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TES_RAT
ID   TES_RAT                 Reviewed;         419 AA.
AC   Q2LAP6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Testin;
GN   Name=Tes;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Ovary;
RA   Seo Y.M., Jang S.J., Chun S.Y.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [4]
RP   IDENTIFICATION IN A COMPLEX WITH ENAH AND ACTL7A, AND SUBUNIT.
RX   PubMed=21278383; DOI=10.1074/jbc.m110.171264;
RA   Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA   Garvalov B.K., McDonald N.Q., Way M.;
RT   "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT   protein Arp7A.";
RL   J. Biol. Chem. 286:11543-11554(2011).
CC   -!- FUNCTION: Scaffold protein that may play a role in cell adhesion, cell
CC       spreading and in the reorganization of the actin cytoskeleton. Plays a
CC       role in the regulation of cell proliferation. May act as a tumor
CC       suppressor (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM domain
CC       3) with ENAH and VASP. Interacts with ALKBH4, talin, actin, alpha-
CC       actinin, GRIP1 and PXN (By similarity). Interacts (via LIM domain 2)
CC       with ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer
CC       interacts with ENAH to form a heterotrimer. {ECO:0000250,
CC       ECO:0000269|PubMed:21278383}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal
CC       adhesion {ECO:0000250}. Note=Detected along actin stress fibers.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal and the C-terminal halves of the protein can
CC       associate with each other, thereby hindering interactions with ZYX.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {ECO:0000305}.
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DR   EMBL; DQ339047; ABC68418.1; -; mRNA.
DR   EMBL; DP000027; ABC87757.1; -; Genomic_DNA.
DR   EMBL; BC129069; AAI29070.1; -; mRNA.
DR   RefSeq; NP_001034433.1; NM_001039344.2.
DR   AlphaFoldDB; Q2LAP6; -.
DR   SMR; Q2LAP6; -.
DR   BioGRID; 271348; 1.
DR   IntAct; Q2LAP6; 2.
DR   STRING; 10116.ENSRNOP00000051294; -.
DR   iPTMnet; Q2LAP6; -.
DR   PhosphoSitePlus; Q2LAP6; -.
DR   jPOST; Q2LAP6; -.
DR   PaxDb; Q2LAP6; -.
DR   PRIDE; Q2LAP6; -.
DR   Ensembl; ENSRNOT00000091095; ENSRNOP00000070338; ENSRNOG00000051952.
DR   GeneID; 500040; -.
DR   KEGG; rno:500040; -.
DR   UCSC; RGD:1566346; rat.
DR   CTD; 26136; -.
DR   RGD; 1566346; Tes.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00940000155993; -.
DR   HOGENOM; CLU_008937_1_1_1; -.
DR   InParanoid; Q2LAP6; -.
DR   OMA; NKLWHPA; -.
DR   OrthoDB; 997264at2759; -.
DR   PhylomeDB; Q2LAP6; -.
DR   TreeFam; TF313265; -.
DR   PRO; PR:Q2LAP6; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000051952; Expressed in colon and 20 other tissues.
DR   Genevisible; Q2LAP6; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   CDD; cd09413; LIM1_Testin; 1.
DR   CDD; cd09416; LIM2_Testin; 1.
DR   CDD; cd09419; LIM3_Testin; 1.
DR   CDD; cd09829; PET_testin; 1.
DR   InterPro; IPR034958; LIM1_Testin.
DR   InterPro; IPR034959; LIM2_Testin.
DR   InterPro; IPR034960; LIM3_Testin.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR033724; PET_testin.
DR   InterPro; IPR027683; Testin.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24211:SF1; PTHR24211:SF1; 1.
DR   Pfam; PF00412; LIM; 2.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasm; LIM domain; Metal-binding; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN           1..419
FT                   /note="Testin"
FT                   /id="PRO_0000278802"
FT   DOMAIN          92..199
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          232..295
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          297..357
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          360..419
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          133..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  47632 MW;  3AE8CF90F395B2CE CRC64;
     MDLETKMKKM GLGHEQGFGA PCLKCKENCE GFELHFWRKI CRNCKCGQEE HDVLLSTEED
     RKVGRLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
     ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPK EVKEMEQFVK
     KYKSEALGVG DVKLPSEMNA QGDKVHNPAG DRNTPAAVGS KDKSAEAKKT QYSCYCCKNT
     MREGDPAIYA ERAGYDKLWH PACFICSTCG ELLVDMIYFW KNGKLYCGRH YCDSEKPRCA
     GCDELIFSNE YTQAENQNWH LKHFCCFDCD NILAGKIYVM VRDKPVCKPC YVKNHAVVCQ
     GCHNAIDPEV QRVTYNNFSW HASTECFLCS CCSKCLIGQK FMPVEGMVFC SVECKKMMS
 
 
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