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MZT1_SCHPO
ID   MZT1_SCHPO              Reviewed;          64 AA.
AC   P0CF96; G2TRK7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 3.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Mitotic-spindle organizing protein 1;
DE   AltName: Full=Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1;
DE   AltName: Full=Transcripts altered in meiosis protein 4;
GN   Name=mzt1; Synonyms=tam4; ORFNames=SPAC9G1.15c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=20360068; DOI=10.1126/science.1181348;
RA   Hutchins J.R., Toyoda Y., Hegemann B., Poser I., Heriche J.K., Sykora M.M.,
RA   Augsburg M., Hudecz O., Buschhorn B.A., Bulkescher J., Conrad C.,
RA   Comartin D., Schleiffer A., Sarov M., Pozniakovsky A., Slabicki M.M.,
RA   Schloissnig S., Steinmacher I., Leuschner M., Ssykor A., Lawo S.,
RA   Pelletier L., Stark H., Nasmyth K., Ellenberg J., Durbin R., Buchholz F.,
RA   Mechtler K., Hyman A.A., Peters J.M.;
RT   "Systematic analysis of human protein complexes identifies chromosome
RT   segregation proteins.";
RL   Science 328:593-599(2010).
RN   [3]
RP   IDENTIFICATION, AND INDUCTION.
RX   PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA   Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA   Hagan I.M., Miller C.J.;
RT   "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT   additional genes required for growth and viability.";
RL   Genetics 187:1207-1217(2011).
RN   [4]
RP   FUNCTION, IDENTIFICATION OF PROBABLE INITIATION SITE, SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=23885124; DOI=10.1091/mbc.e13-05-0235;
RA   Masuda H., Mori R., Yukawa M., Toda T.;
RT   "Fission yeast MOZART1/Mzt1 is an essential gamma-tubulin complex component
RT   required for complex recruitment to the microtubule organizing center, but
RT   not its assembly.";
RL   Mol. Biol. Cell 24:2894-2906(2013).
RN   [5]
RP   FUNCTION, IDENTIFICATION OF PROBABLE INITIATION SITE, SUBCELLULAR LOCATION,
RP   AND INTERACTION WITH ALP6.
RX   PubMed=24006493; DOI=10.1091/mbc.e13-05-0253;
RA   Dhani D.K., Goult B.T., George G.M., Rogerson D.T., Bitton D.A.,
RA   Miller C.J., Schwabe J.W., Tanaka K.;
RT   "Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of
RT   the gamma-tubulin complex and directly interacts with GCP3(Alp6).";
RL   Mol. Biol. Cell 24:3337-3349(2013).
CC   -!- FUNCTION: Required for gamma-tubulin complex recruitment to the
CC       microtubule organizing center (MTOC). {ECO:0000269|PubMed:23885124,
CC       ECO:0000269|PubMed:24006493}.
CC   -!- SUBUNIT: Part of the gamma-tubulin complex. Interacts directly with
CC       alp6/GPC3. {ECO:0000269|PubMed:23885124, ECO:0000269|PubMed:24006493}.
CC   -!- INTERACTION:
CC       P0CF96; Q9USQ2: alp6; NbExp=6; IntAct=EBI-9549556, EBI-9549762;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:23885124,
CC       ECO:0000269|PubMed:24006493}. Note=Localizes to all the MTOCs,
CC       including the SPB and interphase and equatorial MTOCs.
CC   -!- INDUCTION: Differentially expressed during meiosis.
CC       {ECO:0000269|PubMed:21270388}.
CC   -!- SIMILARITY: Belongs to the MOZART1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCD31316.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CU329670; CCD31316.1; ALT_INIT; Genomic_DNA.
DR   PDB; 6L80; X-ray; 2.00 A; B/D=1-64.
DR   PDBsum; 6L80; -.
DR   AlphaFoldDB; P0CF96; -.
DR   SMR; P0CF96; -.
DR   IntAct; P0CF96; 2.
DR   STRING; 4896.SPAC9G1.15c.1; -.
DR   PaxDb; P0CF96; -.
DR   EnsemblFungi; SPAC9G1.15c.1; SPAC9G1.15c.1:pep; SPAC9G1.15c.
DR   PomBase; SPAC9G1.15c; mzt1.
DR   VEuPathDB; FungiDB:SPAC9G1.15c; -.
DR   eggNOG; ENOG502S6UI; Eukaryota.
DR   HOGENOM; CLU_160285_0_1_1; -.
DR   InParanoid; P0CF96; -.
DR   PRO; PR:P0CF96; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR   GO; GO:0000931; C:gamma-tubulin large complex; IEA:InterPro.
DR   GO; GO:0008275; C:gamma-tubulin small complex; IDA:PomBase.
DR   GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; ISS:PomBase.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0140475; F:spindle pole body anchor activity; IPI:PomBase.
DR   GO; GO:0033566; P:gamma-tubulin complex localization; IEA:InterPro.
DR   GO; GO:0051415; P:microtubule nucleation by interphase microtubule organizing center; IMP:PomBase.
DR   GO; GO:0051417; P:microtubule nucleation by spindle pole body; IMP:PomBase.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR   InterPro; IPR022214; MZT1.
DR   PANTHER; PTHR28520; PTHR28520; 1.
DR   Pfam; PF12554; MOZART1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..64
FT                   /note="Mitotic-spindle organizing protein 1"
FT                   /id="PRO_0000394216"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:6L80"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:6L80"
FT   HELIX           41..53
FT                   /evidence="ECO:0007829|PDB:6L80"
SQ   SEQUENCE   64 AA;  7137 MW;  B7F61F2498330CEF CRC64;
     MSESTKETIE VLYEIGTLLG TELDKTTLSL CISLCENNVH PEAIAQIIRE IRMAQEQTVD
     TEPS
 
 
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