TANC1_RAT
ID TANC1_RAT Reviewed; 1849 AA.
AC Q6F6B3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein TANC1;
DE AltName: Full=TPR domain, ankyrin-repeat and coiled-coil domain-containing protein 1;
GN Name=Tanc1; Synonyms=Tanc;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH DLG1; DLG4; HOMER1; DLGAP1; INA; CAMK2A; GRIN2B AND GRIA1,
RP AND MUTAGENESIS OF VAL-1849.
RX PubMed=15673434; DOI=10.1111/j.1460-9568.2005.03856.x;
RA Suzuki T., Li W., Zhang J.P., Tian Q.B., Sakagami H., Usuda N., Kondo H.,
RA Fujii T., Endo S.;
RT "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila
RT rolling pebbles (rols), forms a multiprotein complex with various
RT postsynaptic density proteins.";
RL Eur. J. Neurosci. 21:339-350(2005).
RN [2]
RP INTERACTION WITH TNIK AND MINK1.
RX PubMed=18930710; DOI=10.1016/j.bbrc.2008.10.038;
RA Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M.,
RA Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.;
RT "MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold
RT protein TANC1.";
RL Biochem. Biophys. Res. Commun. 377:573-578(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1429 AND SER-1456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May be a scaffold component in the postsynaptic density.
CC -!- SUBUNIT: Interacts probably directly with DLG1, DLG4, HOMER1. Interacts
CC with DLGAP1, INA, CAMK2A, GRIN2B and GRIA1. Interacts with TNIK and
CC MINK1. {ECO:0000269|PubMed:15673434, ECO:0000269|PubMed:18930710}.
CC -!- INTERACTION:
CC Q6F6B3; Q9UKE5: TNIK; Xeno; NbExp=2; IntAct=EBI-2133582, EBI-1051794;
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000269|PubMed:15673434}. Note=Largly colocalizes with
CC SYP/synaptophysin, DLG1, DLG4 and GRIA1 at synaptic sites.
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, liver and kidney.
CC Expressed in brain (at protein level). {ECO:0000269|PubMed:15673434}.
CC -!- DEVELOPMENTAL STAGE: Detected as early as postnatal day one with
CC increasing expression levels through 20 weeks after birth.
CC -!- PTM: Phosphorylated; by MINK1 and TNIK upon stimulation by RAP2A.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TANC family. {ECO:0000305}.
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DR EMBL; AB098072; BAD27523.1; -; mRNA.
DR RefSeq; NP_001002854.1; NM_001002854.1.
DR AlphaFoldDB; Q6F6B3; -.
DR SMR; Q6F6B3; -.
DR BioGRID; 259817; 12.
DR IntAct; Q6F6B3; 2.
DR STRING; 10116.ENSRNOP00000033136; -.
DR iPTMnet; Q6F6B3; -.
DR PhosphoSitePlus; Q6F6B3; -.
DR PaxDb; Q6F6B3; -.
DR PeptideAtlas; Q6F6B3; -.
DR PRIDE; Q6F6B3; -.
DR GeneID; 311055; -.
DR KEGG; rno:311055; -.
DR UCSC; RGD:1302949; rat.
DR CTD; 85461; -.
DR RGD; 1302949; Tanc1.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q6F6B3; -.
DR PhylomeDB; Q6F6B3; -.
DR PRO; PR:Q6F6B3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0097062; P:dendritic spine maintenance; ISO:RGD.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; TPR repeat.
FT CHAIN 1..1849
FT /note="Protein TANC1"
FT /id="PRO_0000316961"
FT REPEAT 886..918
FT /note="ANK 1"
FT REPEAT 924..953
FT /note="ANK 2"
FT REPEAT 957..986
FT /note="ANK 3"
FT REPEAT 990..1019
FT /note="ANK 4"
FT REPEAT 1030..1059
FT /note="ANK 5"
FT REPEAT 1068..1097
FT /note="ANK 6"
FT REPEAT 1101..1130
FT /note="ANK 7"
FT REPEAT 1134..1163
FT /note="ANK 8"
FT REPEAT 1167..1196
FT /note="ANK 9"
FT REPEAT 1200..1229
FT /note="ANK 10"
FT REPEAT 1233..1262
FT /note="ANK 11"
FT REPEAT 1279..1312
FT /note="TPR 1"
FT REPEAT 1326..1359
FT /note="TPR 2"
FT REPEAT 1361..1393
FT /note="TPR 3"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 1429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D5"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VGY8"
FT MOD_RES 1667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0VGY8"
FT MUTAGEN 1849
FT /note="Missing: Abolishes interaction with DLG1, DLG4 and
FT HOMER1."
FT /evidence="ECO:0000269|PubMed:15673434"
SQ SEQUENCE 1849 AA; 200507 MW; E52BA9EABF2ECECF CRC64;
MLKAVLKKSR EGVKGSKKEA GGDFGSETPT LSSSGDSPVN SLSTTEDTYR VSLAKGVSMS
LPSSPLLPRQ SHLTQSRANK KSPGPVRKPK YVESPRVPGD PVMIPFREGS KPAEPIETEA
KVDNEPSCSP AAQELLTRLG FLLGEGIPSA THITIEDKNE AMCTALSQGI SPCSTLTSST
ASPSTDSPCS TLNSCVSKTA ANKSPCETIS SPSSTLESKD SGIIATITSS SENDDRSGSS
LEWNRDGSLR LGVQKGVLHD RRLDNCSPVA EEETTGSAES VLPKAESSAG DGPVPYSQSS
GSLIMPRPNS VAATSSTKLE DLSYLDGQRN APLRTSIRLP WHSTAGARFA PYKPQEILLK
PLLFEVPSIT TDSVFVGRDW LFQQIEENLR NTELAENRGA VVVGNVGFGK TAIISKLVAL
SCHGSRMRQV ASSSPSSSLK TSDPTHDLPG TPLLSPSSST SALSAARTPP GPGTVDSQRP
REDAVKYLAS RVVAYHYCQA DNTYTCLVPE FVHSIATLLC RSHQLAAYRD LLIREPQLQS
MLNLRSCVQD PVAAFKRGIL EPLTNLRNEQ KIPEEEYIIL IDGLNEAEFH KPDHGDTLSS
FITKIIPKFP PWLKLIVTVR ADFQEIISTL PFVKLSLDDF PGNQDIHSDL HAYVQHRVHS
SQDILSNISL NGKADAALIG KVSSRLVLRN LGSYLYLKLT LDLFQRGHLV IKSASYKVVP
VSLSELYLLQ CNMKFMTQSA FDRALPILNV ALASLHPMTD EQIFQAINAG HIQGEQGWED
FQQKMEALSC FLIKKRDKTR MFCHPSFREW LVWRADGEST AFLCEPRNGH ALLAFMFSRQ
ESKLNRQQTV ELGHHILKAH IFKGLSKKTG VSSSHPQALW IGYSTEGLSA ALASLRNLYT
PNVKVSRLLI LGGANVNYRT EVLNNAPILC VQSHLGHEEV VTLLLEFGAC LDGMSENGMN
ALCYAAAAGH MKLVCLLTKK GARVDHLDKK GQCALVHSAL RGHSDILQYL LNCEWSAGPP
QPGTLRKSQA LQQALTAAAS MGHSAVVQSL LGMAEEHEIE VNGTDTLWGE TALTAAAGRG
KLEICELLLE RGAAVSRANR RGVPPLFCAA RQGHWQVVQL LLDRGCDVNP NDKQGRTPLM
VAACEGHLST VEFLLSKGAA LSSLDKEGLS ALSWACLKGH RAVVQYLVEE GAEIDQTDKN
GRTPLDLAAF YGDAETVLYL VEKGAVIEHV DHSGMRPLDR AIGCRNTAVV VTLLRKGAKL
GNAAWAMATF KPDILIILLQ KLMEEGNVMY KKGKMKEAAQ RYQYALRKFP REGPGEDMRP
FNELRVSLYL NLSRCRRKTN DFGLAEEFAS KALELKPKSY EAFYARARAK RNSRQFLAAL
ADLQEAVKLC PTNQEIKRLL ARVEEECKQL QRNQQQKQQA PLPAPPNDSD NDEEAPASSL
KDHFPIEEAE EEDTSSQEES ISPTPRSQPP PSVPSPYIRN LQEGLQSKGR PASPQSWAGI
SKSLRETVAQ PGLVMQPTKQ AQIVKTNQHL GSGQSSMRNS NTKVQVSSQN PPPSPMPGRV
SAAPAVSRNQ HLEGTGPFST GTGCGHFGDR LGPSQSLQLQ RGESGTAYPL PSKVKAAERL
LAHASVAVDM ALPSQGGPVS CSDVRHPASL SSSGSSGSPS SSVKMSSSTS SLTSSSSVSD
GFKAQGPDCR IRDRGTTQVQ GGTAEHRPRN TPFMGIMDKI ARFQQQVNPP SRSWHCPVTE
GLLTNTATAA GLQTNSEKPA LKPGGYCSQA KPCSVPPLGM GVHNGAQVKE LEENKCQVPA
LCQDNRKTKG VPHLYPEGVS KQPLHVSTEA HRSHLTSAKP KRSFIESNV
