SSRA_ARATH
ID SSRA_ARATH Reviewed; 258 AA.
AC P45434; Q94A59; Q9SKP7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Translocon-associated protein subunit alpha;
DE Short=TRAP-alpha;
DE AltName: Full=Signal sequence receptor subunit alpha;
DE Short=SSR-alpha;
DE Flags: Precursor;
GN OrderedLocusNames=At2g21160; ORFNames=F26H11.8;
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=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 [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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-258.
RX PubMed=8050590; DOI=10.1016/0014-5793(94)00693-8;
RA Hartmann E., Prehn S.;
RT "The N-terminal region of the alpha-subunit of the TRAP complex has a
RT conserved cluster of negative charges.";
RL FEBS Lett. 349:324-326(1994).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC calcium to the ER membrane and thereby regulate the retention of ER
CC resident proteins. May be involved in the recycling of the
CC translocation apparatus after completion of the translocation process
CC or may function as a membrane-bound chaperone facilitating folding of
CC translocated proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P45434-1; Sequence=Displayed;
CC -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC being highly negatively charged, and the cytoplasmic C-terminus
CC positively charged.
CC -!- PTM: Phosphorylated in its cytoplasmic tail. {ECO:0000250}.
CC -!- MISCELLANEOUS: Seems to bind calcium.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
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DR EMBL; AC006264; AAD29800.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07129.1; -; Genomic_DNA.
DR EMBL; AY050351; AAK91368.1; -; mRNA.
DR EMBL; L32016; AAA21820.1; -; mRNA.
DR PIR; H84597; H84597.
DR RefSeq; NP_565498.1; NM_127686.4. [P45434-1]
DR AlphaFoldDB; P45434; -.
DR BioGRID; 2004; 5.
DR IntAct; P45434; 2.
DR STRING; 3702.AT2G21160.1; -.
DR SwissPalm; P45434; -.
DR PaxDb; P45434; -.
DR PRIDE; P45434; -.
DR ProteomicsDB; 228386; -. [P45434-1]
DR EnsemblPlants; AT2G21160.1; AT2G21160.1; AT2G21160. [P45434-1]
DR GeneID; 816651; -.
DR Gramene; AT2G21160.1; AT2G21160.1; AT2G21160. [P45434-1]
DR KEGG; ath:AT2G21160; -.
DR Araport; AT2G21160; -.
DR TAIR; locus:2047077; AT2G21160.
DR eggNOG; KOG1631; Eukaryota.
DR HOGENOM; CLU_095145_0_0_1; -.
DR InParanoid; P45434; -.
DR OMA; FNFHIQN; -.
DR PhylomeDB; P45434; -.
DR PRO; PR:P45434; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P45434; baseline and differential.
DR Genevisible; P45434; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR InterPro; IPR005595; TRAP_alpha.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..258
FT /note="Translocon-associated protein subunit alpha"
FT /id="PRO_0000033287"
FT TOPO_DOM 25..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 258 AA; 28167 MW; C424ACFAC834EF59 CRC64;
MMNLRVLFLA LLLLASPLLQ VARCQSDAED HSSLVDDVVG ENTDDAVEED DHDLDMNLSS
FPGVETVCVF PKNSAKLVPA GEETELLVGL KNEGKTRVGV MGIRASVHLP YDHKLLVQNL
TMLRLNNASI PTSLQATFPY IFAVSQYLQP GAFDLVGYII YDVEGKPYQS VFYNGTIEVV
ESGGLLSGES VFLLTLGIGL LLLLGLWAYS QVQRLTKKTK KVSKVEVGTR STEASLDEWL
EGTTLAKTSS GKTKNKKN
