ID   TBB1_DAUCA              Reviewed;         315 AA.
AC   P20364;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
DE   Flags: Fragment;
GN   Name=TUBB1;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Kintoki;
RX   PubMed=9195054; DOI=10.1247/csf.22.291;
RA   Okamura S., Naito K., Sonehara S., Ohkawa H., Kuramori S., Tatsuta M.,
RA   Minamizono M., Kataoka T.;
RT   "Characterization of the carrot beta-tubulin gene coding a divergent
RT   isotype, beta-2.";
RL   Cell Struct. Funct. 22:291-298(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 277-315.
RX   PubMed=3178860;
RA   Okamura S., Azumano I.;
RT   "Primary structure of the carboxy-terminal region of a higher plant beta-
RT   tubulin.";
RL   Biochem. Int. 16:1103-1109(1988).
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; U64029; AAB64307.1; -; Genomic_DNA.
DR   PIR; PQ0011; PQ0011.
DR   AlphaFoldDB; P20364; -.
DR   SMR; P20364; -.
DR   PRIDE; P20364; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
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.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding.
FT   CHAIN           <1..315
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048338"
FT   REGION          295..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   315 AA;  35812 MW;  682C434581983B0F CRC64;
     FQVCHSLGGG TGSGMGTLLI SKIREEYPDR MMLTFSVFPS PKVSDTVVEP YNATLSVHQL
     VENADVCMVL DNEALYDICF RTLKLTTPSF GDLNHLISAT MSGVTCSLRF PGQLNSDLRK
     LAVILIPFPR LHFFMVGFAP LTSRGSQQYR SLSVPELTQQ MWDSKNMMCA ADPRHGRYLT
     ASAMFREKMS TKDLDEQMIN VQNKNSSYFV EWIPNNVKST VCDIPPTGLK MASTFIGNST
     SIQEMFRRVS EQFTAMFRRK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY QQYQDATADE
     EEYYEDEEEE EAQGM