位置:首页 > 蛋白库 > SPD1_ARATH
SPD1_ARATH
ID   SPD1_ARATH              Reviewed;         684 AA.
AC   F4J3R7; Q0WWY6; Q940C8; Q9CAE6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein SEEDLING PLASTID DEVELOPMENT 1 {ECO:0000303|PubMed:21045120};
DE   Flags: Precursor;
GN   Name=SPD1 {ECO:0000303|PubMed:21045120};
GN   OrderedLocusNames=At3g10420 {ECO:0000312|Araport:AT3G10420};
GN   ORFNames=F13M14.30 {ECO:0000312|EMBL:AAG51387.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-684 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=21045120; DOI=10.1104/pp.110.161414;
RA   Ruppel N.J., Logsdon C.A., Whippo C.W., Inoue K., Hangarter R.P.;
RT   "A mutation in Arabidopsis seedling plastid development1 affects plastid
RT   differentiation in embryo-derived tissues during seedling growth.";
RL   Plant Physiol. 155:342-353(2011).
CC   -!- FUNCTION: Required during eoplast (a highly reduced plastid type
CC       present during the degreening and dehydration stages of seed
CC       maturation) development in embryos and early stages of eoplast
CC       redifferentiation during seedling growth.
CC       {ECO:0000269|PubMed:21045120}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:21045120}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21045120}; Intermembrane side
CC       {ECO:0000269|PubMed:21045120}. Plastid, chloroplast envelope
CC       {ECO:0000269|PubMed:21045120}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4J3R7-1; Sequence=Displayed;
CC       Name=2 {ECO:0000312|EMBL:AEE74904.1};
CC         IsoId=F4J3R7-2; Sequence=VSP_060460, VSP_060461;
CC   -!- DISRUPTION PHENOTYPE: Albino seedlings with defects in etioplast and
CC       amyloplast development leading to degenerate organelle-like structures,
CC       but normal green vegetative tissues (PubMed:21045120). Reduced
CC       hypocotyl gravitropism probably due to the lack of amyloplasts
CC       (PubMed:21045120). {ECO:0000269|PubMed:21045120}.
CC   -!- SIMILARITY: Belongs to the ycf45 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL06991.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE98362.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE98362.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC011560; AAG51387.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74903.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74904.1; -; Genomic_DNA.
DR   EMBL; AK226197; BAE98362.1; ALT_FRAME; mRNA.
DR   EMBL; AY056103; AAL06991.1; ALT_INIT; mRNA.
DR   EMBL; BT004529; AAO42775.1; -; mRNA.
DR   RefSeq; NP_566373.2; NM_111877.3. [F4J3R7-1]
DR   RefSeq; NP_850553.1; NM_180222.1. [F4J3R7-2]
DR   AlphaFoldDB; F4J3R7; -.
DR   STRING; 3702.AT3G10420.2; -.
DR   PaxDb; F4J3R7; -.
DR   PRIDE; F4J3R7; -.
DR   ProteomicsDB; 197235; -. [F4J3R7-1]
DR   EnsemblPlants; AT3G10420.1; AT3G10420.1; AT3G10420. [F4J3R7-2]
DR   EnsemblPlants; AT3G10420.2; AT3G10420.2; AT3G10420. [F4J3R7-1]
DR   GeneID; 820206; -.
DR   Gramene; AT3G10420.1; AT3G10420.1; AT3G10420. [F4J3R7-2]
DR   Gramene; AT3G10420.2; AT3G10420.2; AT3G10420. [F4J3R7-1]
DR   KEGG; ath:AT3G10420; -.
DR   Araport; AT3G10420; -.
DR   TAIR; locus:2075825; AT3G10420.
DR   eggNOG; ENOG502QQ4X; Eukaryota.
DR   HOGENOM; CLU_022515_2_0_1; -.
DR   InParanoid; F4J3R7; -.
DR   OMA; NHWIRNV; -.
DR   OrthoDB; 1035234at2759; -.
DR   PRO; PR:F4J3R7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4J3R7; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR   GO; GO:0031972; C:chloroplast intermembrane space; IDA:UniProtKB.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009657; P:plastid organization; IMP:UniProtKB.
DR   GO; GO:0090677; P:reversible differentiation; IMP:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; IMP:UniProtKB.
DR   CDD; cd02645; R3H_AAA; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR034081; R3H_AAA.
DR   InterPro; IPR045735; Spore_III_AA_AAA+_ATPase.
DR   Pfam; PF19568; Spore_III_AA; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Chloroplast; Developmental protein;
KW   Membrane; Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..78
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           79..684
FT                   /note="Protein SEEDLING PLASTID DEVELOPMENT 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000448862"
FT   REGION          33..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220..227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         541..547
FT                   /note="STTMAQM -> VSFFLHG (in isoform 2)"
FT                   /id="VSP_060460"
FT   VAR_SEQ         548..684
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060461"
SQ   SEQUENCE   684 AA;  75061 MW;  49CF7AB0889AF2BE CRC64;
     MRALNSRLVL IDINSSWQAS RRLISATATA FSSDSSSSFR RTRGARQRIA SSKSPASSPS
     PVRRPSDGFS FDVRSPSSDS SISSRKSPTT APPTVELDAF LEILPPATRK ELVKHEAIEE
     LIEVVMDLGR KPLARFPSGD WVISEQPVTH QDLELAVSKV GDFSDDNRSG IDRSLHRISA
     IRNRKLQVIG LTCRVGRVVS GSAEIIRDLI EGGGSILVIG SPGVGKTTLI REIARMLADE
     HRKRVVIVDT SNEIGGDGDV PHSGIGRARR MQVPNVNLQH DVMIEAVENH MPETIIIDEI
     GTELEALAAS TIAQRGVQLV ATAHGMTIDN IIKNPSLQIL IGGIESVTLG DEEARKRKVQ
     KTILERKGPP TFTCAVEMIS RTECRVHQRL DVTVDAILAG KSAPFEIRQI RGEDDVPHKL
     VTPIPLENLE EEPAPLLNRD FVSELLSDDE DEDFLLIRSN KARSNTYTSP RSSPVHVYTY
     NVLEADLLQV AEVMGLDDEI EVTDDVGEAD VILASSSELK QNSSIRRVAK LHKLPIFVIK
     STTMAQMVKA VRMILGRESF GSAPKAIEKS SVDDIEIKDD APESKPSLEE LDALEEVRLA
     IEYIVIPGGE PVELLPRRSD IIVRQLELVE SYQLAVENLG THLNPRLQIL PRRSTKKTLT
     SSSPQKSADG SMGTTGTRLP FLKD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024