ID   TBB2_HOMAM              Reviewed;         452 AA.
AC   Q94571;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-II tubulin;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8666270; DOI=10.1016/0378-1119(96)00006-6;
RA   Demers D.M., Metcalf A.E., Talbot P., Hyman B.C.;
RT   "Multiple lobster tubulin isoforms are encoded by a simple gene family.";
RL   Gene 171:185-191(1996).
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; U66319; AAB07482.1; -; mRNA.
DR   AlphaFoldDB; Q94571; -.
DR   SMR; Q94571; -.
DR   PRIDE; Q94571; -.
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; 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; PS00228; TUBULIN_B_AUTOREG; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..452
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048274"
FT   REGION          431..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..452
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         145..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  50930 MW;  48D58044BE72CACC CRC64;
     MREIVHIQTG QCGNQIGTKF WEIISDEHGI QPTGEYTTGV EKDLMELQLE RINVYYNEGN
     QGKYVPRAVL VDLEPGTMDS VRAGPHGQLF KPDSFVFGQS GAGNNWAKGH YTEGAELVDS
     VLDVVRKKSE KCDCLQGFQL THSLGGVTGS GMGTLLVSKI LEEFPDRIMV TFSVVPSPKV
     SDTVVEPYNA TLSIHQLVEN TDETYCIDNE ALYDICFRTL KLQNPTYGDL NHLVSLTMSG
     VTTCLRFPGQ LNADLRKLAV NMVPFPRLHF FMPGFAPLTA RGSQQYRALT VPELTQQMFD
     AKNMMAACDP RHGRYLTVAA IFRGRMSMRE VDDQMYNIQN KNSSFFVEWI PNNVKTAVCD
     IPPRGLKMSA TFIGNSTAIQ ELFKRVSEQF TAMFRRKAFL HWYTGEGMDE MEFTEAESNM
     NDLVSEYQQY QEATADDEAE FEEEGEVEGE YD