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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}.
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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
 
 
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