TACC3_XENLA
ID TACC3_XENLA Reviewed; 931 AA.
AC Q9PTG8; Q52L20;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 3;
DE AltName: Full=Cytoplasmic polyadenylation element-binding protein-associated factor Maskin;
DE Short=CPEB-associated factor Maskin;
GN Name=tacc3; Synonyms=maskin;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAF19726.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP IDENTIFICATION IN A COMPLEX WITH CPEB1 AND EIF4E, INTERACTION WITH CPEB1
RP AND EIF4E, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP THR-577 AND 581-PHE--LEU-583.
RX PubMed=10635326; DOI=10.1016/s1097-2765(00)80230-0;
RA Stebbins-Boaz B., Cao Q., de Moor C.H., Mendez R., Richter J.D.;
RT "Maskin is a CPEB-associated factor that transiently interacts with eIF-
RT 4E.";
RL Mol. Cell 4:1017-1027(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND PHOSPHORYLATION AT SER-33; SER-620 AND SER-626.
RX PubMed=16172205; DOI=10.1083/jcb.200503023;
RA Kinoshita K., Noetzel T.L., Pelletier L., Mechtler K., Drechsel D.N.,
RA Schwager A., Lee M., Raff J.W., Hyman A.A.;
RT "Aurora A phosphorylation of TACC3/maskin is required for centrosome-
RT dependent microtubule assembly in mitosis.";
RL J. Cell Biol. 170:1047-1055(2005).
RN [4]
RP FUNCTION, INTERACTION WITH CKAP5, AND PHOSPHORYLATION.
RX PubMed=16172207; DOI=10.1083/jcb.200504037;
RA Peset I., Seiler J., Sardon T., Bejarano L.A., Rybina S., Vernos I.;
RT "Function and regulation of Maskin, a TACC family protein, in microtubule
RT growth during mitosis.";
RL J. Cell Biol. 170:1057-1066(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CKAP5, AND MUTAGENESIS OF.
RX PubMed=25262927; DOI=10.1038/ncomms6072;
RA Mortuza G.B., Cavazza T., Garcia-Mayoral M.F., Hermida D., Peset I.,
RA Pedrero J.G., Merino N., Blanco F.J., Lyngsoe J., Bruix M., Pedersen J.S.,
RA Vernos I., Montoya G.;
RT "XTACC3-XMAP215 association reveals an asymmetric interaction promoting
RT microtubule elongation.";
RL Nat. Commun. 5:5072-5072(2014).
CC -!- FUNCTION: Maternal RNA in oocytes remains in a dormant state as masking
CC outcompetes eif4g to bind eif4e, thereby preventing translation. During
CC oocyte maturation this complex dissolves and eif4g binds eif4e to allow
CC translation of maternal RNAs (PubMed:10635326). Plays a role in the
CC microtubule-dependent coupling of the nucleus and the centrosome (By
CC similarity). Involved in microtubule assembly during M-phase. Involved
CC in spindle pole assembly by recruiting and regulating ckap5 at the
CC spindle pole leading to microtubule elongation (PubMed:16172207,
CC PubMed:25262927). {ECO:0000250|UniProtKB:Q9Y6A5,
CC ECO:0000269|PubMed:10635326, ECO:0000269|PubMed:16172207,
CC ECO:0000269|PubMed:25262927}.
CC -!- SUBUNIT: Found in a complex with cpeb1, tacc3/maskin and eif4e.
CC Interacts with eif4e and cpeb1. Competes with eif4g for binding to
CC eif4e (PubMed:10635326) Interacts with ckap5-a; two molecules of ckap5
CC interact with 1 molecule of tacc3 probably mediated by coiled coil
CC domains forming a four-helix bundle (PubMed:25262927).
CC {ECO:0000269|PubMed:10635326}.
CC -!- INTERACTION:
CC Q9PTG8; Q91572: cpeb1-a; NbExp=3; IntAct=EBI-65726, EBI-65730;
CC Q9PTG8; P48597: eif4e; NbExp=3; IntAct=EBI-65726, EBI-65739;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10635326}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:25262927}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25262927}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Abundant in oocytes, with expression maintained through the midblastula
CC stage, declining in gastrula and neurula stages, and disappearing by
CC the tailbud stage (at protein level). {ECO:0000269|PubMed:10635326}.
CC -!- PTM: Phosphorylation by aurka is required for localization to mitotic
CC centrosomes. {ECO:0000269|PubMed:16172205,
CC ECO:0000269|PubMed:16172207}.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
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 EMBL; AF200212; AAF19726.1; -; mRNA.
DR EMBL; BC094101; AAH94101.1; -; mRNA.
DR RefSeq; NP_001081964.1; NM_001088495.1.
DR AlphaFoldDB; Q9PTG8; -.
DR SMR; Q9PTG8; -.
DR DIP; DIP-29250N; -.
DR IntAct; Q9PTG8; 6.
DR MINT; Q9PTG8; -.
DR iPTMnet; Q9PTG8; -.
DR DNASU; 398145; -.
DR GeneID; 398145; -.
DR KEGG; xla:398145; -.
DR CTD; 398145; -.
DR Xenbase; XB-GENE-865032; tacc3.S.
DR Proteomes; UP000186698; Chromosome 1S.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Mitosis; Phosphoprotein;
KW Protein synthesis inhibitor; Reference proteome; Repressor;
KW Translation regulation.
FT CHAIN 1..931
FT /note="Transforming acidic coiled-coil-containing protein
FT 3"
FT /id="PRO_0000179992"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..930
FT /evidence="ECO:0000255"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:16172205"
FT MOD_RES 620
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:16172205"
FT MOD_RES 626
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:16172205"
FT MUTAGEN 577
FT /note="T->A: Fails to bind eif4e; when associated with 581-
FT AAA-583."
FT /evidence="ECO:0000269|PubMed:10635326"
FT MUTAGEN 581..583
FT /note="FLL->AAA: Fails to bind eif4e; when associated with
FT A-577."
FT /evidence="ECO:0000269|PubMed:10635326"
FT MUTAGEN 915
FT /note="D->K: Disrupts interactions with ckap5-a."
FT /evidence="ECO:0000269|PubMed:25262927"
FT MUTAGEN 922..923
FT /note="DD->AA: Disrupts interactions with ckap5-a."
FT /evidence="ECO:0000269|PubMed:25262927"
FT CONFLICT 205
FT /note="S -> Y (in Ref. 1; AAF19726)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="D -> Y (in Ref. 1; AAF19726)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="A -> T (in Ref. 1; AAF19726)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="A -> R (in Ref. 1; AAF19726)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="F -> L (in Ref. 1; AAF19726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 102541 MW; B0BF1F2AA4901439 CRC64;
MSLQIINDEN AGNDITAEKF DLLLNPQTTG RPSILRPSQK DNLPPKPALK STKVTFQTPM
RDPQTLRIMT PSVANKPENV FLLEDCTQAL EQLHLSLPSS CGPNPVEINV SVSNNQPDSE
ELPVRTTGAY SIDFDNFDDI NPFKSKTQML NSPIKADLPS LTENIETTTP VVPADEASKQ
MVSLNLSAAN LDSPVTVQFS SESGSIGVSE KTALDDTLPL SESGIKDLQG LNASSNNIEE
PVPLDKDICS NNEKDDATMA DSTCEGTSDA HTSSNNIEEP VTLDKDICSS NEKDNAAVAD
STCEGTSDAQ SPLPIPKSSY SFDPDQFDMM NPFKTGGSKL QNSPAGKKQT PPSADLNTAK
TEPVKLEFNF GDGDVSERKP PPKKLGKRPL LKTAAKKPSP KPEIASEKQE QQTAKPSEDE
AIVPKASYKF DWEKFDDPNF NPFGCGGSKI SSSPKGQKIA NEQPSACTQG SKPEAECTAS
DMAPAENADE KDHGEIEPSQ DSGAAEDRSQ AEDQSVALSK VEVPHEQTTD CSPVENETQP
EVSLINEEPS QKEVEHTSSD MTPPEINGTD SEFKLATEAD FLLAADMDFK PASEIFSEGF
RQPVEIDYLE NFGTNSFKES VLRKQSLYLK FDPLLRESPK KSAAGINLLP SVPLKCSSDL
FGAIPEANFP LIPSIENEEK PKGLDLLGTF TVADTALLIV DAPSSVAVPN PFLSTSDAIV
EMLKYSQKDM DAAIEAVRLE VQEKDLEVLE WKTKHEKLYL EYVEMGKIIA EFEGTITQIL
EDSQRQKETA KLELNKVLQE KQQVQVDLNS METSFSELFK RLEKQKEALE GYRKNEEALK
KCVEDYLVRI KKEEQRYQAL KAHAEEKLNR ANEEIAHVRS KAKSEATALQ ATLRKEQMKI
QSLERSLEQK SKENDELTKI CDDFILKMEK I
