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Database: UniProt
Entry: Q9XF98
LinkDB: Q9XF98
Original site: Q9XF98 
ID   CALR_PRUAR              Reviewed;         421 AA.
AC   Q9XF98;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   01-OCT-2014, entry version 84.
DE   RecName: Full=Calreticulin;
DE   Flags: Precursor;
OS   Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae;
OC   Amygdaleae; Prunus.
OX   NCBI_TaxID=36596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bergeron; TISSUE=Endocarp, and Mesocarp;
RA   Mbeguie-A-Mbeguie D., Fils-Lycaon B.R.;
RT   "Molecular cloning and nucleotide sequence of a calreticulin from
RT   apricot (Prunus armeniaca cv. Bergeron).";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular calcium-binding chaperone promoting folding,
CC       oligomeric assembly and quality control in the ER via the
CC       calreticulin/calnexin cycle. This lectin may interact transiently
CC       with almost all of the monoglucosylated glycoproteins that are
CC       synthesized in the ER (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000255|PROSITE-ProRule:PRU10138}.
CC   -!- DOMAIN: Can be divided into a N-terminal globular domain, a
CC       proline-rich P-domain forming an elongated arm-like structure and
CC       a C-terminal acidic domain. The P-domain binds one molecule of
CC       calcium with high affinity, whereas the acidic C-domain binds
CC       multiple calcium ions with low affinity (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The interaction with glycans occurs through a binding site
CC       in the globular lectin domain. {ECO:0000250}.
CC   -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; AF134733; AAD32207.1; -; mRNA.
DR   ProteinModelPortal; Q9XF98; -.
DR   SMR; Q9XF98; 210-311.
DR   PRIDE; Q9XF98; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.10.250.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009169; Calreticulin.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom.
DR   InterPro; IPR008985; ConA-like_lec_gl_sf.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   PANTHER; PTHR11073; PTHR11073; 1.
DR   Pfam; PF00262; Calreticulin; 1.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF63887; SSF63887; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Lectin; Metal-binding; Repeat; Signal; Zinc.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    421       Calreticulin.
FT                                /FTId=PRO_0000004194.
FT   REPEAT      196    207       1-1.
FT   REPEAT      215    226       1-2.
FT   REPEAT      232    243       1-3.
FT   REPEAT      250    261       1-4.
FT   REPEAT      265    275       2-1.
FT   REPEAT      279    289       2-2.
FT   REPEAT      293    303       2-3.
FT   REGION      196    261       4 X approximate repeats.
FT   REGION      265    303       3 X approximate repeats.
FT   MOTIF       418    421       Prevents secretion from ER.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10138}.
FT   COMPBIAS    357    417       Asp/Glu/Lys-rich.
FT   BINDING     114    114       Carbohydrate. {ECO:0000250}.
FT   BINDING     116    116       Carbohydrate. {ECO:0000250}.
FT   BINDING     133    133       Carbohydrate. {ECO:0000250}.
FT   BINDING     140    140       Carbohydrate. {ECO:0000250}.
FT   BINDING     323    323       Carbohydrate. {ECO:0000250}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    110    142       {ECO:0000250}.
SQ   SEQUENCE   421 AA;  48416 MW;  4F5F94CBAA6C6690 CRC64;
     MAFRVPNSSL LSLILLSLLA IASAKVFFEE RFEDGWDKRW VTSEWKKDEN LAGEWNYTSG
     KWNGDPNDKG IQTSEDYRFY AISAEFPEFS NKDKTLVFQF SVKHEQKLDC GGGYIKLLSG
     DVDQKKFGGD TPYSIMFGPD ICGYSTKKVH AILNYNNTNN LIKKDVPCET DQLTHVYTFI
     IRPDATYSIL IDNLEKQTGS LYSDWDLLPA KKIKDPEAKK PEDWEDQEYI PDPEDKKPEG
     YDDIPKEITD PDAKKPEDWD DEEDGEWTAP TIPNPEYKGE WKPKKIKNPN FKGKWKAPLI
     DNPEFKDDPE LYVYPNLKYV GIELWQVKSG TLFDNILITD EPEYAKQLAE ETWGKQKDAE
     KAAFEELEKK LQEEESKEDP VDSDAEDDDN EAEDGEESDS ESKPDSTEES AETEAEKHDE
     L
//
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