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UCC1_ARATH
ID   UCC1_ARATH              Reviewed;         261 AA.
AC   O82081; Q0WPC5;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Uclacyanin 1 {ECO:0000303|PubMed:9761472};
DE   Flags: Precursor;
GN   Name=UCC1 {ECO:0000303|PubMed:9761472};
GN   OrderedLocusNames=At2g32300 {ECO:0000312|Araport:AT2G32300};
GN   ORFNames=T32F6 {ECO:0000305};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=9761472; DOI=10.1002/pro.5560070907;
RA   Nersissian A.M., Immoos C., Hill M.G., Hart P.J., Williams G.,
RA   Herrmann R.G., Valentine J.S.;
RT   "Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of
RT   phytocyanins: plant-specific mononuclear blue copper proteins.";
RL   Protein Sci. 7:1915-1929(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY.
RX   PubMed=17293437; DOI=10.1104/pp.106.092296;
RA   Khan J.A., Wang Q., Sjoelund R.D., Schulz A., Thompson G.A.;
RT   "An early nodulin-like protein accumulates in the sieve element plasma
RT   membrane of Arabidopsis.";
RL   Plant Physiol. 143:1576-1589(2007).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=~600 nm {ECO:0000269|PubMed:9761472};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC       anchor {ECO:0000255}.
CC   -!- PTM: Glycosylated. {ECO:0000303|PubMed:9761472}.
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DR   EMBL; U76298; AAC32038.1; -; mRNA.
DR   EMBL; AC005700; AAC69948.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08665.1; -; Genomic_DNA.
DR   EMBL; AK229150; BAF01024.1; -; mRNA.
DR   PIR; D84731; D84731.
DR   RefSeq; NP_180789.1; NM_128789.3.
DR   AlphaFoldDB; O82081; -.
DR   SMR; O82081; -.
DR   STRING; 3702.AT2G32300.1; -.
DR   MetOSite; O82081; -.
DR   PaxDb; O82081; -.
DR   ProteomicsDB; 243241; -.
DR   EnsemblPlants; AT2G32300.1; AT2G32300.1; AT2G32300.
DR   GeneID; 817791; -.
DR   Gramene; AT2G32300.1; AT2G32300.1; AT2G32300.
DR   KEGG; ath:AT2G32300; -.
DR   Araport; AT2G32300; -.
DR   TAIR; locus:2062525; AT2G32300.
DR   eggNOG; ENOG502RZRN; Eukaryota.
DR   HOGENOM; CLU_058719_2_1_1; -.
DR   InParanoid; O82081; -.
DR   PRO; PR:O82081; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82081; baseline and differential.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR039391; Phytocyanin.
DR   InterPro; IPR003245; Phytocyanin_dom.
DR   PANTHER; PTHR33021; PTHR33021; 1.
DR   Pfam; PF02298; Cu_bind_like; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
DR   PROSITE; PS51485; PHYTOCYANIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Copper; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..237
FT                   /note="Uclacyanin 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5006739294"
FT   PROPEP          238..261
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000437143"
FT   DOMAIN          24..123
FT                   /note="Phytocyanin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   REGION          194..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         105
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         110
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         115
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   LIPID           237
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   CONFLICT        226
FT                   /note="T -> M (in Ref. 4; BAF01024)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  26451 MW;  8C2BB83F749A764E CRC64;
     MASREMLIII SVLATTLIGL TVATDHTIGG PSGWTVGASL RTWAAGQTFA VGDNLVFSYP
     AAFHDVVEVT KPEFDSCQAV KPLITFANGN SLVPLTTPGK RYFICGMPGH CSQGMKLEVN
     VVPTATVAPT APLPNTVPSL NAPSPSSVLP IQPLLPLNPV PVLSPSSSTP LPSSSLPLIP
     PLSPALSPAT AAGTSLPLFP GSPGSSSSTT STKTVGTFPS STTGTTADLA GADSPPADSS
     SAAKTLVLGF GFMVAMMLHL F
 
 
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