ID A0A3Q2FYS8_CYPVA Unreviewed; 423 AA.
AC A0A3Q2FYS8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Transforming growth factor beta-1-induced transcript 1 protein {ECO:0000256|PIRNR:PIRNR037881};
GN Name=TGFB1I1 {ECO:0000313|Ensembl:ENSCVAP00000013675.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000013675.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000013675.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|PIRNR:PIRNR037881}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|PIRNR:PIRNR037881}. Nucleus matrix
CC {ECO:0000256|PIRNR:PIRNR037881}. Cytoplasm, cytoskeleton
CC {ECO:0000256|PIRNR:PIRNR037881}.
CC -!- DOMAIN: The LD (leucine and aspartate-rich) motif 3 mediates
CC interaction with GIT1 and functions as a nuclear export signal.
CC {ECO:0000256|PIRNR:PIRNR037881}.
CC -!- SIMILARITY: Belongs to the paxillin family.
CC {ECO:0000256|ARBA:ARBA00005813, ECO:0000256|PIRNR:PIRNR037881}.
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DR AlphaFoldDB; A0A3Q2FYS8; -.
DR Ensembl; ENSCVAT00000030813.1; ENSCVAP00000013675.1; ENSCVAG00000016278.1.
DR GeneTree; ENSGT00940000160447; -.
DR Proteomes; UP000265020; Unplaced.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd09336; LIM1_Paxillin_like; 1.
DR CDD; cd09409; LIM3_Paxillin; 1.
DR CDD; cd09339; LIM4_Paxillin_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR InterPro; IPR047075; Paxillin_TGFB1I1_LIM_dom1.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24205; FOUR AND A HALF LIM DOMAINS PROTEIN; 1.
DR PANTHER; PTHR24205:SF4; LIM DOMAIN FAMILY; 1.
DR Pfam; PF00412; LIM; 4.
DR PIRSF; PIRSF037881; Leupaxin; 1.
DR SMART; SM00132; LIM; 4.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR037881};
KW Differentiation {ECO:0000256|PIRNR:PIRNR037881};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PIRNR:PIRNR037881};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Nucleus {ECO:0000256|PIRNR:PIRNR037881};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Wnt signaling pathway {ECO:0000256|PIRNR:PIRNR037881};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 188..246
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 247..306
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 307..365
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 366..423
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46635 MW; 287888550B9C4848 CRC64;
MTDALFLPDA LLADLENTSS PLPRCPVLLT SDPPQNPDAN SHDSTVCKPR SPRSADPPPA
FSSSSLLGGG LNELDHLLQE LNATQFNITD EILAQFPSSQ KDERDKIKDK ASTSSSSSSK
PSATSATMEL DKLMASLSDF RVQTTRPATP PQQPAAPPQP SSGGSLDSML GLLQSDLTRQ
GVQTSSKGNC SACQKPVVGQ VVTALGKVWH PEHFVCTECE TELGSRNFFE KDGRPYCESD
YFMLFSPHCA HCSKPILNKM VTALDKNWHP ECFCCVKCSR SFGDEGFHDR DGQQYCQQCF
LTLFASRCQG CSQPILENYI SALNSLWHPQ CFVCRECYSP FVNGSFFEHD GKPLCEAHYH
QSRGSMCQAC QQPILGRCVT AMGAKFHPHH LVCHFCLKPL SKGCFKEQES KPYCHPCFIK
LFG
//
