ID   TBA3_MESAU              Reviewed;         196 AA.
AC   P86234;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Tubulin alpha-3 chain {ECO:0000250|UniProtKB:P05214};
DE   Flags: Fragments;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC       resulting in polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into axonemes
CC       (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC       cells, centrioles, axonemes, and the mitotic spindle. Both
CC       modifications can coexist on the same protein on adjacent residues, and
CC       lowering polyglycylation levels increases polyglutamylation, and
CC       reciprocally. Cilia and flagella glycylation is required for their
CC       stability and maintenance. Flagella glycylation controls sperm
CC       motility. {ECO:0000250|UniProtKB:P05214}.
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC       resulting in polyglutamate chains on the gamma-carboxyl group (By
CC       similarity). Polyglutamylation plays a key role in microtubule severing
CC       by spastin (SPAST). SPAST preferentially recognizes and acts on
CC       microtubules decorated with short polyglutamate tails: severing
CC       activity by SPAST increases as the number of glutamates per tubulin
CC       rises from one to eight, but decreases beyond this glutamylation
CC       threshold (By similarity). Glutamylation is also involved in cilia
CC       motility (By similarity). {ECO:0000250|UniProtKB:P05214,
CC       ECO:0000250|UniProtKB:Q71U36}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000255}.
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DR   AlphaFoldDB; P86234; -.
DR   SMR; P86234; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
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:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 3.30.1330.20; -; 2.
DR   Gene3D; 3.40.50.1440; -; 2.
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; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 3.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
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.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nitration;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           <1..>196
FT                   /note="Tubulin alpha-3 chain"
FT                   /id="PRO_0000394741"
FT   MOD_RES         19
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P68368"
FT   NON_CONS        57..58
FT                   /evidence="ECO:0000305"
FT   NON_CONS        65..66
FT                   /evidence="ECO:0000305"
FT   NON_CONS        154..155
FT                   /evidence="ECO:0000305"
FT   NON_CONS        185..186
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         196
SQ   SEQUENCE   196 AA;  22006 MW;  3096E7AA00B336D7 CRC64;
     AVFVDLEPTV VDEVRTGTYR QLFHPEQLIT GKEDAANNYA RGHYTIGKEI VDLVLDRLSV
     DYGKKNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA
     TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKTIQFVD WCPTGFKVGI NYQPPTVVPG
     GDLAKLDHKF DLMYAK