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TLRN1_HUMAN
ID   TLRN1_HUMAN             Reviewed;         362 AA.
AC   Q9H1K6;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Talin rod domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=Mesoderm development candidate 1 {ECO:0000312|HGNC:HGNC:13519};
GN   Name=TLNRD1 {ECO:0000312|HGNC:HGNC:13519};
GN   Synonyms=MESDC1 {ECO:0000312|HGNC:HGNC:13519};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=11247670; DOI=10.1006/geno.2000.6466;
RA   Wines M.E., Lee L., Katari M.S., Zhang L., DeRossi C., Shi Y., Perkins S.,
RA   Feldman M., McCombie W.R., Holdener B.C.;
RT   "Identification of mesoderm development (mesd) candidate genes by
RT   comparative mapping and genome sequence analysis.";
RL   Genomics 72:88-98(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [4]
RP   FUNCTION, AND INDUCTION BY MIR574-3P.
RX   PubMed=22179486; DOI=10.3892/ijo.2011.1294;
RA   Tatarano S., Chiyomaru T., Kawakami K., Enokida H., Yoshino H., Hidaka H.,
RA   Nohata N., Yamasaki T., Gotanda T., Tachiwada T., Seki N., Nakagawa M.;
RT   "Novel oncogenic function of mesoderm development candidate 1 and its
RT   regulation by MiR-574-3p in bladder cancer cell lines.";
RL   Int. J. Oncol. 40:951-959(2012).
CC   -!- FUNCTION: Actin-binding protein which may have an oncogenic function
CC       and regulates cell proliferation, migration and invasion in cancer
CC       cells. {ECO:0000269|PubMed:22179486}.
CC   -!- SUBUNIT: May homodimerize. Interacts with F-actin.
CC       {ECO:0000250|UniProtKB:Q9ERE8}.
CC   -!- INTERACTION:
CC       Q9H1K6; Q9BSQ5: CCM2; NbExp=3; IntAct=EBI-12344941, EBI-1573056;
CC       Q9H1K6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12344941, EBI-79165;
CC       Q9H1K6; O14492-2: SH2B2; NbExp=3; IntAct=EBI-12344941, EBI-19952306;
CC       Q9H1K6; Q9H1K6: TLNRD1; NbExp=3; IntAct=EBI-12344941, EBI-12344941;
CC   -!- INDUCTION: Down-regulated by microRNA MIR574-3p.
CC       {ECO:0000269|PubMed:22179486}.
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DR   EMBL; AY007810; AAG41058.1; -; mRNA.
DR   EMBL; BC084554; AAH84554.1; -; mRNA.
DR   CCDS; CCDS10316.1; -.
DR   RefSeq; NP_072088.1; NM_022566.2.
DR   PDB; 6XZ3; X-ray; 2.19 A; A=143-273.
DR   PDB; 6XZ4; X-ray; 2.30 A; A/B=1-362.
DR   PDBsum; 6XZ3; -.
DR   PDBsum; 6XZ4; -.
DR   AlphaFoldDB; Q9H1K6; -.
DR   SMR; Q9H1K6; -.
DR   BioGRID; 121865; 17.
DR   IntAct; Q9H1K6; 3.
DR   STRING; 9606.ENSP00000267984; -.
DR   iPTMnet; Q9H1K6; -.
DR   PhosphoSitePlus; Q9H1K6; -.
DR   BioMuta; TLNRD1; -.
DR   DMDM; 24418561; -.
DR   EPD; Q9H1K6; -.
DR   jPOST; Q9H1K6; -.
DR   MassIVE; Q9H1K6; -.
DR   MaxQB; Q9H1K6; -.
DR   PaxDb; Q9H1K6; -.
DR   PeptideAtlas; Q9H1K6; -.
DR   PRIDE; Q9H1K6; -.
DR   ProteomicsDB; 80425; -.
DR   Antibodypedia; 63061; 25 antibodies from 10 providers.
DR   DNASU; 59274; -.
DR   Ensembl; ENST00000267984.4; ENSP00000267984.2; ENSG00000140406.4.
DR   GeneID; 59274; -.
DR   KEGG; hsa:59274; -.
DR   MANE-Select; ENST00000267984.4; ENSP00000267984.2; NM_022566.3; NP_072088.1.
DR   UCSC; uc002bfz.4; human.
DR   CTD; 59274; -.
DR   DisGeNET; 59274; -.
DR   GeneCards; TLNRD1; -.
DR   HGNC; HGNC:13519; TLNRD1.
DR   HPA; ENSG00000140406; Low tissue specificity.
DR   MIM; 615466; gene.
DR   neXtProt; NX_Q9H1K6; -.
DR   OpenTargets; ENSG00000140406; -.
DR   PharmGKB; PA30760; -.
DR   VEuPathDB; HostDB:ENSG00000140406; -.
DR   eggNOG; KOG4261; Eukaryota.
DR   GeneTree; ENSGT00910000144335; -.
DR   HOGENOM; CLU_764970_0_0_1; -.
DR   InParanoid; Q9H1K6; -.
DR   OMA; EQSCGVL; -.
DR   OrthoDB; 1284476at2759; -.
DR   PhylomeDB; Q9H1K6; -.
DR   PathwayCommons; Q9H1K6; -.
DR   SignaLink; Q9H1K6; -.
DR   BioGRID-ORCS; 59274; 16 hits in 1083 CRISPR screens.
DR   ChiTaRS; MESDC1; human.
DR   GenomeRNAi; 59274; -.
DR   Pharos; Q9H1K6; Tdark.
DR   PRO; PR:Q9H1K6; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9H1K6; protein.
DR   Bgee; ENSG00000140406; Expressed in ileal mucosa and 183 other tissues.
DR   Genevisible; Q9H1K6; HS.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; ISS:HGNC.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   InterPro; IPR042799; TLNRD1.
DR   PANTHER; PTHR47133; PTHR47133; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..362
FT                   /note="Talin rod domain-containing protein 1"
FT                   /id="PRO_0000096441"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   HELIX           75..102
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   HELIX           105..135
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   HELIX           150..169
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           177..204
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           208..237
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           241..249
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           251..265
FT                   /evidence="ECO:0007829|PDB:6XZ3"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   HELIX           279..308
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:6XZ4"
FT   HELIX           319..341
FT                   /evidence="ECO:0007829|PDB:6XZ4"
SQ   SEQUENCE   362 AA;  37758 MW;  37BF391D663E1D6E CRC64;
     MASGSAGKPT GEAASPAPAS AIGGASSQPR KRLVSVCDHC KGKMQLVADL LLLSSEARPV
     LFEGPASSGA GAESFEQCRD TIIARTKGLS ILTHDVQSQL NMGRFGEAGD SLVELGDLVV
     SLTECSAHAA YLAAVATPGA QPAQPGLVDR YRVTRCRHEV EQGCAVLRAT PLADMTPQLL
     LEVSQGLSRN LKFLTDACAL ASDKSRDRFS REQFKLGVKC MSTSASALLA CVREVKVAPS
     ELARSRCALF SGPLVQAVSA LVGFATEPQF LGRAAAVSAE GKAVQTAILG GAMSVVSACV
     LLTQCLRDLA QHPDGGAKMS DHRERLRNSA CAVSEGCTLL SQALRERSSP RTLPPVNSNS
     VN
 
 
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