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Q9SP22

- CALR_MAIZE

UniProt

Q9SP22 - CALR_MAIZE

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Protein

Calreticulin

Gene
CRT
Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Carbohydrate By similarity
Binding sitei117 – 1171Carbohydrate By similarity
Binding sitei134 – 1341Carbohydrate By similarity
Binding sitei141 – 1411Carbohydrate By similarity
Binding sitei324 – 3241Carbohydrate By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Gene namesi
Name:CRT
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiQ9SP22.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed predictionAdd
BLAST
Chaini26 – 420395CalreticulinPRO_0000004191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9SP22.

Structurei

3D structure databases

ProteinModelPortaliQ9SP22.
SMRiQ9SP22. Positions 212-312.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati197 – 208121-1Add
BLAST
Repeati216 – 227121-2Add
BLAST
Repeati233 – 244121-3Add
BLAST
Repeati251 – 262121-4Add
BLAST
Repeati266 – 276112-1Add
BLAST
Repeati280 – 290112-2Add
BLAST
Repeati294 – 304112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 262664 X approximate repeatsAdd
BLAST
Regioni266 – 304393 X approximate repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi417 – 4204Prevents secretion from ER Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi358 – 41659Asp/Glu/Lys-richAdd
BLAST

Domaini

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 similaritiesi

Belongs to the calreticulin family.

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR001580. 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]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SP22-1 [UniParc]FASTAAdd to Basket

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MAIRKGSSYA VAALLALASV AAVAGEVFFQ EKFEDGWESR WVKSEWKKDE    50
NMAGEWNHTS GKWNGDAEDK GIQTSEDYRF YAISAEYPEF SNKDKTLVLQ 100
FSVKHEQKLD CGGGYVKLLG GDVDQKTLGG DTSYSIISRP DISRYSTKKV 150
HTILTKDGKN HLIKKDVPCQ TDQLTHVYTF IIRPDATYSI LIDNEEKHTG 200
SIYEHWDILP PKKIKDPEAK KPEDWDDKEY IPDPEDKKPE GYDDIPKEIP 250
DPDAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKQKKIKNP NYQGKWKAPM 300
IDNPDFKDDP YIYAFDSLKY IGIELWQVKS GTLFDNIIIT DDPALAKTFA 350
EETWGKHKEA EKAAFDEAEK KKEEEDAAKG GDDEDDDLED EEDDEKADED 400
KADSDAEDGK DSDDEKHDEL 420
Length:420
Mass (Da):47,940
Last modified:May 1, 2000 - v1
Checksum:iE73B7F43E7494735
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190454 mRNA. Translation: AAF01470.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190454 mRNA. Translation: AAF01470.1 .

3D structure databases

ProteinModelPortali Q9SP22.
SMRi Q9SP22. Positions 212-312.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9SP22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei Q9SP22.

Family and domain databases

Gene3Di 2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProi 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 ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Expression of the high capacity calcium-binding domain of calreticulin increases bioavailable calcium stores in plants."
    Wyatt S.E., Tsou P.-L., Robertson D.
    Transgenic Res. 11:1-10(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiCALR_MAIZE
AccessioniPrimary (citable) accession number: Q9SP22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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