TSA1_ARATH
ID TSA1_ARATH Reviewed; 759 AA.
AC F4ICX9; F4ICY0; Q94AE1; Q9C831;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=TSK-associating protein 1;
DE Flags: Precursor;
GN Name=TSA1; OrderedLocusNames=At1g52410; ORFNames=F19K6.14;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 2).
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 [4]
RP INTERACTION WITH TSK, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP CALCIUM-BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15964904; DOI=10.1093/pcp/pci155;
RA Suzuki T., Nakajima S., Morikami A., Nakamura K.;
RT "An Arabidopsis protein with a novel calcium-binding repeat sequence
RT interacts with TONSOKU/MGOUN3/BRUSHY1 involved in meristem maintenance.";
RL Plant Cell Physiol. 46:1452-1461(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [6]
RP IDENTIFICATION, AND DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=18780803; DOI=10.1105/tpc.108.059345;
RA Yamada K., Nagano A.J., Nishina M., Hara-Nishimura I., Nishimura M.;
RT "NAI2 is an endoplasmic reticulum body component that enables ER body
RT formation in Arabidopsis thaliana.";
RL Plant Cell 20:2529-2540(2008).
RN [7]
RP FUNCTION, AND INTERACTION WITH CSN1.
RC STRAIN=cv. Columbia;
RX PubMed=22133685; DOI=10.1016/j.jgg.2011.08.007;
RA Li W., Zang B., Liu C., Lu L., Wei N., Cao K., Deng X.W., Wang X.;
RT "TSA1 interacts with CSN1/CSN and may be functionally involved in
RT Arabidopsis seedling development in darkness.";
RL J. Genet. Genomics 38:539-546(2011).
RN [8]
RP INDUCTION.
RX PubMed=22102697; DOI=10.1093/pcp/pcr156;
RA Yamada K., Hara-Nishimura I., Nishimura M.;
RT "Unique defense strategy by the endoplasmic reticulum body in plants.";
RL Plant Cell Physiol. 52:2039-2049(2011).
RN [9]
RP FUNCTION, INTERACTION WITH GIP1, AND SUBCELLULAR LOCATION.
RX PubMed=24348487; DOI=10.3389/fpls.2013.00480;
RA Batzenschlager M., Masoud K., Janski N., Houlne G., Herzog E., Evrard J.L.,
RA Baumberger N., Erhardt M., Nomine Y., Kieffer B., Schmit A.C.,
RA Chaboute M.E.;
RT "The GIP gamma-tubulin complex-associated proteins are involved in nuclear
RT architecture in Arabidopsis thaliana.";
RL Front. Plant Sci. 4:480-480(2013).
CC -!- FUNCTION: Involved in seedling development in the dark. May be
CC involved, when interacting with TSK, in the organization of spindle
CC microtubules and may participate, when interacting with GIP1, in
CC structural links between the nuclear envelope and the cytoskeleton.
CC {ECO:0000269|PubMed:22133685, ECO:0000269|PubMed:24348487}.
CC -!- SUBUNIT: Homomultimer. Interacts (via C-terminal domain) with GIP1,
CC CSN1 (via N-terminal domain) and TSK (via TPR repeats).
CC {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:22133685,
CC ECO:0000269|PubMed:24348487}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus envelope
CC {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Cytoplasm
CC {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Note=In
CC interphase, found in ER bodies and at the nuclear envelope
CC (PubMed:24348487). During mitosis, concentrates in limited areas close
CC to the ends of spindle microtubules ahead of separating chromatids
CC (PubMed:15964904). {ECO:0000269|PubMed:15964904,
CC ECO:0000269|PubMed:24348487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4ICX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4ICX9-2; Sequence=VSP_056759;
CC -!- TISSUE SPECIFICITY: Expressed preferentially in flowers and shoot apex.
CC {ECO:0000269|PubMed:15964904}.
CC -!- INDUCTION: Up-regulated by wounding and jasmonic acid treatment.
CC {ECO:0000269|PubMed:22102697}.
CC -!- DOMAIN: Contains a N-terminal NAI2 domain (474-759).
CC {ECO:0000269|PubMed:18780803}.
CC -!- PTM: Binds calcium through the EFE repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC037424; AAG51543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32802.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32803.1; -; Genomic_DNA.
DR EMBL; AY048247; AAK82509.1; -; mRNA.
DR EMBL; BT005818; AAO64753.1; -; mRNA.
DR PIR; D96564; D96564.
DR RefSeq; NP_564607.1; NM_104119.3. [F4ICX9-2]
DR RefSeq; NP_849797.1; NM_179466.3. [F4ICX9-1]
DR AlphaFoldDB; F4ICX9; -.
DR SMR; F4ICX9; -.
DR BioGRID; 26896; 3.
DR DIP; DIP-61420N; -.
DR IntAct; F4ICX9; 1.
DR STRING; 3702.AT1G52410.2; -.
DR PaxDb; F4ICX9; -.
DR PRIDE; F4ICX9; -.
DR ProMEX; F4ICX9; -.
DR ProteomicsDB; 232474; -. [F4ICX9-1]
DR EnsemblPlants; AT1G52410.1; AT1G52410.1; AT1G52410. [F4ICX9-2]
DR EnsemblPlants; AT1G52410.2; AT1G52410.2; AT1G52410. [F4ICX9-1]
DR GeneID; 841671; -.
DR Gramene; AT1G52410.1; AT1G52410.1; AT1G52410. [F4ICX9-2]
DR Gramene; AT1G52410.2; AT1G52410.2; AT1G52410. [F4ICX9-1]
DR KEGG; ath:AT1G52410; -.
DR Araport; AT1G52410; -.
DR TAIR; locus:2018164; AT1G52410.
DR OMA; DSHFATA; -.
DR OrthoDB; 369553at2759; -.
DR PRO; PR:F4ICX9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4ICX9; baseline and differential.
DR Genevisible; F4ICX9; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Nucleus; Reference proteome; Repeat; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..759
FT /note="TSK-associating protein 1"
FT /id="PRO_0000430466"
FT REPEAT 91..138
FT /note="EFE repeat 1"
FT REPEAT 139..176
FT /note="EFE repeat 2"
FT REPEAT 177..215
FT /note="EFE repeat 3"
FT REPEAT 216..254
FT /note="EFE repeat 4"
FT REPEAT 255..293
FT /note="EFE repeat 5"
FT REPEAT 294..329
FT /note="EFE repeat 6"
FT REPEAT 330..368
FT /note="EFE repeat 7"
FT REPEAT 369..407
FT /note="EFE repeat 8"
FT REPEAT 408..443
FT /note="EFE repeat 9"
FT REPEAT 444..473
FT /note="EFE repeat 10"
FT REGION 55..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..473
FT /note="10 X approximate EFE repeat"
FT REGION 154..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..461
FT /evidence="ECO:0000255"
FT COILED 685..734
FT /evidence="ECO:0000255"
FT COMPBIAS 284..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 271..274
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_056759"
FT CONFLICT 200
FT /note="Q -> R (in Ref. 3; AAK82509/AAO64753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 84376 MW; A8283CFA29FFD160 CRC64;
MEIYTMKTNF LVLALSLCIL LSSFHEVSCQ DDGSGLSNLD LIERDYQDSV NALQGKDDED
QSAKIQSENQ NNTTVTDKNT ISLSLSDESE VGSVSDESVG RSSLLDQIKL EFEAHHNSIN
QAGSDGVKAE SKDDDEELSA HRQKMLEEIE HEFEAASDSL KQLKTDDVNE GNDEEHSAKR
QSLLEEIERE FEAATKELEQ LKVNDFTGDK DDEEHSAKRK SMLEAIEREF EAAMEGIEAL
KVSDSTGSGD DEEQSAKRLS MLEEIEREFE AASKGLEQLR ASDSTADNNE EEHAAKGQSL
LEEIEREFEA ATESLKQLQV DDSTEDKEHF TAAKRQSLLE EIEREFEAAT KDLKQLNDFT
EGSADDEQSA KRNKMLEDIE REFEAATIGL EQLKANDFSE GNNNEEQSAK RKSMLEEIER
EFEAAIGGLK QIKVDDSRNL EEESAKRKII LEEMEREFEE AHSGINAKAD KEESAKKQSG
SAIPEVLGLG QSGGCSCSKQ DEDSSIVIPT KYSIEDILSE ESAVQGTETS SLTASLTQLV
ENHRKEKESL LGHRVLTSPS IASSTSESSA TSETVETLRA KLNELRGLTA RELVTRKDFG
QILITAASFE ELSSAPISYI SRLAKYRNVI KEGLEASERV HIAQVRAKML KEVATEKQTA
VDTHFATAKK LAQEGDALFV KIFAIKKLLA KLEAEKESVD GKFKETVKEL SHLLADASEA
YEEYHGAVRK AKDEQAAEEF AKEATQSAEI IWVKFLSSL
