TGFI1_XENLA
ID TGFI1_XENLA Reviewed; 506 AA.
AC Q2TCH4; A0JMS0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Transforming growth factor beta-1-induced transcript 1 protein;
DE AltName: Full=Androgen receptor activator of 55 kDa;
DE AltName: Full=Hydrogen peroxide-inducible clone 5 protein;
DE Short=Hic-5;
GN Name=tgfb1i1; Synonyms=ara55;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH TCF3 AND TCF7L2.
RC TISSUE=Tail bud;
RX PubMed=16291758; DOI=10.1074/jbc.m505869200;
RA Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.;
RT "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-
RT driven transcription.";
RL J. Biol. Chem. 281:1755-1764(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a molecular adapter coordinating multiple
CC protein-protein interactions at the focal adhesion complex and in the
CC nucleus. May regulate both Wnt and steroid signaling pathways and play
CC a role in the processes of cell growth, proliferation, migration,
CC differentiation and senescence. May have a zinc-dependent DNA-binding
CC activity. {ECO:0000269|PubMed:16291758}.
CC -!- SUBUNIT: Interacts with tcf3 and tcf7l2. {ECO:0000269|PubMed:16291758}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Associated with the actin cytoskeleton; colocalizes with stress
CC fibers. {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding domains mediate glucocorticoid receptor
CC coactivation and mediates interaction with tcf3 and tcf7l2. The LIM
CC zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to
CC focal adhesions and actin stress fibers. The LIM zinc-binding 4 domain
CC mediates targeting to the nuclear matrix (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The LD (leucine and aspartate-rich) motif 3 functions as a
CC nuclear export signal. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25984.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY971603; AAY40865.1; -; mRNA.
DR EMBL; BC125983; AAI25984.1; ALT_INIT; mRNA.
DR RefSeq; NP_001090425.2; NM_001096956.1.
DR AlphaFoldDB; Q2TCH4; -.
DR SMR; Q2TCH4; -.
DR BioGRID; 608044; 1.
DR IntAct; Q2TCH4; 1.
DR DNASU; 779337; -.
DR GeneID; 779337; -.
DR KEGG; xla:779337; -.
DR CTD; 779337; -.
DR Xenbase; XB-GENE-866238; tgfb1i1.L.
DR OrthoDB; 1593918at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 779337; Expressed in lung and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Activator; Cell junction; Cytoplasm; Cytoskeleton; Differentiation;
KW LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Wnt signaling pathway; Zinc.
FT CHAIN 1..506
FT /note="Transforming growth factor beta-1-induced transcript
FT 1 protein"
FT /id="PRO_0000291585"
FT DOMAIN 271..330
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 331..388
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 389..448
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 449..506
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 15..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..244
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 139..150
FT /note="LD motif 3"
FT MOTIF 248..260
FT /note="LD motif 4"
FT COMPBIAS 31..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 51
FT /note="K -> T (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="D -> H (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> N (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="S -> A (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..166
FT /note="VEAPGAY -> GEVPDSN (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..176
FT /note="SRPG -> FKPR (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="L -> P (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..189
FT /note="STAC -> DTLD (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> A (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..199
FT /note="APT -> IPS (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..208
FT /note="FKVVSA -> SEVMST (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> M (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="TN -> ID (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="E -> K (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="V -> L (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="Y -> H (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="T -> A (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="S -> T (in Ref. 2; AAI25984)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> D (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="C -> R (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="V -> I (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="T -> A (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="N -> S (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="E -> G (in Ref. 1; AAY40865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56001 MW; 1097E3A0DDC61A32 CRC64;
MEDLDALLAD LQITTPPRCP VLLTDSPEKP QPTETRPPPP PYDPKTAMSN KTSDHETFPV
DKDHLYSTVQ KYPLPSVSPA LGGGLCELDR LLNELNATQF NITDEIMSQF PTRDPSEQKA
EAQKEAEKRA LSASSATLEL DRLMASLSDF HKQNTVSQEV EAPGAYKGSE EVSRPGDTED
LSSPRSTACV PKDLEDAPTP KSFKVVSAPG HLEVKTNQVN SDEVTASRVP DSVSGSKVPE
ATSVPRSDLD SMLVKLQSGL KQQGIETYSK GLCESCQRPI AGQVVTALGH TWHPEHFVCA
HCHTLIGTSN FFEKDGRPYC EKDYFMLYAP RCALCELPIV QNMVTALGCT WHPEHFCCKV
CKKPIGEEGF HEKDGEQYCS DDYFRLFGAV CAGCTEAVKE SYISALGGLW HPQCFVCHVC
HTPFINGSFF EHEGLPLCET HYHSRRGSLC AGCEQPITGR CVTAMGKKFH PQHLNCTFCL
RQLNKGTFRE HDEKPYCQAC YARLYG
