Кальретикулін (англ. Calreticulin) – білок, який кодується геном CALR, розташованим у людей на короткому плечі 19-ї хромосоми. Довжина поліпептидного ланцюга білка становить 417 амінокислот, а молекулярна маса — 48 142.
Кальретикулін | |||||||||||||||||
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Ідентифікатори | |||||||||||||||||
Символи | CALR, CRT, HEL-S-99n, RO, SSA, cC1qR, calreticulin | ||||||||||||||||
Зовнішні ІД | OMIM: 109091 MGI: 88252 HomoloGene: 37911 GeneCards: CALR | ||||||||||||||||
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Ортологи | |||||||||||||||||
Види | Людина | Миша | |||||||||||||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (мРНК) |
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RefSeq (білок) |
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Локус (UCSC) | Хр. 19: 12.94 – 12.94 Mb | Хр. 8: 85.57 – 85.57 Mb | |||||||||||||||
PubMed search | |||||||||||||||||
Вікідані | |||||||||||||||||
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10 | 20 | 30 | 40 | 50 | ||||
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MLLSVPLLLG | LLGLAVAEPA | VYFKEQFLDG | DGWTSRWIES | KHKSDFGKFV | ||||
LSSGKFYGDE | EKDKGLQTSQ | DARFYALSAS | FEPFSNKGQT | LVVQFTVKHE | ||||
QNIDCGGGYV | KLFPNSLDQT | DMHGDSEYNI | MFGPDICGPG | TKKVHVIFNY | ||||
KGKNVLINKD | IRCKDDEFTH | LYTLIVRPDN | TYEVKIDNSQ | VESGSLEDDW | ||||
DFLPPKKIKD | PDASKPEDWD | ERAKIDDPTD | SKPEDWDKPE | HIPDPDAKKP | ||||
EDWDEEMDGE | WEPPVIQNPE | YKGEWKPRQI | DNPDYKGTWI | HPEIDNPEYS | ||||
PDPSIYAYDN | FGVLGLDLWQ | VKSGTIFDNF | LITNDEAYAE | EFGNETWGVT | ||||
KAAEKQMKDK | QDEEQRLKEE | EEDKKRKEEE | EAEDKEDDED | KDEDEEDEED | ||||
KEEDEEEDVP | GQAKDEL |
Цей білок за функцією належить до шаперонів. Білок має сайт для зв'язування з іонами металів, іоном цинку, іоном кальцію, лектинами. Локалізований у цитоплазмі, позаклітинному матриксі, ендоплазматичному ретикулумі, саркоплазматичному ретикулумі. Також секретований назовні.
Література
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
- Lieu T.-S., Newkirk M.M., Capra J.D., Sontheimer R.D. (1988). Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide. J. Clin. Invest. 82: 96—101. PMID 3260607 DOI:10.1172/JCI113607
- Rojiani M.V., Finlay B.B., Gray V., Dedhar S. (1991). In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits. Biochemistry. 30: 9859—9866. PMID 1911778 DOI:10.1021/bi00105a008
- Krause K.-H., Simmerman H.K.B., Jones L.R., Campbell K.P. (1990). Sequence similarity of calreticulin with a Ca2(+)-binding protein that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60 cells. Biochem. J. 270: 545—548. PMID 2400400 DOI:10.1042/bj2700545
- Dupuis M., Schaerer E., Krause K.-H., Tschopp J. (1993). The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J. Exp. Med. 177: 1—7. PMID 8418194 DOI:10.1084/jem.177.1.1
- Nauseef W.M., McCormick S.J., Clark R.A. (1995). Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270: 4741—4747. PMID 7876246 DOI:10.1074/jbc.270.9.4741
Примітки
- Human PubMed Reference:.
- Mouse PubMed Reference:.
- (англ.) . Архів оригіналу за 31 травня 2017. Процитовано 30 січня 2017.
- (англ.) . Архів оригіналу за 1 лютого 2017. Процитовано 30 січня 2017.
Див. також
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Kalretikulin angl Calreticulin bilok yakij koduyetsya genom CALR roztashovanim u lyudej na korotkomu plechi 19 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 417 aminokislot a molekulyarna masa 48 142 KalretikulinNayavni strukturiPDBPoshuk ortologiv PDBe RCSBSpisok kodiv PDB3POW 2CLR 3DOW 3POSIdentifikatoriSimvoliCALR CRT HEL S 99n RO SSA cC1qR calreticulinZovnishni ID OMIM 109091 MGI 88252 HomoloGene 37911 GeneCards CALROntologiya genaMolekulyarna funkciya calcium ion binding protein folding chaperone activity carbohydrate binding hormone binding zv yazuvannya z ionom metalu complement component C1q complex binding mRNA binding iron ion binding unfolded protein binding zinc ion binding integrin binding DNA binding chaperone binding peptidnij zv yazok androgen receptor binding ubiquitin protein ligase binding RNA binding GO 0001948 GO 0016582 protein bindingKlitinna komponenta citoplazma gialoplazma endoplasmic reticulum lumen membrana focal adhesion extracellular region perinuclear region of cytoplasm sarcoplasmic reticulum lumen klitinne yadro endocytic vesicle lumen cell surface endoplazmatichnij retikulum ekzosoma kompleks Goldzhi vnutrishnoklitinna membranna organela GO 0005578 Pozaklitinna matricya vnutrishnoklitinnij integral component of lumenal side of endoplasmic reticulum membrane sarcoplasmic reticulum smooth endoplasmic reticulum MHC class I peptide loading complex Akrosoma external side of plasma membrane Polisoma phagocytic vesicle membrane endoplasmic reticulum Golgi intermediate compartment membrane mizhklitinnij prostir nuclear envelope GO 0009327 protein containing complex endoplasmic reticulum quality control compartment collagen containing extracellular matrixBiologichnij proces negative regulation of neuron differentiation protein folding in endoplasmic reticulum receptor oposeredkovanij endocitoz response to organic substance klitinne starinnya Spermatogenez positive regulation of dendritic cell chemotaxis regulation of apoptotic process cellular response to organic substance positive regulation of phagocytosis negative regulation of intracellular steroid hormone receptor signaling pathway GO 0009373 regulation of transcription DNA templated negative regulation of retinoic acid receptor signaling pathway cardiac muscle cell differentiation regulation of meiotic nuclear division protein maturation by protein folding positive regulation of cell cycle protein export from nucleus cellular response to lithium ion peptide antigen assembly with MHC class I protein complex antigen processing and presentation of peptide antigen via MHC class I protein stabilization cellular calcium ion homeostasis GO 1901227 negative regulation of transcription by RNA polymerase II positive regulation of DNA replication zgortannya bilkiv GO 0045996 negative regulation of transcription DNA templated GO 0033109 cortical actin cytoskeleton organization chaperone mediated protein folding response to estradiol response to testosterone ATF6 mediated unfolded protein response positive regulation of substrate adhesion dependent cell spreading sequestering of calcium ion GO 1901313 positive regulation of gene expression positive regulation of cell population proliferation protein localization to nucleus glucocorticoid receptor signaling pathway positive regulation of NIK NF kappaB signaling antigen processing and presentation of exogenous peptide antigen via MHC class I TAP dependent negative regulation of translation vesicle fusion with endoplasmic reticulum Golgi intermediate compartment ERGIC membrane positive regulation of endothelial cell migration negative regulation of trophoblast cell migrationDzherela Amigo QuickGOShablon ekspresiyiBilshe danihOrtologiVidi Lyudina MishaEntrez811 12317Ensembl ENSG00000179218 ENSMUSG00000003814UniProt P27797 P14211RefSeq mRNK NM 004343NM 007591RefSeq bilok NP 004334NP 031617Lokus UCSC Hr 19 12 94 12 94 MbHr 8 85 57 85 57 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishejPoslidovnist aminokislot1020304050MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDELA Alanin C Cisteyin D Asparaginova kislota E Glutaminova kislota F Fenilalanin G Glicin H Gistidin I Izolejcin K Lizin L Lejcin M Metionin N Asparagin P Prolin Q Glutamin R Arginin S Serin T Treonin V Valin W Triptofan Y Tirozin Cej bilok za funkciyeyu nalezhit do shaperoniv Bilok maye sajt dlya zv yazuvannya z ionami metaliv ionom cinku ionom kalciyu lektinami Lokalizovanij u citoplazmi pozaklitinnomu matriksi endoplazmatichnomu retikulumi sarkoplazmatichnomu retikulumi Takozh sekretovanij nazovni LiteraturaThe status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 2121 2127 2004 PMID 15489334 DOI 10 1101 gr 2596504 Lieu T S Newkirk M M Capra J D Sontheimer R D 1988 Molecular characterization of human Ro SS A antigen Amino terminal sequence of the protein moiety of human Ro SS A antigen and immunological activity of a corresponding synthetic peptide J Clin Invest 82 96 101 PMID 3260607 DOI 10 1172 JCI113607 Rojiani M V Finlay B B Gray V Dedhar S 1991 In vitro interaction of a polypeptide homologous to human Ro SS A antigen calreticulin with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits Biochemistry 30 9859 9866 PMID 1911778 DOI 10 1021 bi00105a008 Krause K H Simmerman H K B Jones L R Campbell K P 1990 Sequence similarity of calreticulin with a Ca2 binding protein that co purifies with an Ins 1 4 5 P3 sensitive Ca2 store in HL 60 cells Biochem J 270 545 548 PMID 2400400 DOI 10 1042 bj2700545 Dupuis M Schaerer E Krause K H Tschopp J 1993 The calcium binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes J Exp Med 177 1 7 PMID 8418194 DOI 10 1084 jem 177 1 1 Nauseef W M McCormick S J Clark R A 1995 Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase J Biol Chem 270 4741 4747 PMID 7876246 DOI 10 1074 jbc 270 9 4741PrimitkiHuman PubMed Reference Mouse PubMed Reference angl Arhiv originalu za 31 travnya 2017 Procitovano 30 sichnya 2017 angl Arhiv originalu za 1 lyutogo 2017 Procitovano 30 sichnya 2017 Div takozhHromosoma 19Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi