TANC2_RAT
ID TANC2_RAT Reviewed; 1992 AA.
AC F1LTE0;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein TANC2 {ECO:0000305};
GN Name=Tanc2 {ECO:0000312|RGD:1309285};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:22673903}
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF1A.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
CC -!- FUNCTION: Scaffolding protein in the dendritic spines which acts as
CC immobile postsynaptic posts able to recruit KIF1A-driven dense core
CC vesicles to dendritic spines. {ECO:0000269|PubMed:30021165}.
CC -!- SUBUNIT: Interacts with KIF1A; the interaction decreases in presence of
CC calcium. {ECO:0000269|PubMed:30021165}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:30021165}.
CC -!- SIMILARITY: Belongs to the TANC family. {ECO:0000305}.
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DR EMBL; AABR07030574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178582.1; NM_001191653.1.
DR AlphaFoldDB; F1LTE0; -.
DR SMR; F1LTE0; -.
DR STRING; 10116.ENSRNOP00000052007; -.
DR GlyGen; F1LTE0; 1 site.
DR iPTMnet; F1LTE0; -.
DR PhosphoSitePlus; F1LTE0; -.
DR PaxDb; F1LTE0; -.
DR PRIDE; F1LTE0; -.
DR GeneID; 303599; -.
DR KEGG; rno:303599; -.
DR CTD; 26115; -.
DR RGD; 1309285; Tanc2.
DR VEuPathDB; HostDB:ENSRNOG00000052840; -.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_001464_0_1_1; -.
DR InParanoid; F1LTE0; -.
DR PRO; PR:F1LTE0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000052840; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; F1LTE0; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 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 ANK repeat; Cell projection; Glycoprotein; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; TPR repeat.
FT CHAIN 1..1992
FT /note="Protein TANC2"
FT /id="PRO_0000448661"
FT REPEAT 846..878
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 884..913
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 917..946
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 950..979
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 990..1019
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 1033..1062
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 1066..1095
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 1099..1128
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 1132..1161
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 1165..1194
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 1198..1227
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT REPEAT 1244..1277
FT /note="TPR 1"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 1291..1324
FT /note="TPR 2"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 1325..1358
FT /note="TPR 3"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1786..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1970..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1565
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1578
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
FT MOD_RES 1829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT CARBOHYD 1930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:A2A690"
SQ SEQUENCE 1992 AA; 219812 MW; 5767B163481711BB CRC64;
MFRNSLKMLL TGGKSSRKNR SSDGGSEEPP DRRQSSVDSR QSRSGPGGIS TESDCAFEPD
YAVPALPVSE GDVEQELGPP PSVDEAANTL MTRLGFLLGE KVTEVQPGDQ YSMEVQDENQ
TSAITQRISP CSTLTSSTAS PPASSPCSTL PPVSTNATAK DCSYGAVTSP TSTLESRDSG
IIATLTNYSE NMERTKYVGE AGKELGSGGN LKPWQSQKSS MDSCLYRVDE NMAASTYSLN
KIPERNLETV LSQSVQSIPL YLMPRPNSVA ATSSAHLEDL AYLDEQRHTP LRTSLRMPRQ
SMSGARTQQD LRVRFAPYRP PDISLKPLLF EVPSITTESV FVGRDWVFHE IDAQLQSSNA
SVNQGVVIVG NIGFGKTAII SRLVALSCHG TRMRQIASDS PHASPKHVDA NRELPLTQAP
SAHSSIASGS CPGTPEMRRR QEEAMRRLAS QVVAYHYCQA DNAYTCLVPE FVHNVAALLC
RSPQLTAYRE QLLREPHLQS MLSLRSCVQD PMASFRRGVL EPLENLHKER KIPDEDFIIL
IDGLNEAEFH KPDYGDTIVS FLSKMIGNFP SWLKLIVTVR TSLQEITKLL PFHRIFLDRL
EENEAIDQDL QAYILHRIHS SSEIQNNISL NGKMDNTTFG KLSSHLKTLS QGSYLYLKLT
FDLIEKGYLV LKSSSYKVVP VSLSEVYLLQ CNMKFPTQSS FDRVMPLLNV AVASLHPLTD
EHIFQAINAG SIEGTLEWED FQQRMENLSM FLIKRRDMTR MFVHPSFREW LIWREEGEKT
KFLCDPRSGH TLLAFWFSRQ EGKLNRQQTI ELGHHILKAH IFKGLSKKVG VSSSILQGLW
ISYSTEGLSM ALASLRNLYT PNIKVSRLLI LGGANINYRT EVLNNAPILC VQSHLGYTEM
VALLLEFGAN VDASSESGLT PLGYAAAAGF LSIVVLLCKK RAKVDHLDKN GQCALVHAAL
RGHLEVVKFL IQCDWTMAGQ QQGVFKKSQA IQQALIAAAS MGYTEIVSYL LDLPEKDEEE
VERAQINSFD SLWGETALTA AAGRGKLDVC RLLLEQGAAV AQPNRRGAVP LFSTVRQGHW
QIVDLLLTHG ADVNMADKQG RTPLMMAASE GHLGTVDFLL AQGASIALMD KEGLTALSWA
CLKGHLSVVR SLVDNGAATD HADKNGRTPL DLAAFYGDAE VVQFLVDHGA MIEHVDYSGM
RPLDRAVGCR NTSVVVTLLK KGAKIGPATW AMATSKPDIM IILLSKLMEE GDMFYKKGKV
KEAAQRYQYA LKKFPREGFG EDLKTFRELK VSLLLNLSRC RRKMNDFGMA EEFATKALEL
KPKSYEAYYA RARAKRSSRQ FAAALEDLKE AIKLCPNNRE IQRLLMRVEE ECRQMQQQQQ
PPPPPQQPPE ELPEEETEPE PQPEDIYSVQ DIFEEEYLEQ DVENVSIGLQ TEARPSQGLP
VIQSPPSSPA HRDSAYISSS PLGSHQVFDF RSNSSVGSPT RQGYQSTSPA LSPTHQNSHY
RPSPPHTSPA HQGASYRFSP PPVGGQGKEY PSPPPSPLRR GPQYRASPPA ESMSIYRSQS
GSPVRYQQEA NVSQLPGRPK SPLSKMAQRP YQMPQLPVAV PQQGLRLQPA KAQIVRSNQP
SSAVHSSTVI PTGAYGQVAH PMASKYQSSQ GDMGVSQSRL VYQGSIGGIV GDGRPVQHVQ
ASLSAGAICQ HGGLTKEDLP QRPSSAYRGG MRYSQTPQIG RSQSASYYPV CHSKLDLERS
SSQLGSPDVS HLIRRPISVN PNEIKPHPPT PRPLLHSQSV GLRFSPSSNS ISSTANLTPT
FRPSSSIQQM EIPLKPAYDR SCDELSPVSP TQGGYPSEPT RSRTTPFMGI IDKTARTQQY
PHLHQQNRTW AVSSVDTVLS PTSPGNLSQP ESFSPPSSIS NIAFYNKTNN AQNGHLLEDD
YYSPHGMLAN GSRGDLLERV SQASSYPDVK VARTLPVAQA YQDNLYRQLS RDSRQGQTSP
IKPKRPFVES NV
