, 546-601.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223098. 1 interaction.

PTM databases

PhosphoSitei Q8CJ53.

Proteomic databases

MaxQBi Q8CJ53.
PaxDbi Q8CJ53.
PRIDEi Q8CJ53.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019631 ; ENSMUSP00000019631 ; ENSMUSG00000019487 . [Q8CJ53-3 ]
GeneIDi 106628.
KEGGi mmu:106628.
UCSCi uc008dej.2. mouse. [Q8CJ53-3 ]
uc008dek.2. mouse. [Q8CJ53-1 ]
uc008del.2. mouse. [Q8CJ53-2 ]
uc008dem.2. mouse. [Q8CJ53-4 ]

Organism-specific databases

CTDi 9322.
MGIi MGI:2146901. Trip10.

Phylogenomic databases

eggNOGi NOG323796.
GeneTreei ENSGT00510000046403.
HOGENOMi HOG000231767.
HOVERGENi HBG002489.
InParanoidi Q8CJ53.
KOi K07196.
OMAi SPKFGRD.
OrthoDBi EOG780RQK.
PhylomeDBi Q8CJ53.
TreeFami TF351162.

Enzyme and pathway databases

Reactomei REACT_210090. Rho GTPase cycle.

Miscellaneous databases

NextBioi 358316.
PROi Q8CJ53.
SOURCEi Search...

Gene expression databases

Bgeei Q8CJ53.
CleanExi MM_TRIP10.
Genevestigatori Q8CJ53.

Family and domain databases

InterProi IPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR12602:SF7. PTHR12602:SF7. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
    Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
    Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Heart.
  2. "The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes."
    Chang L., Adams R.D., Saltiel A.R.
    Proc. Natl. Acad. Sci. U.S.A. 99:12835-12840(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42 AND RHOQ, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-454.
    Tissue: Adipocyte.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow and Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 98-104, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle."
    Archila S., King M.A., Carlson G.M., Rice N.A.
    Biochem. Biophys. Res. Commun. 345:1592-1599(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
    Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
    J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION.
  8. "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes."
    Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M., Pessin J.E., Saltiel A.R.
    Cell Metab. 5:59-72(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAPVD1.

Entry informationi

Entry nameiCIP4_MOUSE
AccessioniPrimary (citable) accession number: Q8CJ53
Secondary accession number(s): Q8BTR8, Q8R433, Q99LI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3