TGFI1_BOVIN
ID TGFI1_BOVIN Reviewed; 456 AA.
AC Q3MHZ4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transforming growth factor beta-1-induced transcript 1 protein;
DE AltName: Full=Hydrogen peroxide-inducible clone 5 protein;
DE Short=Hic-5;
GN Name=TGFB1I1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RT "Bovine genome sequencing program: full-length cDNA sequencing.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-448.
RC STRAIN=Hereford; TISSUE=Fetal ascending colon, and Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15333043; DOI=10.1111/j.1538-7836.2004.00902.x;
RA Panetti T.S., Hannah D.F., Avraamides C.J., Gaughan J.P., Marcinkiewicz C.,
RA Huttenlocher A., Mosher D.F.;
RT "Extracellular matrix molecules regulate endothelial cell migration
RT stimulated by lysophosphatidic acid.";
RL J. Thromb. Haemost. 2:1645-1656(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17337598; DOI=10.1152/ajpheart.00728.2006;
RA Avraamides C.J., Bromberg M.E., Gaughan J.P., Thomas S.M., Tsygankov A.Y.,
RA Panetti T.S.;
RT "Hic-5 promotes endothelial cell migration to lysophosphatidic acid.";
RL Am. J. Physiol. 293:H193-H203(2007).
CC -!- FUNCTION: Functions as a molecular adapter coordinating multiple
CC protein-protein interactions at the focal adhesion complex and in the
CC nucleus. Links various intracellular signaling modules to plasma
CC membrane receptors and regulates the Wnt and TGFB signaling pathways.
CC May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane
CC hence regulating their activity. In the nucleus, functions as a nuclear
CC receptor coactivator regulating glucocorticoid, androgen,
CC mineralocorticoid and progesterone receptor transcriptional activity.
CC May play a role in the processes of cell growth, proliferation,
CC migration, differentiation and senescence. May have a zinc-dependent
CC DNA-binding activity. {ECO:0000269|PubMed:17337598}.
CC -!- SUBUNIT: Homooligomer. Interacts with CRIP2, HSPB1, ILK, LIMS1, LIMS2,
CC NCK2, NUDT16L1, PAK, PPARG, PTPN12, TCF3, TCF7L2 and VCL. Forms a
CC complex with GIT1 and ARHGEF7. Interacts with AR/androgen receptor in a
CC ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG,
CC PTK2/FAK1, PTK2B/PYK2, SLC6A3, SLC6A4, SMAD3, SRC and talin. Interacts
CC (via LIM zinc-binding domain 2) with CBLC (via RING-type zinc finger);
CC the interaction is direct and enhances CBLC E3 ubiquitin-protein ligase
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the actin
CC cytoskeleton, colocalizes with stress fibers. {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding domains mediate glucocorticoid receptor
CC coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG,
CC TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-
CC binding 3 domains mediate targeting to focal adhesions and actin stress
CC fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate
CC interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain
CC mediates interaction with HSPB1, homooligomerization and targeting to
CC the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction
CC with PTPN12 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The LD (leucine and aspartate-rich) motif 3 mediates
CC interaction with GIT1 and functions as a nuclear export signal.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI04511.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DV813479; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC104510; AAI04511.1; ALT_INIT; mRNA.
DR RefSeq; NP_001030390.1; NM_001035313.1.
DR RefSeq; XP_005224965.1; XM_005224908.2.
DR RefSeq; XP_005224966.1; XM_005224909.3.
DR AlphaFoldDB; Q3MHZ4; -.
DR SMR; Q3MHZ4; -.
DR STRING; 9913.ENSBTAP00000003094; -.
DR PaxDb; Q3MHZ4; -.
DR Ensembl; ENSBTAT00000003094; ENSBTAP00000003094; ENSBTAG00000002391.
DR GeneID; 515834; -.
DR KEGG; bta:515834; -.
DR CTD; 7041; -.
DR VEuPathDB; HostDB:ENSBTAG00000002391; -.
DR VGNC; VGNC:35801; TGFB1I1.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000160447; -.
DR HOGENOM; CLU_001357_1_2_1; -.
DR InParanoid; Q3MHZ4; -.
DR OMA; CREPFGD; -.
DR OrthoDB; 1593918at2759; -.
DR TreeFam; TF314113; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000002391; Expressed in vas deferens and 103 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0048495; F:Roundabout binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 4.
DR PIRSF; PIRSF037881; Leupaxin; 1.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cell junction; Cytoplasm; Cytoskeleton;
KW Differentiation; LIM domain; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Wnt signaling pathway; Zinc.
FT CHAIN 1..456
FT /note="Transforming growth factor beta-1-induced transcript
FT 1 protein"
FT /id="PRO_0000291581"
FT DOMAIN 221..280
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 281..338
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 339..398
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 399..456
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..235
FT /note="Interaction with PTK2B/PYK2"
FT /evidence="ECO:0000250"
FT REGION 1..195
FT /note="Transcription activation"
FT /evidence="ECO:0000250"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..131
FT /note="Interaction with PTK2/FAK1"
FT /evidence="ECO:0000250"
FT REGION 109..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="LD motif 1"
FT MOTIF 87..99
FT /note="LD motif 2"
FT MOTIF 152..163
FT /note="LD motif 3"
FT MOTIF 198..210
FT /note="LD motif 4"
FT COMPBIAS 116..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 55
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62219"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43294"
SQ SEQUENCE 456 AA; 49452 MW; 96236F6BA34B736C CRC64;
MEDLDALLSD LETTTSHMPR SGALKERPPE PLTSPLTQMG PGESSGASGD KDHLYSTVCK
PRSPKPAAPA TPPFSSSCGV LGTGLCELDR LLQELNATQF NITDEIMSQF PSSKETAGEQ
KEDQSEDKKR PSPPPSPSPV LPKPSATSAT LELDRLMASL SDFRVQNHLP ASGPTPPPVP
SSMSEDTPSP PGPTSKGSLD TMLGLLQSDL SRRGVPTQAK GLCGSCNKPI AGQVVTALGR
AWHPEHFVCG GCSTALGGSS FFEKDGAPFC PECYFERFSP RCGLCNQPIR HKMVTALGTH
WHPEHFCCVS CGEPFGDEGF HEREGRPYCR RDFLQLFAPR CQGCQGPILD NYISALSALW
HPDCFVCREC FAPFSGGSFF EHEGRPLCEN HFHARRGSLC ATCGLPVTGR CVSALGRRFH
PDHFTCTFCL RPLTKGSFQE RAGKPYCQPC FLKLFG
