位置:首页 > 蛋白库 > 2SS3_ARATH
2SS3_ARATH
ID   2SS3_ARATH              Reviewed;         164 AA.
AC   P15459;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=2S seed storage protein 3;
DE   AltName: Full=2S albumin storage protein;
DE   AltName: Full=NWMU2-2S albumin 3;
DE   Contains:
DE     RecName: Full=2S seed storage protein 3 small subunit;
DE   Contains:
DE     RecName: Full=2S seed storage protein 3 large subunit;
DE   Flags: Precursor;
GN   Name=AT2S3; OrderedLocusNames=At4g27160; ORFNames=T24A18.110;
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 [GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=16666238; DOI=10.1104/pp.87.4.859;
RA   Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J.,
RA   van Damme J., Segura M., Gheysen G., van Montagu M., Vandekerckhove J.;
RT   "Determination of the processing sites of an Arabidopsis 2S albumin and
RT   characterization of the complete gene family.";
RL   Plant Physiol. 87:859-866(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=8012403; DOI=10.1046/j.1365-313x.1994.05040493.x;
RA   da Silva Conceicao A., Krebbers E.;
RT   "A cotyledon regulatory region is responsible for the different spatial
RT   expression patterns of Arabidopsis 2S albumin genes.";
RL   Plant J. 5:493-505(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-164.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RX   PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA   Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA   Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA   Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
RN   [7]
RP   INTERACTION WITH AHK2.
RX   PubMed=18642946; DOI=10.1021/pr0703831;
RA   Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT   "Toward an interaction map of the two-component signaling pathway of
RT   Arabidopsis thaliana.";
RL   J. Proteome Res. 7:3649-3660(2008).
CC   -!- FUNCTION: This is a 2S seed storage protein.
CC   -!- SUBUNIT: The mature protein consists of a small and a large chain
CC       linked by disulfide bonds. Interacts with AHK2.
CC       {ECO:0000269|PubMed:18642946}.
CC   -!- INTERACTION:
CC       P15459; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1807552, EBI-1100634;
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {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; AH001334; AAA32745.1; -; Genomic_DNA.
DR   EMBL; Z24744; CAA80868.1; -; Genomic_DNA.
DR   EMBL; AL035680; CAB38846.1; -; Genomic_DNA.
DR   EMBL; AL161566; CAB79571.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85308.1; -; Genomic_DNA.
DR   EMBL; AY080779; AAL87263.1; -; mRNA.
DR   EMBL; AY117157; AAM51232.1; -; mRNA.
DR   EMBL; Z17580; CAA79001.1; -; mRNA.
DR   PIR; JA0163; NWMU3.
DR   RefSeq; NP_194446.1; NM_118850.3.
DR   AlphaFoldDB; P15459; -.
DR   SMR; P15459; -.
DR   BioGRID; 14111; 3.
DR   IntAct; P15459; 1.
DR   STRING; 3702.AT4G27160.1; -.
DR   PaxDb; P15459; -.
DR   PRIDE; P15459; -.
DR   ProteomicsDB; 244610; -.
DR   EnsemblPlants; AT4G27160.1; AT4G27160.1; AT4G27160.
DR   GeneID; 828824; -.
DR   Gramene; AT4G27160.1; AT4G27160.1; AT4G27160.
DR   KEGG; ath:AT4G27160; -.
DR   Araport; AT4G27160; -.
DR   TAIR; locus:2136486; AT4G27160.
DR   eggNOG; ENOG502S7EV; Eukaryota.
DR   HOGENOM; CLU_131213_1_0_1; -.
DR   InParanoid; P15459; -.
DR   OMA; CDLEPRR; -.
DR   OrthoDB; 1466684at2759; -.
DR   PhylomeDB; P15459; -.
DR   PRO; PR:P15459; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P15459; baseline and differential.
DR   Genevisible; P15459; AT.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; PTHR35496; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Reference proteome; Seed storage protein; Signal;
KW   Storage protein.
FT   SIGNAL          1..21
FT   PROPEP          22..37
FT                   /id="PRO_0000032097"
FT   CHAIN           38..72
FT                   /note="2S seed storage protein 3 small subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000032098"
FT   PROPEP          73..81
FT                   /id="PRO_0000032099"
FT   CHAIN           82..164
FT                   /note="2S seed storage protein 3 large subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000032100"
SQ   SEQUENCE   164 AA;  18762 MW;  C9BEB6718549F248 CRC64;
     MANKLFLVCA TLALCFLLTN ASIYRTVVEF EEDDASNPVG PRQRCQKEFQ QSQHLRACQR
     WMSKQMRQGR GGGPSLDDEF DFEGPQQGYQ LLQQCCNELR QEEPVCVCPT LKQAARAVSL
     QGQHGPFQSR KIYQSAKYLP NICKIQQVGE CPFQTTIPFF PPYY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025