TBB_PORPU
ID TBB_PORPU Reviewed; 457 AA.
AC P50259;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUBB1;
OS Porphyra purpurea (Red seaweed) (Ulva purpurea).
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Avonport;
RA Mackay R.M., Gallant J.W.;
RT "Expression of beta-tubulin genes in the sporophyte and gametophyte of the
RT red alga Porphyra purpurea.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
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; Z67991; CAA91939.1; -; Genomic_DNA.
DR AlphaFoldDB; P50259; -.
DR SMR; P50259; -.
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; 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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..457
FT /note="Tubulin beta chain"
FT /id="PRO_0000048375"
FT REGION 431..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 50047 MW; 0F2E5BFA7E077DAA CRC64;
MREIVHIQAG QCGNQIGAKF WEVISEEHGI DSSGAYNGTS DLQLDRAEVY YNEGSGGRYV
PRAVLVDLEP GVLDTIKAGP HGGLYRPDNF VAGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RREAEGCDCL QGFQVTHSLG GGTGSGMGTL LVSKIREEFP DRMMCTYSVM PSPKVSDTVV
EPYNCTLSVH QLVENADAVF CIDNEALYNI CYNTLKKPEP AYPDLNKLVS GVMSGITSSL
RFPGQLNSDL RKLAVNLVPF PRLHFFMIGY APLSADGVTA YRAKTVADLT KQMFDPKNMM
ADCDPRNGRY LTASAYFRGH VSTKEVEEQM DAIQTKNSGQ FIDWIPNAIK ASVCDVAPTG
ETMSAAFIGN STAIQDIFKR VGSHFSAMFK RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
ELQQYEAATV EGEEEEDAYA EGAVVNGDQS YEDQYAA
