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CALR3_HUMAN
ID   CALR3_HUMAN             Reviewed;         384 AA.
AC   Q96L12; D9N574; Q96LN3;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Calreticulin-3;
DE   AltName: Full=Calreticulin-2;
DE   AltName: Full=Calsperin;
DE   Flags: Precursor;
GN   Name=CALR3; Synonyms=CRT2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND LACK OF
RP   CALCIUM-BINDING.
RX   PubMed=21590275; DOI=10.1007/s00418-011-0817-z;
RA   Nomura R., Orii M., Senda T.;
RT   "Calreticulin-2 is localized in the lumen of the endoplasmic reticulum but
RT   is not a Ca2+ -binding protein.";
RL   Histochem. Cell Biol. 135:531-538(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-8.
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=12384296; DOI=10.1016/s0378-1119(02)00880-6;
RA   Persson S., Rosenquist M., Sommarin M.;
RT   "Identification of a novel calreticulin isoform (Crt2) in human and
RT   mouse.";
RL   Gene 297:151-158(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   VARIANT ARG-82.
RX   PubMed=17655857; DOI=10.1016/j.yjmcc.2007.06.009;
RA   Chiu C., Tebo M., Ingles J., Yeates L., Arthur J.W., Lind J.M.,
RA   Semsarian C.;
RT   "Genetic screening of calcium regulation genes in familial hypertrophic
RT   cardiomyopathy.";
RL   J. Mol. Cell. Cardiol. 43:337-343(2007).
CC   -!- FUNCTION: During spermatogenesis, may act as a lectin-independent
CC       chaperone for specific client proteins such as ADAM3. Required for
CC       sperm fertility (By similarity). CALR3 capacity for calcium-binding may
CC       be absent or much lower than that of CALR. {ECO:0000250,
CC       ECO:0000269|PubMed:21590275}.
CC   -!- SUBUNIT: Component of an EIF2 complex at least composed of
CC       CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138, ECO:0000269|PubMed:21590275}.
CC   -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12384296}.
CC   -!- DOMAIN: Can be divided into a N-terminal globular domain, a proline-
CC       rich P-domain forming an elongated arm-like structure and a C-terminal
CC       acidic domain. The P-domain binds one molecule of calcium with high
CC       affinity, whereas the acidic C-domain binds multiple calcium ions with
CC       low affinity (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The interaction with glycans occurs through a binding site in
CC       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; AB576176; BAJ14705.1; -; mRNA.
DR   EMBL; AK058084; BAB71655.1; -; mRNA.
DR   EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471106; EAW84546.1; -; Genomic_DNA.
DR   EMBL; BC014595; AAH14595.1; -; mRNA.
DR   CCDS; CCDS12344.1; -.
DR   RefSeq; NP_659483.2; NM_145046.4.
DR   AlphaFoldDB; Q96L12; -.
DR   SMR; Q96L12; -.
DR   BioGRID; 125941; 141.
DR   IntAct; Q96L12; 8.
DR   MINT; Q96L12; -.
DR   STRING; 9606.ENSP00000269881; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   GlyGen; Q96L12; 2 sites.
DR   iPTMnet; Q96L12; -.
DR   PhosphoSitePlus; Q96L12; -.
DR   BioMuta; CALR3; -.
DR   DMDM; 116241279; -.
DR   EPD; Q96L12; -.
DR   MassIVE; Q96L12; -.
DR   PaxDb; Q96L12; -.
DR   PeptideAtlas; Q96L12; -.
DR   PRIDE; Q96L12; -.
DR   ProteomicsDB; 77137; -.
DR   Antibodypedia; 66699; 331 antibodies from 28 providers.
DR   DNASU; 125972; -.
DR   Ensembl; ENST00000269881.8; ENSP00000269881.3; ENSG00000269058.6.
DR   GeneID; 125972; -.
DR   KEGG; hsa:125972; -.
DR   MANE-Select; ENST00000269881.8; ENSP00000269881.3; NM_145046.5; NP_659483.2.
DR   UCSC; uc002ned.3; human.
DR   CTD; 125972; -.
DR   DisGeNET; 125972; -.
DR   GeneCards; CALR3; -.
DR   HGNC; HGNC:20407; CALR3.
DR   HPA; ENSG00000269058; Tissue enriched (testis).
DR   MIM; 611414; gene.
DR   neXtProt; NX_Q96L12; -.
DR   OpenTargets; ENSG00000269058; -.
DR   Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR   PharmGKB; PA134922944; -.
DR   VEuPathDB; HostDB:ENSG00000269058; -.
DR   eggNOG; KOG0674; Eukaryota.
DR   GeneTree; ENSGT00950000182915; -.
DR   HOGENOM; CLU_018224_0_0_1; -.
DR   InParanoid; Q96L12; -.
DR   OMA; DWPAPML; -.
DR   OrthoDB; 822188at2759; -.
DR   PhylomeDB; Q96L12; -.
DR   TreeFam; TF338438; -.
DR   PathwayCommons; Q96L12; -.
DR   SignaLink; Q96L12; -.
DR   BioGRID-ORCS; 125972; 19 hits in 1068 CRISPR screens.
DR   GenomeRNAi; 125972; -.
DR   Pharos; Q96L12; Tbio.
DR   PRO; PR:Q96L12; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96L12; protein.
DR   Bgee; ENSG00000269058; Expressed in right testis and 41 other tissues.
DR   ExpressionAtlas; Q96L12; baseline and differential.
DR   Genevisible; Q96L12; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009169; Calreticulin.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR11073; PTHR11073; 1.
DR   Pfam; PF00262; Calreticulin; 2.
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; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Cardiomyopathy; Chaperone; Differentiation; Disease variant;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding;
KW   Reference proteome; Repeat; Signal; Spermatogenesis; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..384
FT                   /note="Calreticulin-3"
FT                   /id="PRO_0000004178"
FT   REPEAT          191..202
FT                   /note="1-1"
FT   REPEAT          208..219
FT                   /note="1-2"
FT   REPEAT          221..230
FT                   /note="1-3"
FT   REPEAT          234..245
FT                   /note="1-4"
FT   REPEAT          249..259
FT                   /note="2-1"
FT   REPEAT          263..271
FT                   /note="2-2"
FT   REPEAT          273..283
FT                   /note="2-3"
FT   REGION          20..197
FT                   /note="N-domain"
FT   REGION          191..245
FT                   /note="4 X approximate repeats"
FT   REGION          198..294
FT                   /note="P-domain"
FT   REGION          249..283
FT                   /note="3 X approximate repeats"
FT   REGION          295..384
FT                   /note="C-domain"
FT   MOTIF           381..384
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   BINDING         109
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         111
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         128
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         135
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         303
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..137
FT                   /evidence="ECO:0000250"
FT   VARIANT         8
FT                   /note="L -> F (in dbSNP:rs11544148)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027944"
FT   VARIANT         82
FT                   /note="K -> R (found in a patient with hypertrophic
FT                   cardiomyopathy; unknown pathological significance;
FT                   dbSNP:rs142951029)"
FT                   /evidence="ECO:0000269|PubMed:17655857"
FT                   /id="VAR_065476"
FT   VARIANT         248
FT                   /note="D -> G (in dbSNP:rs10411092)"
FT                   /id="VAR_027945"
FT   VARIANT         274
FT                   /note="V -> I (in dbSNP:rs12459238)"
FT                   /id="VAR_027946"
FT   VARIANT         284
FT                   /note="D -> N (in dbSNP:rs10404156)"
FT                   /id="VAR_048589"
SQ   SEQUENCE   384 AA;  44996 MW;  32D8AFB23D1DF7C5 CRC64;
     MARALVQLWA ICMLRVALAT VYFQEEFLDG EHWRNRWLQS TNDSRFGHFR LSSGKFYGHK
     EKDKGLQTTQ NGRFYAISAR FKPFSNKGKT LVIQYTVKHE QKMDCGGGYI KVFPADIDQK
     NLNGKSQYYI MFGPDICGFD IKKVHVILHF KNKYHENKKL IRCKVDGFTH LYTLILRPDL
     SYDVKIDGQS IESGSIEYDW NLTSLKKETS PAESKDWEQT KDNKAQDWEK HFLDASTSKQ
     SDWNGDLDGD WPAPMLQKPP YQDGLKPEGI HKDVWLHRKM KNTDYLTQYD LSEFENIGAI
     GLELWQVRSG TIFDNFLITD DEEYADNFGK ATWGETKGPE REMDAIQAKE EMKKAREEEE
     EELLSGKINR HEHYFNQFHR RNEL
 
 
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