ID   TBB1_CHOCR              Reviewed;         453 AA.
AC   Q42480;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
GN   Name=TUBB; Synonyms=TUB1;
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Stackhouse;
RX   PubMed=7599316; DOI=10.1007/bf00020250;
RA   Liaud M.-F., Brandt U., Cerff R.;
RT   "The marine red alga Chondrus crispus has a highly divergent beta-tubulin
RT   gene with a characteristic 5' intron: functional and evolutionary
RT   implications.";
RL   Plant Mol. Biol. 28:313-325(1995).
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; X71785; CAA50670.1; -; Genomic_DNA.
DR   EMBL; X71784; CAA50669.1; -; mRNA.
DR   PIR; S55935; S49168.
DR   RefSeq; XP_005715672.1; XM_005715615.1.
DR   AlphaFoldDB; Q42480; -.
DR   SMR; Q42480; -.
DR   EnsemblPlants; CDF35853; CDF35853; CHC_T00004301001.
DR   GeneID; 17323383; -.
DR   Gramene; CDF35853; CDF35853; CHC_T00004301001.
DR   KEGG; ccp:CHC_T00004301001; -.
DR   OMA; RYQGEND; -.
DR   OrthoDB; 962471at2759; -.
DR   PhylomeDB; Q42480; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..453
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048333"
FT   REGION          431..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..453
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  50346 MW;  52C51FB7B1510B1A CRC64;
     MTRSIVSLQV GQCGNQVGLK FWEGISAEHG IDVDGKYIGD RPDQELHRIG VYYNESSSGS
     YVPRAAMLDL EPGVLMAIKN SKRGQLFHPD NFAYGQSGAG NNWAKGHYTE GAELVETALD
     IIRREAETCD VLQGFQVTHS LGGGTGSGMG TLLVSKIREE YPDRMMCTYS VLPSPKVSDT
     VVEPYNCTLS IHQLIENADC VFAIDNEALY NICYNTLKIE QPSYDELNSL ISSVMSGITC
     SLRFPGQLNA DLRKLAVNLV PFPRLHFFAV GHAPLAASNS AGYRSLSVPE LAGQMFDRNN
     MMAEIDPREG RYLTAAVYFR GKVSTKEVED EMTLMQTKNS AYFVEWIPHN IKTSVCDIPA
     AGEKISSAFI GNTTAIEATF KRFGNQFRSM FRRKAFLHWY KSEGMDELEF SEAESNLADL
     VSEYQQYGEA TADGVEGYEE EGYENDHPED DEE