O04153 (CALR3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calreticulin-3

Gene names

Name:	CRT3
Ordered Locus Names:	At1g08450
ORF Names:	T27G7.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Domain	Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity By similarity. The interaction with glycans occurs through a binding site in the globular lectin domain By similarity. The zinc binding sites are localized to the N-domain By similarity.
Sequence similarities	Belongs to the calreticulin family.
Sequence caution	The sequence AAF22902.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal
Ligand	Calcium Lectin Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anthocyanin-containing compound metabolic process Inferred from mutant phenotype PubMed 19763087. Source: TAIR calcium ion homeostasis Inferred from genetic interaction PubMed 20596537. Source: TAIR defense response signaling pathway, resistance gene-independent Inferred from mutant phenotype PubMed 19717464. Source: TAIR defense response to bacterium Inferred from mutant phenotype PubMed 19717464. Source: TAIR plant-type hypersensitive response Inferred from mutant phenotype PubMed 19763087. Source: TAIR protein folding Inferred from genetic interaction PubMed 19763087. Source: TAIR
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from direct assay PubMed 19763087. Source: TAIR
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O04153-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 424	396	Calreticulin-3		PRO_0000004186
Regions
	Repeat	200 – 211	12	1-1
	Repeat	219 – 230	12	1-2
	Repeat	236 – 247	12	1-3
	Repeat	254 – 265	12	1-4
	Repeat	269 – 279	11	2-1
	Repeat	283 – 293	11	2-2
	Repeat	297 – 307	11	2-3
	Region	200 – 265	66	4 X approximate repeats
	Region	269 – 307	39	3 X approximate repeats
	Motif	421 – 424	4	Prevents secretion from ER Potential
	Compositional bias	361 – 414	54	Arg/Glu/Lys-rich
Sites
	Binding site	118	1	Carbohydrate By similarity
	Binding site	120	1	Carbohydrate By similarity
	Binding site	137	1	Carbohydrate By similarity
	Binding site	144	1	Carbohydrate By similarity
	Binding site	327	1	Carbohydrate By similarity
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Disulfide bond	114 ↔ 146		By similarity
Experimental info
	Sequence conflict	279	1	S → F in AAC49697. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 64445A06359F0B8C	FASTA	424	49,844
	10 20 30 40 50 60 MGLPQNKLSF FCFFFLVSVL TLAPLAFSEI FLEEHFEGGW KSRWVLSDWK RNEGKAGTFK 70 80 90 100 110 120 HTAGKWPGDP DNKGIQTYND AKHYAISAKI PEFSNKNRTL VVQYSVKIEQ DIECGGAYIK 130 140 150 160 170 180 LLSGYVNQKQ FGGDTPYSLM FGPDICGTQT KKLHVIVSYQ GQNYPIKKDL QCETDKLNHF 190 200 210 220 230 240 YTFILRPDAS YSVLVDNKER EFGSMYTDWD ILPPRKIKVK NAKKPEDWDD REYIDDPNDV 250 260 270 280 290 300 KPEGFDSIPR EIPDRKAKEP EDWDEEENGL WEPPKIPNSA YKGPWKAKRI KNPNYKGKWK 310 320 330 340 350 360 NPWIDNPEFE DDPDLYVLKS IKYAGIEVWQ VKAGSIFDNI LICDDPAYAR SIVDDYFAQH 370 380 390 400 410 420 RESEKELFAE AEKERKARED EEARIAREEG ERRRKERDHR YGDRRRRYKR PNPRDYMDDY HDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana." Nelson D.E., Glaunsinger B., Bohnert H.J. Plant Physiol. 114:29-37(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U66345 mRNA. Translation: AAC49697.1. AC006932 Genomic DNA. Translation: AAF22902.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28291.1. AY056320 mRNA. Translation: AAL07169.1.
IPI	IPI00536618.
RefSeq	NP_563816.1. NM_100718.4.
UniGene	At.24804.
3D structure databases
ProteinModelPortal	O04153.
SMR	O04153. Positions 30-385.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48930N.
Proteomic databases
PaxDb	O04153.
PRIDE	O04153.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G08450.1; AT1G08450.1; AT1G08450.
GeneID	837365.
KEGG	ath:AT1G08450.
Organism-specific databases
TAIR	At1g08450.
Phylogenomic databases
eggNOG	NOG295283.
HOGENOM	HOG000192435.
InParanoid	O04153.
KO	K08057.
OMA	EREFGSM.
PhylomeDB	O04153.
ProtClustDB	CLSN2916983.
Gene expression databases
ArrayExpress	O04153.
Genevestigator	O04153.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. IPR009033. Calreticulin/calnexin_P_dom. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. [Graphical view]
PANTHER	PTHR11073. PTHR11073. 1 hit.
Pfam	PF00262. Calreticulin. 1 hit. [Graphical view]
PIRSF	PIRSF002356. Calreticulin. 1 hit.
PRINTS	PR00626. CALRETICULIN.
SUPFAM	SSF63887. Calret_calnex_P. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 1 hit. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CALR3_ARATH

Accession

Primary (citable) accession number: O04153
Secondary accession number(s): Q93ZR4, Q9SJE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program