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COLD1_ORYSI
ID   COLD1_ORYSI             Reviewed;         468 AA.
AC   A2XX57; Q01HU0;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=GPCR-type G protein COLD1 {ECO:0000305};
DE   AltName: Full=Protein CHILLING TOLERANCE DIVERGENCE 1 {ECO:0000303|PubMed:25728666};
GN   Name=COLD1 {ECO:0000303|PubMed:25728666};
GN   ORFNames=B0403H10-OSIGBa0105A11.8 {ECO:0000312|EMBL:CAH67856.1},
GN   OsI_17258 {ECO:0000312|EMBL:EAY95417.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Guang-Lu-Ai No.4;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=25728666; DOI=10.1016/j.cell.2015.01.046;
RA   Ma Y., Dai X., Xu Y., Luo W., Zheng X., Zeng D., Pan Y., Lin X., Liu H.,
RA   Zhang D., Xiao J., Guo X., Xu S., Niu Y., Jin J., Zhang H., Xu X., Li L.,
RA   Wang W., Qian Q., Ge S., Chong K.;
RT   "COLD1 confers chilling tolerance in rice.";
RL   Cell 160:1209-1221(2015).
CC   -!- FUNCTION: Involved in chilling tolerance.
CC       {ECO:0000269|PubMed:25728666}.
CC   -!- SUBUNIT: Interacts with GPA1/RGA1. {ECO:0000250|UniProtKB:Q7X7S8}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7X7S8};
CC       Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:Q7X7S8}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- MISCELLANEOUS: In cold tolerant cultivars (AC Q7X7S8) Met-187 is
CC       replaced by Lys-187. This polymorphism is associated with divergence in
CC       chilling tolerance of rice cultivars. COLD1 confers adaptation of
CC       japonica rice to chilling and originated from the Chinese wild
CC       populations of Oryza rufipogon. {ECO:0000269|PubMed:25728666}.
CC   -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family.
CC       {ECO:0000305}.
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DR   EMBL; CR855228; CAH67856.1; -; Genomic_DNA.
DR   EMBL; CM000129; EAY95417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XX57; -.
DR   STRING; 39946.A2XX57; -.
DR   TCDB; 1.A.38.1.3; the golgi ph regulator (gphr) family.
DR   EnsemblPlants; BGIOSGA014418-TA; BGIOSGA014418-PA; BGIOSGA014418.
DR   Gramene; BGIOSGA014418-TA; BGIOSGA014418-PA; BGIOSGA014418.
DR   HOGENOM; CLU_030540_1_0_1; -.
DR   OMA; HFNFYHR; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051020; F:GTPase binding; IEA:EnsemblPlants.
DR   GO; GO:0070417; P:cellular response to cold; IEA:EnsemblPlants.
DR   InterPro; IPR025969; ABA_GPCR_dom.
DR   InterPro; IPR022535; Golgi_pH-regulator_cons_dom.
DR   InterPro; IPR015672; GPHR/GTG.
DR   PANTHER; PTHR15948; PTHR15948; 1.
DR   Pfam; PF12430; ABA_GPCR; 1.
DR   Pfam; PF12537; GPHR_N; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Endoplasmic reticulum; Lipoprotein; Membrane;
KW   Myristate; Reference proteome; Stress response; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7X7S8"
FT   CHAIN           2..468
FT                   /note="GPCR-type G protein COLD1"
FT                   /id="PRO_0000432810"
FT   TRANSMEM        7..27
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..319
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        437..457
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   COILED          243..279
FT                   /evidence="ECO:0000255"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7X7S8"
SQ   SEQUENCE   468 AA;  53407 MW;  7A908F405918016B CRC64;
     MGWGAVVYEG GVVGASLVGL GWAGLWFLNR RLYKEYEERR ALVQILFGLV FAFSCNLFQL
     VLFEILPVLS KHARFLNWHL DLFCLILLLV FVLPYYHCYL LLRNSGVRRE RALLVAALFL
     LVFLYGFWRM GIHFPMPSPE KGFFTMPQLV SRIGVIGVSV MAVLSGFGAV NLPYSYLSLF
     IREIDEMDIK TLERQLMQSM ETCIAKKKKI VLSKMEMERI QGSEEKLKAR SFLKRIVGTV
     VRSVQEDQTE QDIKSLDAEV QALEELSKQL FLEIYELRQA KIAAAFSRTW RGHAQNLLGY
     ALSVYCVYKM LKSLQSVVFK EAGSVDPVTM TITIFLRHFD IGIDVTLLSQ YISLIFIGML
     VVISVRGFLA NVMKFFFAVS RVGSGSTTNV VLFLSEIMGM YFISSILLIR KSLANEYRVI
     ITDVLGGDIQ FDFYHRWFDA IFVASAFLSL LLISAQYTSR QTDKHPID
 
 
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