ID D4A858_RAT Unreviewed; 1141 AA. AC D4A858; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 27-MAR-2024, entry version 86. DE SubName: Full=Transforming, acidic coiled-coil containing protein 2 {ECO:0000313|Ensembl:ENSRNOP00000042296.3}; GN Name=Tacc2 {ECO:0000313|Ensembl:ENSRNOP00000042296.3, GN ECO:0000313|RGD:1303004}; 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 {ECO:0000313|Ensembl:ENSRNOP00000042296.3, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000042296.3, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042296.3, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; 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:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; 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] {ECO:0000313|Ensembl:ENSRNOP00000042296.3} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042296.3}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the TACC family. CC {ECO:0000256|ARBA:ARBA00009423}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; D4A858; -. DR PeptideAtlas; D4A858; -. DR Ensembl; ENSRNOT00000047161.5; ENSRNOP00000042296.3; ENSRNOG00000020457.9. DR UCSC; RGD:1303004; rat. DR AGR; RGD:1303004; -. DR RGD; 1303004; Tacc2. DR VEuPathDB; HostDB:ENSRNOG00000020457; -. DR GeneTree; ENSGT00940000157052; -. DR OrthoDB; 5406887at2759; -. DR PhylomeDB; D4A858; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000020457; Expressed in skeletal muscle tissue and 20 other cell types or tissues. DR ExpressionAtlas; D4A858; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD. DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD. DR GO; GO:0030953; P:astral microtubule organization; ISO:RGD. DR GO; GO:0008283; P:cell population proliferation; ISO:RGD. DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD. DR GO; GO:0022027; P:interkinetic nuclear migration; ISO:RGD. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD. DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro. DR GO; GO:0022008; P:neurogenesis; ISO:RGD. DR GO; GO:0032886; P:regulation of microtubule-based process; ISO:RGD. DR Gene3D; 1.20.5.1700; -; 1. DR InterPro; IPR039915; TACC. DR InterPro; IPR007707; TACC_C. DR PANTHER; PTHR13924; TRANSFORMING ACIDIC COILED-COIL CONTAINING PROTEIN 1/2; 1. DR PANTHER; PTHR13924:SF11; TRANSFORMING ACIDIC COILED-COIL-CONTAINING PROTEIN 2; 1. DR Pfam; PF05010; TACC_C; 1. DR Genevisible; D4A858; RN. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}. FT DOMAIN 935..1135 FT /note="Transforming acidic coiled-coil-containing protein FT C-terminal" FT /evidence="ECO:0000259|Pfam:PF05010" FT REGION 1..219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 244..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 400..609 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 628..657 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 687..708 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 747..771 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 944..1137 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..51 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..94 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 147..177 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 256..280 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 296..313 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 361..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..556 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 567..584 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..651 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 689..708 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..771 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1141 AA; 123585 MW; CEB01CADFBF79A32 CRC64; MGNENSTSDH QRTSSVQSLR SLQPPGNSQT PQKQGDSPGS GAASIPGTND VIQSAAPEDL GHPPLADSSR YGVTVSSVST HLTVQSTSPS AAHASLAPVA SEHAALASAA AGPGVETPTA SCQHLAKNIN RSSDSEEAFE TPESTTPVKA PPAPPPPPPE VTPEPEVIEP PAPEEPGCIS EPVVVPDGPR SESVEGSPFR PSHSSSAVFD EDKPIASSGT YNLDFDSIEL VDNFQSLEPC SADYKGQECK VSTRRKSTES VPPSKTTLSR SLSLQASDFD GASCPGSPEA GTLATDACGT GSNSASSTLK RTKKTRPPSL KKKQATKKPT ETPPVKETQQ EPGEESPVPS EEHLAPETKT ESATPEGTGC TLSEETSLES AAVPTATCPL TLESVEDVSP LVSGGGRVQN SPPVGRKSVP LTTASEAVEV TLPDGGGQED LPAKGLSVRL EFDYSEDKGS WESQQENAPP TKKIGKKPVA KMPLRRPKLK KTPEKLDNTP ASPPRSPAEP SDIPIAKGTY TFDIDKWDDP NFNPFSSTSK MQESPTLSQQ SYNFDPDACE ESLDPFKASS KTPSSPSKSP ASFEIPASTI EADGDGLNKP AKKKKTPLKT MVEDVMSVCS LFDTFRVKKS PKRSPLSDPP SQDPTPAATP EAPPVSTVVH ATDEEKLAVT SQKWTCMTVD LDADKQDFPQ PSDLSNFVNE TKFNSPSEEL DYRNSYEIEY MEKLGSSLPQ DDDTPKKQAL YLMFDTPQES PVKSPPVRMS DSPTPCSGSS FEDTEALVNA TAKLQHPVPR GLASNQEPLL QLPEKSSQKE LEAMALGTPA EAIEITAPEG AFASADALLS RLAHPASLCG ALGYLEPDLA EKNPPVFAQK LQEELEFAVM RIEALKLARQ IALASRSRQD TKREATHPPD VSISKTTLYS RIGPTEVEKP PGLLFQQPDL DSALQVARAE VIAKEREVSE WRDKYEESRR EVVEMRKIVA EYEKTIAQMI EDEQREKSIS HQTVQQLVLE KEQALADLNS VEKSLADLFR RYEKMKEVLE GFRKNEEVLK KCAQEYLSRV KKEEQRYQAL KVHAEEKLDR ANAEIAQVRG KAQQEQAAYQ ASLRKEQLRV DALERTLEQK NKEIEELTKI CDELIAKMGK S //