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TBB4_MAIZE
ID   TBB4_MAIZE              Reviewed;         447 AA.
AC   Q41782; Q43696;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Tubulin beta-4 chain;
DE   AltName: Full=Beta-4-tubulin;
GN   Name=TUBB4; Synonyms=TUB4;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A188; TISSUE=Pollen;
RX   PubMed=8275104; DOI=10.1046/j.1365-313x.1993.04050875.x;
RA   Rogers H.J., Greenland A.J., Hussey P.J.;
RT   "Four members of the maize beta-tubulin gene family are expressed in the
RT   male gametophyte.";
RL   Plant J. 4:875-882(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73; TISSUE=Seedling shoot;
RX   PubMed=8111033; DOI=10.1007/bf00020169;
RA   Villemur R., Haas N.A., Joyce C.M., Snustad D.P., Silflow C.D.;
RT   "Characterization of four new beta-tubulin genes and their expression
RT   during male flower development in maize (Zea mays L.).";
RL   Plant Mol. Biol. 24:295-315(1994).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC       two moles of GTP, one at an exchangeable site on the beta chain and one
CC       at a non-exchangeable site on the alpha chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X74655; CAA52719.1; -; mRNA.
DR   EMBL; L10635; AAA19707.1; -; mRNA.
DR   PIR; S43326; S43326.
DR   RefSeq; NP_001105457.1; NM_001111987.1.
DR   RefSeq; NP_001167653.1; NM_001174182.1.
DR   AlphaFoldDB; Q41782; -.
DR   SMR; Q41782; -.
DR   STRING; 4577.GRMZM2G066191_P03; -.
DR   PaxDb; Q41782; -.
DR   PRIDE; Q41782; -.
DR   GeneID; 542417; -.
DR   KEGG; zma:542417; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   OrthoDB; 962471at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q41782; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..447
FT                   /note="Tubulin beta-4 chain"
FT                   /id="PRO_0000048358"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..447
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        304
FT                   /note="S -> A (in Ref. 2; AAA19707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50132 MW;  D878A64653013A0E CRC64;
     MREILHIQGG QCGNQIGAKF WEVICGEHCV DSTGRYSGTS SQQLELERIN VYYNEAGGGR
     YVPRAVLMDL EPGTMESIRA GPFGGIFRPD NFVYGQSGAG NNWAKGHYTE GAELIDSVLD
     VVRKEAENCD CLQGFQVCHS LGGGTGSGMG TLLISKIREE YPDRMMLTFS VFPSPKVSDT
     VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLT NPSFGDLNHL ISATMSGVTC
     CLRFPGQLNS DLRKLAVNLI PFPRLHFFMV GFAPLTSRGS QQYRALTVPE LTQQMWDAKN
     MMCSADPRHG RYLTASAMFR GKMSTKEVDE QMINVQNKNS SYFVEWIPNN VKSSVCDIPP
     VGLPMASTFV GNSTSIQEMF RRVSEQFTAM FRRKAFLHWY TSEGMDEMEF TEAESNMNDL
     VAEYQQYQDA TAEEYEEEEH DGEEEHA
 
 
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