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Database: UniProt
Entry: I1JRY0_SOYBN
LinkDB: I1JRY0_SOYBN
Original site: I1JRY0_SOYBN 
ID   I1JRY0_SOYBN            Unreviewed;       474 AA.
AC   I1JRY0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN   Name=100775439 {ECO:0000313|EnsemblPlants:KRH68879};
GN   ORFNames=GLYMA_03G255800 {ECO:0000313|EMBL:KRH68880.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH68880.1};
RN   [1] {ECO:0000313|EMBL:KRH68880.1, ECO:0000313|EnsemblPlants:KRH68879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH68879};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH68880.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH68879}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH68879};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH68880.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH68880.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome. {ECO:0000256|RuleBase:RU000352}.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles, suggesting that it is involved in the minus-end
CC       nucleation of microtubule assembly. {ECO:0000256|ARBA:ARBA00002783}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000256|ARBA:ARBA00004267}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR   EMBL; CM000836; KRH68879.1; -; Genomic_DNA.
DR   EMBL; CM000836; KRH68880.1; -; Genomic_DNA.
DR   RefSeq; XP_006576214.1; XM_006576151.2.
DR   AlphaFoldDB; I1JRY0; -.
DR   SMR; I1JRY0; -.
DR   STRING; 3847.I1JRY0; -.
DR   PaxDb; 3847-GLYMA03G41670-3; -.
DR   EnsemblPlants; KRH68879; KRH68879; GLYMA_03G255800.
DR   EnsemblPlants; KRH68880; KRH68880; GLYMA_03G255800.
DR   GeneID; 100775439; -.
DR   Gramene; KRH68879; KRH68879; GLYMA_03G255800.
DR   Gramene; KRH68880; KRH68880; GLYMA_03G255800.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; I1JRY0; -.
DR   OMA; HRYISIL; -.
DR   OrthoDB; 5476567at2759; -.
DR   Proteomes; UP000008827; Chromosome 3.
DR   ExpressionAtlas; I1JRY0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR002454; Gamma_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; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          48..247
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          249..395
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   474 AA;  53264 MW;  441D4E5DC9709D12 CRC64;
     MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKDGILEDF ATQGGDRKDV FFYQADDQHY
     IPRALLIDLE PRVINGIQNS DYRNLYNHEN IFVSDHGGGA GNNWASGYDQ GQHVEEEIMD
     MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLETLNDR YSKKLVQTYS VFPNQMETSD
     VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVERLHL SNPSFAQTNS LVSTVMSAST
     TTLRYPGYMN NDLVGLLASL IPTPRCHFLM TGYTPLTVER QANLIRKTTV LDVMRRLLQA
     KNIMVSSYAR TKDASQAKYI SILNIIQGEV DPTQVHESLQ RIRERKLVNF IEWGPASIQV
     ALSRKSPYVQ TAHRVSGLML ASHTSIRHLF SKTLSQYEKL RKKQAFIDVY RKFPMFADND
     LSEFDESRDI IESLVDEYKA CESPDYIKWG MEDPNNMLTG EGNATGSLDS KSVA
//
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